TAOK3_HUMAN
ID TAOK3_HUMAN Reviewed; 898 AA.
AC Q9H2K8; Q658N1; Q8IUM4; Q9HC79; Q9NZM9; Q9UHG7;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Serine/threonine-protein kinase TAO3;
DE EC=2.7.11.1;
DE AltName: Full=Cutaneous T-cell lymphoma-associated antigen HD-CL-09;
DE Short=CTCL-associated antigen HD-CL-09;
DE AltName: Full=Dendritic cell-derived protein kinase;
DE AltName: Full=JNK/SAPK-inhibitory kinase;
DE AltName: Full=Jun kinase-inhibitory kinase;
DE AltName: Full=Kinase from chicken homolog A;
DE Short=hKFC-A;
DE AltName: Full=Thousand and one amino acid protein 3;
GN Name=TAOK3; Synonyms=DPK, JIK, KDS, MAP3K18;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, MUTAGENESIS OF THR-181 AND
RP TYR-183, AND FUNCTION.
RX PubMed=10559204; DOI=10.1074/jbc.274.47.33287;
RA Tassi E., Biesova Z., Di Fiore P.P., Gutkind J.S., Wong W.T.;
RT "Human JIK, a novel member of the STE20 kinase family that inhibits JNK and
RT is negatively regulated by epidermal growth factor.";
RL J. Biol. Chem. 274:33287-33295(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Dendritic cell;
RX PubMed=10924369; DOI=10.1006/bbrc.2000.3244;
RA Zhang W., Chen T., Wan T., He L., Li N., Yuan Z., Cao X.;
RT "Cloning of DPK, a novel dendritic cell-derived protein kinase activating
RT the ERK1/ERK2 and JNK/SAPK pathways.";
RL Biochem. Biophys. Res. Commun. 274:872-879(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], SELF-ASSOCIATION, TISSUE SPECIFICITY, VARIANT
RP ASN-47, AND SUBCELLULAR LOCATION.
RX PubMed=13679851; DOI=10.1038/sj.onc.1206605;
RA Yustein J.T., Xia L., Kahlenburg J.M., Robinson D., Templeton D.,
RA Kung H.-J.;
RT "Comparative studies of a new subfamily of human Ste20-like kinases:
RT homodimerization, subcellular localization, and selective activation of
RT MKK3 and p38.";
RL Oncogene 22:6129-6141(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASN-47.
RA Carter T.G., Benton B., Fruhling D., Monks C.R.F., Windmiller D.,
RA Kupfer A., Manfredi J., Johnson G.L., Pleiman C.M.;
RT "KDS and TAO1, two related proteins with kinase domain homology to STE20,
RT differentially relocate in mitogen stimulated T lymphocytes.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 191-898.
RC TISSUE=Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 304-898.
RC TISSUE=T-cell lymphoma;
RX PubMed=14996095; DOI=10.1111/j.1365-2133.2004.05651.x;
RA Hartmann T.B., Thiel D., Dummer R., Schadendorf D., Eichmueller S.;
RT "SEREX identification of new tumour-associated antigens in cutaneous T-cell
RT lymphoma.";
RL Br. J. Dermatol. 150:252-258(2004).
RN [10]
RP INTERACTION WITH ERN1 AND TRAF2.
RX PubMed=11278723; DOI=10.1074/jbc.m010677200;
RA Yoneda T., Imaizumi K., Oono K., Yui D., Gomi F., Katayama T., Tohyama M.;
RT "Activation of caspase-12, an endoplastic reticulum (ER) resident caspase,
RT through tumor necrosis factor receptor-associated factor 2-dependent
RT mechanism in response to the ER stress.";
RL J. Biol. Chem. 276:13935-13940(2001).
RN [11]
RP FUNCTION, PHOSPHORYLATION AT SER-324, INDUCTION, AND MUTAGENESIS OF ASP-165
RP AND SER-324.
RX PubMed=17396146; DOI=10.1038/sj.emboj.7601668;
RA Raman M., Earnest S., Zhang K., Zhao Y., Cobb M.H.;
RT "TAO kinases mediate activation of p38 in response to DNA damage.";
RL EMBO J. 26:2005-2014(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-442, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-331, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [15]
RP PHOSPHORYLATION BY LRRK2.
