Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9H2K8

- TAOK3_HUMAN

UniProt

Q9H2K8 - TAOK3_HUMAN

Protein

Serine/threonine-protein kinase TAO3

Gene

TAOK3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (25 Oct 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Serine/threonine-protein kinase that acts as a regulator of the p38/MAPK14 stress-activated MAPK cascade and of the MAPK8/JNK cascade. Acts as an activator of the p38/MAPK14 stress-activated MAPK cascade. 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. Inhibits basal activity of MAPK8/JNK cascade and diminishes its activation in response epidermal growth factor (EGF).3 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei53 – 531ATPPROSITE-ProRule annotation
    Active sitei147 – 1471Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi30 – 389ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: UniProtKB
    2. DNA repair Source: UniProtKB-KW
    3. G2 DNA damage checkpoint Source: UniProtKB
    4. MAPK cascade Source: HGNC
    5. negative regulation of JNK cascade Source: HGNC
    6. negative regulation of protein kinase activity Source: GOC
    7. positive regulation of JNK cascade Source: HGNC
    8. positive regulation of JUN kinase activity Source: UniProtKB
    9. positive regulation of stress-activated MAPK cascade Source: UniProtKB
    10. protein autophosphorylation Source: HGNC
    11. protein phosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ9H2K8.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase TAO3 (EC:2.7.11.1)
    Alternative name(s):
    Cutaneous T-cell lymphoma-associated antigen HD-CL-09
    Short name:
    CTCL-associated antigen HD-CL-09
    Dendritic cell-derived protein kinase
    JNK/SAPK-inhibitory kinase
    Jun kinase-inhibitory kinase
    Kinase from chicken homolog A
    Short name:
    hKFC-A
    Thousand and one amino acid protein 3
    Gene namesi
    Name:TAOK3
    Synonyms:DPK, JIK, KDS, MAP3K18
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:18133. TAOK3.

    Subcellular locationi

    Cytoplasm 1 Publication. Cell membrane 1 Publication; Peripheral membrane protein 1 Publication
    Note: Also localized to the peripheral cell membrane.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi165 – 1651D → A: Loss of serine/threonine-protein kinase activity. 1 Publication
    Mutagenesisi181 – 1811T → A: No autophosphorylation and no kinase activity; when associated with F-183. 1 Publication
    Mutagenesisi183 – 1831Y → F: No autophosphorylation and no kinase activity; when associated with A-181. 1 Publication
    Mutagenesisi324 – 3241S → A: Inhibits activation of the p38/MAPK14 stress-activated MAPK cascade in response to DNA damage. 1 Publication

    Organism-specific databases

    PharmGKBiPA134975064.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 898898Serine/threonine-protein kinase TAO3PRO_0000086737Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei324 – 3241Phosphoserine; by ATM6 Publications
    Modified residuei331 – 3311Phosphoserine1 Publication
    Modified residuei442 – 4421Phosphoserine1 Publication
    Modified residuei830 – 8301N6-acetyllysineBy similarity

    Post-translational modificationi

    Autophosphorylated. Phosphorylation at Ser-324 by ATM following DNA damage is required for activation of the p38/MAPK14 stress-activated MAPK cascade. Phosphorylated by LRRK2.8 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9H2K8.
    PaxDbiQ9H2K8.
    PRIDEiQ9H2K8.

    PTM databases

    PhosphoSiteiQ9H2K8.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed at a low level, and highly expressed in peripheral blood leukocytes (PBLs), thymus, spleen, kidney, skeletal muscle, heart and liver.2 Publications

    Gene expression databases

    ArrayExpressiQ9H2K8.
    BgeeiQ9H2K8.
    CleanExiHS_TAOK3.
    GenevestigatoriQ9H2K8.

    Organism-specific databases

    HPAiHPA017160.

    Interactioni

    Subunit structurei

    Self-associates. Interacts with ERN1 and TRAF2. Interaction with TRAF2 is facilitated under ER stress conditions, such as treatment with tunicamycin, and may promote TRAF2 phosphorylation.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ERN1O754603EBI-1384100,EBI-371750
    TRAF2Q129332EBI-1384100,EBI-355744

