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Q7L7X3

- TAOK1_HUMAN

UniProt

Q7L7X3 - TAOK1_HUMAN

Protein

Serine/threonine-protein kinase TAO1

Gene

TAOK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Serine/threonine-protein kinase involved in various processes such as p38/MAPK14 stress-activated MAPK cascade, DNA damage response and regulation of cytoskeleton stability. Phosphorylates MAP2K3, MAP2K6 and MARK2. Acts as an activator of the p38/MAPK14 stress-activated MAPK cascade by mediating phosphorylation and subsequent activation of the upstream MAP2K3 and MAP2K6 kinases. Involved in G-protein coupled receptor signaling to p38/MAPK14. 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 MAP2K3 and MAP2K6. Acts as a regulator of cytoskeleton stability by phosphorylating 'Thr-208' of MARK2, leading to activate MARK2 kinase activity and subsequent phosphorylation and detachment of MAPT/TAU from microtubules. Also acts as a regulator of apoptosis: regulates apoptotic morphological changes, including cell contraction, membrane blebbing and apoptotic bodies formation via activation of the MAPK8/JNK cascade.5 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Serine/threonine-protein kinase activity is inhibited by SPRED1.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei57 – 571ATPCurated
    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: HGNC
    2. kinase activity Source: HGNC
    3. protein binding Source: WormBase
    4. protein kinase activity Source: HGNC
    5. protein serine/threonine kinase activity Source: UniProtKB
    6. transferase activity Source: HGNC

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: UniProtKB
    2. DNA repair Source: UniProtKB-KW
    3. execution phase of apoptosis Source: UniProtKB
    4. G2 DNA damage checkpoint Source: UniProtKB
    5. mitotic cell cycle Source: Reactome
    6. positive regulation of JNK cascade Source: UniProtKB
    7. positive regulation of stress-activated MAPK cascade Source: UniProtKB
    8. protein phosphorylation Source: HGNC
    9. regulation of cytoskeleton organization Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, DNA damage, DNA repair

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_682. Mitotic Prometaphase.
    SignaLinkiQ7L7X3.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase TAO1 (EC:2.7.11.1)
    Alternative name(s):
    Kinase from chicken homolog B
    Short name:
    hKFC-B
    MARK Kinase
    Short name:
    MARKK
    Prostate-derived sterile 20-like kinase 2
    Short name:
    PSK-2
    Short name:
    PSK2
    Short name:
    Prostate-derived STE20-like kinase 2
    Thousand and one amino acid protein kinase 1
    Short name:
    TAOK1
    Short name:
    hTAOK1
    Gene namesi
    Name:TAOK1
    Synonyms:KIAA1361, MAP3K16, MARKK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:29259. TAOK1.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi57 – 571K → A: Abolishes kinase activity, ability to activate the MAPK8/JNK cascade and cleavage by caspase-3 (CASP3). 1 Publication
    Mutagenesisi169 – 1691D → A: Loss of serine/threonine-protein kinase activity. 1 Publication
    Mutagenesisi376 – 3761D → N: Does not abolish cleavage by caspase-3 (CASP3). 1 Publication
    Mutagenesisi643 – 6431T → A: Abolishes phosphorylation by ATM; when associated with A-785 and A-990. 1 Publication
    Mutagenesisi785 – 7851T → A: Abolishes phosphorylation by ATM; when associated with A-643 and A-990. 1 Publication
    Mutagenesisi990 – 9901S → A: Abolishes phosphorylation by ATM; when associated with A-643 and A-785. 1 Publication

    Organism-specific databases

    PharmGKBiPA134872946.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10011001Serine/threonine-protein kinase TAO1PRO_0000086728Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei9 – 91Phosphoserine2 Publications
    Modified residuei421 – 4211Phosphoserine7 Publications
    Modified residuei445 – 4451Phosphoserine1 Publication
    Modified residuei669 – 6691Phosphothreonine1 Publication
    Modified residuei965 – 9651Phosphoserine1 Publication

    Post-translational modificationi

    Proteolytically processed by caspase-3 (CASP3).1 Publication
    Autophosphorylated By similarity. Phosphorylated by ATM in response to DNA damage. Phosphorylated by LRRK2.By similarity9 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ7L7X3.
    PaxDbiQ7L7X3.
    PeptideAtlasiQ7L7X3.
    PRIDEiQ7L7X3.

    PTM databases

    PhosphoSiteiQ7L7X3.