RX PubMed=20949042; DOI=10.1371/journal.pone.0013191;
RA Zach S., Felk S., Gillardon F.;
RT "Signal transduction protein array analysis links LRRK2 to Ste20 kinases
RT and PKC zeta that modulate neuronal plasticity.";
RL PLoS ONE 5:E13191-E13191(2010).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-331, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP VARIANTS [LARGE SCALE ANALYSIS] THR-20; ASN-47; TYR-392 AND TYR-727.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Serine/threonine-protein kinase that acts as a regulator of
CC the p38/MAPK14 stress-activated MAPK cascade and of the MAPK8/JNK
CC cascade. Acts as an activator of the p38/MAPK14 stress-activated MAPK
CC cascade. In response to DNA damage, involved in the G2/M transition DNA
CC damage checkpoint by activating the p38/MAPK14 stress-activated MAPK
CC cascade, probably by mediating phosphorylation of upstream MAP2K3 and
CC MAP2K6 kinases. Inhibits basal activity of MAPK8/JNK cascade and
CC diminishes its activation in response epidermal growth factor (EGF).
CC {ECO:0000269|PubMed:10559204, ECO:0000269|PubMed:10924369,
CC ECO:0000269|PubMed:17396146}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Self-associates. Interacts with ERN1 and TRAF2. Interaction
CC with TRAF2 is facilitated under ER stress conditions, such as treatment
CC with tunicamycin, and may promote TRAF2 phosphorylation.
CC {ECO:0000269|PubMed:11278723}.
CC -!- INTERACTION:
CC Q9H2K8; O75460: ERN1; NbExp=3; IntAct=EBI-1384100, EBI-371750;
CC Q9H2K8; P42858: HTT; NbExp=3; IntAct=EBI-1384100, EBI-466029;
CC Q9H2K8; Q12933: TRAF2; NbExp=2; IntAct=EBI-1384100, EBI-355744;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:13679851}. Cell
CC membrane {ECO:0000269|PubMed:13679851}; Peripheral membrane protein
CC {ECO:0000269|PubMed:13679851}. Note=Also localized to the peripheral
CC cell membrane.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at a low level, and highly
CC expressed in peripheral blood leukocytes (PBLs), thymus, spleen,
CC kidney, skeletal muscle, heart and liver. {ECO:0000269|PubMed:10924369,
CC ECO:0000269|PubMed:13679851}.
CC -!- PTM: Autophosphorylated. Phosphorylation at Ser-324 by ATM following
CC DNA damage is required for activation of the p38/MAPK14 stress-
CC activated MAPK cascade. Phosphorylated by LRRK2.
CC {ECO:0000269|PubMed:10559204, ECO:0000269|PubMed:17396146,
CC ECO:0000269|PubMed:20949042}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN09723.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF179867; AAF14559.1; -; mRNA.
DR EMBL; AF135158; AAG09131.1; -; mRNA.
DR EMBL; AF263311; AAG38501.1; -; mRNA.
DR EMBL; AF181985; AAF25817.1; -; mRNA.
DR EMBL; BT007185; AAP35849.1; -; mRNA.
DR EMBL; AC026366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002756; AAH02756.1; -; mRNA.
DR EMBL; AL833731; CAH56239.1; -; mRNA.
DR EMBL; AF328731; AAN09723.1; ALT_INIT; mRNA.
DR CCDS; CCDS9188.1; -.
DR RefSeq; NP_001333417.1; NM_001346488.1.
DR RefSeq; NP_001333418.1; NM_001346489.1.
DR RefSeq; NP_057365.3; NM_016281.3.
DR PDB; 6BDN; X-ray; 1.50 A; A=1-316.
DR PDBsum; 6BDN; -.
DR AlphaFoldDB; Q9H2K8; -.
DR SMR; Q9H2K8; -.
DR BioGRID; 119490; 32.
DR IntAct; Q9H2K8; 20.
DR STRING; 9606.ENSP00000376317; -.
DR BindingDB; Q9H2K8; -.
DR ChEMBL; CHEMBL5701; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q9H2K8; -.
DR GuidetoPHARMACOLOGY; 2235; -.
DR iPTMnet; Q9H2K8; -.
DR MetOSite; Q9H2K8; -.
DR PhosphoSitePlus; Q9H2K8; -.
DR BioMuta; TAOK3; -.
DR DMDM; 78099183; -.
DR EPD; Q9H2K8; -.
DR jPOST; Q9H2K8; -.
DR MassIVE; Q9H2K8; -.
DR MaxQB; Q9H2K8; -.
DR PaxDb; Q9H2K8; -.
DR PeptideAtlas; Q9H2K8; -.
DR PRIDE; Q9H2K8; -.
DR ProteomicsDB; 80560; -.
DR Antibodypedia; 2111; 390 antibodies from 37 providers.
DR DNASU; 51347; -.
DR Ensembl; ENST00000392533.8; ENSP00000376317.3; ENSG00000135090.14.
DR Ensembl; ENST00000419821.6; ENSP00000416374.2; ENSG00000135090.14.
DR GeneID; 51347; -.
DR KEGG; hsa:51347; -.
DR MANE-Select; ENST00000392533.8; ENSP00000376317.3; NM_016281.4; NP_057365.3.