    Protein-protein interaction databases

    BioGridi119490. 8 interactions.
    IntActiQ9H2K8. 5 interactions.
    MINTiMINT-5005619.
    STRINGi9606.ENSP00000376317.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H2K8.
    SMRiQ9H2K8. Positions 8-390.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 277254Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili452 – 50251Sequence AnalysisAdd
    BLAST
    Coiled coili548 – 649102Sequence AnalysisAdd
    BLAST
    Coiled coili754 – 879126Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi343 – 39351Ser-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000236358.
    HOVERGENiHBG088996.
    InParanoidiQ9H2K8.
    KOiK04429.
    OMAiFRGFVDY.
    OrthoDBiEOG74XS5S.
    PhylomeDBiQ9H2K8.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q9H2K8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRKGVLKDPE IADLFYKDDP EELFIGLHEI GHGSFGAVYF ATNAHTSEVV    50
    AIKKMSYSGK QTHEKWQDIL KEVKFLRQLK HPNTIEYKGC YLKEHTAWLV 100
    MEYCLGSASD LLEVHKKPLQ EVEIAAITHG ALHGLAYLHS HALIHRDIKA 150
    GNILLTEPGQ VKLADFGSAS MASPANSFVG TPYWMAPEVI LAMDEGQYDG 200
    KVDIWSLGIT CIELAERKPP LFNMNAMSAL YHIAQNDSPT LQSNEWTDSF 250
    RRFVDYCLQK IPQERPTSAE LLRHDFVRRD RPLRVLIDLI QRTKDAVREL 300
    DNLQYRKMKK ILFQETRNGP LNESQEDEED SEHGTSLNRE MDSLGSNHSI 350
    PSMSVSTGSQ SSSVNSMQEV MDESSSELVM MHDDESTINS SSSVVHKKDH 400
    VFIRDEAGHG DPRPEPRPTQ SVQSQALHYR NRERFATIKS ASLVTRQIHE 450
    HEQENELREQ MSGYKRMRRQ HQKQLIALEN KLKAEMDEHR LKLQKEVETH 500
    ANNSSIELEK LAKKQVAIIE KEAKVAAADE KKFQQQILAQ QKKDLTTFLE 550
    SQKKQYKICK EKIKEEMNED HSTPKKEKQE RISKHKENLQ HTQAEEEAHL 600
    LTQQRLYYDK NCRFFKRKIM IKRHEVEQQN IREELNKKRT QKEMEHAMLI 650
    RHDESTRELE YRQLHTLQKL RMDLIRLQHQ TELENQLEYN KRRERELHRK 700
    HVMELRQQPK NLKAMEMQIK KQFQDTCKVQ TKQYKALKNH QLEVTPKNEH 750
    KTILKTLKDE QTRKLAILAE QYEQSINEMM ASQALRLDEA QEAECQALRL 800
    QLQQEMELLN AYQSKIKMQT EAQHERELQK LEQRVSLRRA HLEQKIEEEL 850
    AALQKERSER IKNLLERQER EIETFDMESL RMGFGNLVTL DFPKEDYR 898
    Length:898
    Mass (Da):105,406
    Last modified:October 25, 2005 - v2
    Checksum:iAE7E30745B09763C
    GO

    Sequence cautioni

    The sequence AAN09723.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti136 – 1361A → T in AAG38501. (PubMed:13679851)Curated
    Sequence conflicti173 – 1731S → P in AAG38501. (PubMed:13679851)Curated
    Sequence conflicti356 – 37823STGSQ…SSSEL → TWNQPEQGNGQPGQQPFHSK HVR in AAF14559. (PubMed:10559204)CuratedAdd
    BLAST
    Sequence conflicti668 – 6681Q → R in AAG38501. (PubMed:13679851)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti20 – 201P → T in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_041205
    Natural varianti47 – 471S → N.3 Publications
    Corresponds to variant rs428073 [ dbSNP | Ensembl ].
    VAR_023691
    Natural varianti392 – 3921S → Y in a lung small cell carcinoma sample; somatic mutation. 1 Publication
    VAR_041206
    Natural varianti727 – 7271C → Y.1 Publication
    Corresponds to variant rs55857273 [ dbSNP | Ensembl ].
    VAR_041207

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF179867 mRNA. Translation: AAF14559.1.
    AF135158 mRNA. Translation: AAG09131.1.
    AF263311 mRNA. Translation: AAG38501.1.
    AF181985 mRNA. Translation: AAF25817.1.
    BT007185 mRNA. Translation: AAP35849.1.
    AC026366 Genomic DNA. No translation available.
    BC002756 mRNA. Translation: AAH02756.1.
    AL833731 mRNA. Translation: CAH56239.1.
    AF328731 mRNA. Translation: AAN09723.1. Different initiation.
    CCDSiCCDS9188.1.
    RefSeqiNP_057365.3. NM_016281.3.
    UniGeneiHs.644420.

    Genome annotation databases

    EnsembliENST00000392533; ENSP00000376317; ENSG00000135090.
    ENST00000419821; ENSP00000416374; ENSG00000135090.
    GeneIDi51347.
    KEGGihsa:51347.
    UCSCiuc001tww.3. human.