    Expressioni

    Tissue specificityi

    Highly expressed in the testis, and to a lower extent also expressed in brain, placenta, colon and skeletal muscle.2 Publications

    Inductioni

    In response to DNA damage.1 Publication

    Gene expression databases

    ArrayExpressiQ7L7X3.
    BgeeiQ7L7X3.
    CleanExiHS_TAOK1.
    GenevestigatoriQ7L7X3.

    Organism-specific databases

    HPAiHPA007669.

    Interactioni

    Subunit structurei

    Self-associates. Interacts with MAP2K3 By similarity. Interacts with SPRED1 and TESK1. Interacts with MAP3K7.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi121607. 11 interactions.
    DIPiDIP-39709N.
    IntActiQ7L7X3. 9 interactions.
    MINTiMINT-5006389.
    STRINGi9606.ENSP00000261716.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7L7X3.
    SMRiQ7L7X3. Positions 12-320.
    ModBaseiSearch...
    MobiDBiSearch...

    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 coili458 – 651194Sequence AnalysisAdd
    BLAST
    Coiled coili754 – 877124Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi330 – 3345Poly-Glu
    Compositional biasi347 – 37933Ser-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000236358.
    HOVERGENiHBG088996.
    InParanoidiQ7L7X3.
    KOiK04429.
    OMAiAGPHWGH.
    OrthoDBiEOG74XS5S.
    PhylomeDBiQ7L7X3.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q7L7X3-1) [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

    MPSTNRAGSL KDPEIAELFF KEDPEKLFTD LREIGHGSFG AVYFARDVRT     50
    NEVVAIKKMS YSGKQSTEKW QDIIKEVKFL QRIKHPNSIE YKGCYLREHT 100
    AWLVMEYCLG SASDLLEVHK KPLQEVEIAA ITHGALQGLA YLHSHTMIHR 150
    DIKAGNILLT EPGQVKLADF GSASMASPAN SFVGTPYWMA PEVILAMDEG 200
    QYDGKVDVWS LGITCIELAE RKPPLFNMNA MSALYHIAQN ESPTLQSNEW 250
    SDYFRNFVDS CLQKIPQDRP TSEELLKHIF VLRERPETVL IDLIQRTKDA 300
    VRELDNLQYR KMKKLLFQEA HNGPAVEAQE EEEEQDHGVG RTGTVNSVGS 350
    NQSIPSMSIS ASSQSSSVNS LPDVSDDKSE LDMMEGDHTV MSNSSVIHLK 400
    PEEENYREEG DPRTRASDPQ SPPQVSRHKS HYRNREHFAT IRTASLVTRQ 450
    MQEHEQDSEL REQMSGYKRM RRQHQKQLMT LENKLKAEMD EHRLRLDKDL 500
    ETQRNNFAAE MEKLIKKHQA AMEKEAKVMS NEEKKFQQHI QAQQKKELNS 550
    FLESQKREYK LRKEQLKEEL NENQSTPKKE KQEWLSKQKE NIQHFQAEEE 600
    ANLLRRQRQY LELECRRFKR RMLLGRHNLE QDLVREELNK RQTQKDLEHA 650
    MLLRQHESMQ ELEFRHLNTI QKMRCELIRL QHQTELTNQL EYNKRREREL 700
    RRKHVMEVRQ QPKSLKSKEL QIKKQFQDTC KIQTRQYKAL RNHLLETTPK 750
    SEHKAVLKRL KEEQTRKLAI LAEQYDHSIN EMLSTQALRL DEAQEAECQV 800
    LKMQLQQELE LLNAYQSKIK MQAEAQHDRE LRELEQRVSL RRALLEQKIE 850
    EEMLALQNER TERIRSLLER QAREIEAFDS ESMRLGFSNM VLSNLSPEAF 900
    SHSYPGASGW SHNPTGGPGP HWGHPMGGPP QAWGHPMQGG PQPWGHPSGP 950
    MQGVPRGSSM GVRNSPQALR RTASGGRTEQ GMSRSTSVTS QISNGSHMSY 1000
    T 1001
    Length:1,001
    Mass (Da):116,070
    Last modified:July 5, 2004 - v1
    Checksum:i82941DEAEADC7651
    GO
    Isoform 2 (identifier: Q7L7X3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-174: Missing.
         569-572: ELNE → VLMS
         573-1001: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:398
    Mass (Da):46,163
    Checksum:iB2744BCA14C7E63F
    GO
    Isoform 3 (identifier: Q7L7X3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         569-716: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:853
    Mass (Da):97,526
    Checksum:i15DE595D707B9E34
    GO