    Polymorphism databases

    DMDMi78099183.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF179867 mRNA. Translation: AAF14559.1 .
    AF135158 mRNA. Translation: AAG09131.1 .
    AF263311 mRNA. Translation: AAG38501.1 .
    AF181985 mRNA. Translation: AAF25817.1 .
    BT007185 mRNA. Translation: AAP35849.1 .
    AC026366 Genomic DNA. No translation available.
    BC002756 mRNA. Translation: AAH02756.1 .
    AL833731 mRNA. Translation: CAH56239.1 .
    AF328731 mRNA. Translation: AAN09723.1 . Different initiation.
    CCDSi CCDS9188.1.
    RefSeqi NP_057365.3. NM_016281.3.
    UniGenei Hs.644420.

    3D structure databases

    ProteinModelPortali Q9H2K8.
    SMRi Q9H2K8. Positions 8-390.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119490. 8 interactions.
    IntActi Q9H2K8. 5 interactions.
    MINTi MINT-5005619.
    STRINGi 9606.ENSP00000376317.

    Chemistry

    BindingDBi Q9H2K8.
    ChEMBLi CHEMBL5701.
    GuidetoPHARMACOLOGYi 2235.

    PTM databases

    PhosphoSitei Q9H2K8.

    Polymorphism databases

    DMDMi 78099183.

    Proteomic databases

    MaxQBi Q9H2K8.
    PaxDbi Q9H2K8.
    PRIDEi Q9H2K8.

    Protocols and materials databases

    DNASUi 51347.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000392533 ; ENSP00000376317 ; ENSG00000135090 .
    ENST00000419821 ; ENSP00000416374 ; ENSG00000135090 .
    GeneIDi 51347.
    KEGGi hsa:51347.
    UCSCi uc001tww.3. human.

    Organism-specific databases

    CTDi 51347.
    GeneCardsi GC12M118587.
    HGNCi HGNC:18133. TAOK3.
    HPAi HPA017160.
    neXtProti NX_Q9H2K8.
    PharmGKBi PA134975064.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000236358.
    HOVERGENi HBG088996.
    InParanoidi Q9H2K8.
    KOi K04429.
    OMAi FRGFVDY.
    OrthoDBi EOG74XS5S.
    PhylomeDBi Q9H2K8.
    TreeFami TF351444.

    Enzyme and pathway databases

    SignaLinki Q9H2K8.

    Miscellaneous databases

    ChiTaRSi TAOK3. human.
    GeneWikii TAOK3.
    GenomeRNAii 51347.
    NextBioi 54794.
    PROi Q9H2K8.

    Gene expression databases

    ArrayExpressi Q9H2K8.
    Bgeei Q9H2K8.
    CleanExi HS_TAOK3.
    Genevestigatori Q9H2K8.

    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. "Human JIK, a novel member of the STE20 kinase family that inhibits JNK and is negatively regulated by epidermal growth factor."
      Tassi E., Biesova Z., Di Fiore P.P., Gutkind J.S., Wong W.T.
      J. Biol. Chem. 274:33287-33295(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, MUTAGENESIS OF THR-181 AND TYR-183, FUNCTION.
    2. "Cloning of DPK, a novel dendritic cell-derived protein kinase activating the ERK1/ERK2 and JNK/SAPK pathways."
      Zhang W., Chen T., Wan T., He L., Li N., Yuan Z., Cao X.
      Biochem. Biophys. Res. Commun. 274:872-879(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: Dendritic cell.
    3. "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], SELF-ASSOCIATION, TISSUE SPECIFICITY, VARIANT ASN-47, SUBCELLULAR LOCATION.
    4. "KDS and TAO1, two related proteins with kinase domain homology to STE20, differentially relocate in mitogen stimulated T lymphocytes."
      Carter T.G., Benton B., Fruhling D., Monks C.R.F., Windmiller D., Kupfer A., Manfredi J., Johnson G.L., Pleiman C.M.
      Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASN-47.
    5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      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].
      Tissue: Placenta.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 191-898.
      Tissue: Stomach.
    9. "SEREX identification of new tumour-associated antigens in cutaneous T-cell lymphoma."
      Hartmann T.B., Thiel D., Dummer R., Schadendorf D., Eichmueller S.
      Br. J. Dermatol. 150:252-258(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 304-898.
      Tissue: T-cell lymphoma.
    10. "Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress."
      Yoneda T., Imaizumi K., Oono K., Yui D., Gomi F., Katayama T., Tohyama M.
      J. Biol. Chem. 276:13935-13940(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ERN1 AND TRAF2.
    11. "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 AT SER-324, INDUCTION, MUTAGENESIS OF ASP-165 AND SER-324.
    12. "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-324, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-331, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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.
    16. "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-324, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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-324, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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] THR-20; ASN-47; TYR-392 AND TYR-727.

    Entry informationi

    Entry nameiTAOK3_HUMAN
    AccessioniPrimary (citable) accession number: Q9H2K8
    Secondary accession number(s): Q658N1
    , Q8IUM4, Q9HC79, Q9NZM9, Q9UHG7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2005
    Last sequence update: October 25, 2005
    Last modified: October 1, 2014
    This is version 118 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 12
      Human chromosome 12: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3