    Sequence cautioni

    The sequence BAA92599.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti251 – 2511S → T in BAB14901. (PubMed:14702039)Curated
    Sequence conflicti257 – 2571F → S in AAG38502. (PubMed:13679851)Curated
    Sequence conflicti860 – 8601R → C in AAG38502. (PubMed:13679851)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti855 – 8551A → T.1 Publication
    Corresponds to variant rs34151057 [ dbSNP | Ensembl ].
    VAR_041204

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 174174Missing in isoform 2. 1 PublicationVSP_015964Add
    BLAST
    Alternative sequencei569 – 716148Missing in isoform 3. 1 PublicationVSP_043706Add
    BLAST
    Alternative sequencei569 – 5724ELNE → VLMS in isoform 2. 1 PublicationVSP_015965
    Alternative sequencei573 – 1001429Missing in isoform 2. 1 PublicationVSP_015966Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF263312 mRNA. Translation: AAG38502.1.
    AY049015 mRNA. Translation: AAL12217.1.
    CQ834802 mRNA. Translation: CAH05616.1.
    AB037782 mRNA. Translation: BAA92599.1. Different initiation.
    AK024376 mRNA. Translation: BAB14901.1.
    AC068025 Genomic DNA. No translation available.
    AC068588 Genomic DNA. No translation available.
    AC090698 Genomic DNA. No translation available.
    CH471159 Genomic DNA. Translation: EAW51188.1.
    BC133039 mRNA. Translation: AAI33040.1.
    BC144067 mRNA. Translation: AAI44068.1.
    CCDSiCCDS32601.1. [Q7L7X3-1]
    CCDS56024.1. [Q7L7X3-3]
    RefSeqiNP_065842.1. NM_020791.2. [Q7L7X3-1]
    NP_079418.1. NM_025142.1. [Q7L7X3-3]
    UniGeneiHs.597434.
    Hs.735869.

    Genome annotation databases

    EnsembliENST00000261716; ENSP00000261716; ENSG00000160551. [Q7L7X3-1]
    ENST00000536202; ENSP00000438819; ENSG00000160551. [Q7L7X3-3]
    GeneIDi57551.
    KEGGihsa:57551.
    UCSCiuc002hdz.2. human. [Q7L7X3-1]
    uc002heb.1. human. [Q7L7X3-2]
    uc010wbe.2. human. [Q7L7X3-3]

    Polymorphism databases

    DMDMi74759012.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF263312 mRNA. Translation: AAG38502.1 .
    AY049015 mRNA. Translation: AAL12217.1 .
    CQ834802 mRNA. Translation: CAH05616.1 .
    AB037782 mRNA. Translation: BAA92599.1 . Different initiation.
    AK024376 mRNA. Translation: BAB14901.1 .
    AC068025 Genomic DNA. No translation available.
    AC068588 Genomic DNA. No translation available.
    AC090698 Genomic DNA. No translation available.
    CH471159 Genomic DNA. Translation: EAW51188.1 .
    BC133039 mRNA. Translation: AAI33040.1 .
    BC144067 mRNA. Translation: AAI44068.1 .
    CCDSi CCDS32601.1. [Q7L7X3-1 ]
    CCDS56024.1. [Q7L7X3-3 ]
    RefSeqi NP_065842.1. NM_020791.2. [Q7L7X3-1 ]
    NP_079418.1. NM_025142.1. [Q7L7X3-3 ]
    UniGenei Hs.597434.
    Hs.735869.

    3D structure databases

    ProteinModelPortali Q7L7X3.
    SMRi Q7L7X3. Positions 12-320.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121607. 11 interactions.
    DIPi DIP-39709N.
    IntActi Q7L7X3. 9 interactions.
    MINTi MINT-5006389.
    STRINGi 9606.ENSP00000261716.

    Chemistry

    BindingDBi Q7L7X3.
    ChEMBLi CHEMBL5261.
    GuidetoPHARMACOLOGYi 2233.

    PTM databases

    PhosphoSitei Q7L7X3.

    Polymorphism databases

    DMDMi 74759012.

    Proteomic databases

    MaxQBi Q7L7X3.
    PaxDbi Q7L7X3.
    PeptideAtlasi Q7L7X3.
    PRIDEi Q7L7X3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261716 ; ENSP00000261716 ; ENSG00000160551 . [Q7L7X3-1 ]
    ENST00000536202 ; ENSP00000438819 ; ENSG00000160551 . [Q7L7X3-3 ]
    GeneIDi 57551.
    KEGGi hsa:57551.
    UCSCi uc002hdz.2. human. [Q7L7X3-1 ]
    uc002heb.1. human. [Q7L7X3-2 ]
    uc010wbe.2. human. [Q7L7X3-3 ]

    Organism-specific databases

    CTDi 57551.
    GeneCardsi GC17P027717.
    HGNCi HGNC:29259. TAOK1.
    HPAi HPA007669.
    MIMi 610266. gene.
    neXtProti NX_Q7L7X3.
    PharmGKBi PA134872946.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000236358.
    HOVERGENi HBG088996.
    InParanoidi Q7L7X3.
    KOi K04429.
    OMAi AGPHWGH.
    OrthoDBi EOG74XS5S.
    PhylomeDBi Q7L7X3.
    TreeFami TF351444.

    Enzyme and pathway databases

    Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_682. Mitotic Prometaphase.
    SignaLinki Q7L7X3.

    Miscellaneous databases

    ChiTaRSi TAOK1. human.
    GeneWikii TAOK1.
    GenomeRNAii 57551.
    NextBioi 64014.
    PROi Q7L7X3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7L7X3.
    Bgeei Q7L7X3.
    CleanExi HS_TAOK1.
    Genevestigatori Q7L7X3.

    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. "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 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    2. "Characterization of human TAO1."
      Jenkins S.G., D'Andrea R.J., Gamble J.R., Vadas M.A.
      Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    5. "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: Placenta.
    6. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [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 AND 3).
      Tissue: Brain.
    9. "Isolation of TAO1, a protein kinase that activates MEKs in stress-activated protein kinase cascades."
      Hutchison M., Berman K.S., Cobb M.H.
      J. Biol. Chem. 273:28625-28632(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    10. "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.
    11. "Prostate-derived sterile 20-like kinase 2 (PSK2) regulates apoptotic morphology via C-Jun N-terminal kinase and Rho kinase-1."
      Zihni C., Mitsopoulos C., Tavares I.A., Ridley A.J., Morris J.D.
      J. Biol. Chem. 281:7317-7323(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PROTEOLYTIC PROCESSING, MUTAGENESIS OF LYS-57 AND ASP-376.
    12. "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: INTERACTION WITH MAP3K7.
    13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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, MUTAGENESIS OF ASP-169; THR-643; THR-785 AND SER-990.
    15. "A functional genomic screen identifies a role for TAO1 kinase in spindle-checkpoint signalling."
      Draviam V.M., Stegmeier F., Nalepa G., Sowa M.E., Chen J., Liang A., Hannon G.J., Sorger P.K., Harper J.W., Elledge S.J.
      Nat. Cell Biol. 9:556-564(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: POSSIBLE ROLE IN SPINDLE CHECKPOINT.
    16. "Human TAO kinase 1 induces apoptosis in SH-SY5Y cells."
      Wu M.F., Wang S.G.
      Cell Biol. Int. 32:151-156(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND SER-965, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    18. "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-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND SER-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-421 AND THR-669, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "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-9 AND SER-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    23. "Re-examination of siRNA specificity questions role of PICH and Tao1 in the spindle checkpoint and identifies Mad2 as a sensitive target for small RNAs."
      Hubner N.C., Wang L.H., Kaulich M., Descombes P., Poser I., Nigg E.A.
      Chromosoma 119:149-165(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: LACK OF ROLE IN SPINDLE CHECKPOINT.
    24. "Re-evaluating the role of Tao1 in the spindle checkpoint."
      Westhorpe F.G., Diez M.A., Gurden M.D., Tighe A., Taylor S.S.
      Chromosoma 119:371-379(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: LACK OF ROLE IN SPINDLE CHECKPOINT.
    25. "Signal transduction protein array analysis links LRRK2 to Ste20 kinases and PKC zeta that modulate neuronal plasticity."
      Zach S., Felk S., Gillardon F.
      PLoS ONE 5:E13191-E13191(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY LRRK2.
    26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "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-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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: VARIANT [LARGE SCALE ANALYSIS] THR-855.

    Entry informationi

    Entry nameiTAOK1_HUMAN
    AccessioniPrimary (citable) accession number: Q7L7X3
    Secondary accession number(s): A2RUT8
    , B7ZLV6, Q96L75, Q9H2K7, Q9H7S5, Q9P2I6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2005
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 110 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3