DR UCSC; uc001twx.4; human.
DR CTD; 51347; -.
DR DisGeNET; 51347; -.
DR GeneCards; TAOK3; -.
DR HGNC; HGNC:18133; TAOK3.
DR HPA; ENSG00000135090; Low tissue specificity.
DR MIM; 616711; gene.
DR neXtProt; NX_Q9H2K8; -.
DR OpenTargets; ENSG00000135090; -.
DR PharmGKB; PA134975064; -.
DR VEuPathDB; HostDB:ENSG00000135090; -.
DR eggNOG; KOG0577; Eukaryota.
DR GeneTree; ENSGT00940000155735; -.
DR HOGENOM; CLU_000288_2_2_1; -.
DR InParanoid; Q9H2K8; -.
DR OMA; KEKIKEX; -.
DR OrthoDB; 617606at2759; -.
DR PhylomeDB; Q9H2K8; -.
DR TreeFam; TF351444; -.
DR PathwayCommons; Q9H2K8; -.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR SignaLink; Q9H2K8; -.
DR SIGNOR; Q9H2K8; -.
DR BioGRID-ORCS; 51347; 9 hits in 1112 CRISPR screens.
DR ChiTaRS; TAOK3; human.
DR GeneWiki; TAOK3; -.
DR GenomeRNAi; 51347; -.
DR Pharos; Q9H2K8; Tchem.
DR PRO; PR:Q9H2K8; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9H2K8; protein.
DR Bgee; ENSG00000135090; Expressed in secondary oocyte and 212 other tissues.
DR ExpressionAtlas; Q9H2K8; baseline and differential.
DR Genevisible; Q9H2K8; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004860; F:protein kinase inhibitor activity; TAS:ProtInc.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:HGNC-UCL.
DR GO; GO:0016740; F:transferase activity; IDA:HGNC-UCL.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000165; P:MAPK cascade; IMP:HGNC-UCL.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IDA:HGNC-UCL.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP:HGNC-UCL.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IMP:UniProtKB.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:HGNC-UCL.
DR GO; GO:0006468; P:protein phosphorylation; IDA:HGNC-UCL.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cell membrane; Coiled coil;
KW Cytoplasm; DNA damage; DNA repair; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..898
FT /note="Serine/threonine-protein kinase TAO3"
FT /id="PRO_0000086737"
FT DOMAIN 24..277
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 316..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 452..502
FT /evidence="ECO:0000255"
FT COILED 548..649
FT /evidence="ECO:0000255"
FT COILED 754..879
FT /evidence="ECO:0000255"
FT COMPBIAS 338..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 30..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 324
FT /note="Phosphoserine; by ATM"
FT /evidence="ECO:0000269|PubMed:17396146,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53UA7"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BYC6"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BYC6"
FT MOD_RES 357
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BYC6"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BYC6"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 830
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BYC6"
FT VARIANT 20
FT /note="P -> T (in a lung adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041205"
FT VARIANT 47
FT /note="S -> N (in dbSNP:rs428073)"
FT /evidence="ECO:0000269|PubMed:13679851,
FT ECO:0000269|PubMed:17344846, ECO:0000269|Ref.4"
FT /id="VAR_023691"
FT VARIANT 392
FT /note="S -> Y (in a lung small cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041206"
FT VARIANT 727
FT /note="C -> Y (in dbSNP:rs55857273)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041207"
FT MUTAGEN 165
FT /note="D->A: Loss of serine/threonine-protein kinase
FT activity."
FT /evidence="ECO:0000269|PubMed:17396146"
FT MUTAGEN 181
FT /note="T->A: No autophosphorylation and no kinase activity;
FT when associated with F-183."
FT /evidence="ECO:0000269|PubMed:10559204"
FT MUTAGEN 183
FT /note="Y->F: No autophosphorylation and no kinase activity;
FT when associated with A-181."
FT /evidence="ECO:0000269|PubMed:10559204"
FT MUTAGEN 324
FT /note="S->A: Inhibits activation of the p38/MAPK14 stress-
FT activated MAPK cascade in response to DNA damage."
FT /evidence="ECO:0000269|PubMed:17396146"
FT CONFLICT 136
FT /note="A -> T (in Ref. 3; AAG38501)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="S -> P (in Ref. 3; AAG38501)"
FT /evidence="ECO:0000305"
FT CONFLICT 356..378
FT /note="STGSQSSSVNSMQEVMDESSSEL -> TWNQPEQGNGQPGQQPFHSKHVR
FT (in Ref. 1; AAF14559)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="Q -> R (in Ref. 3; AAG38501)"
FT /evidence="ECO:0000305"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:6BDN"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:6BDN"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:6BDN"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:6BDN"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:6BDN"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:6BDN"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:6BDN"
FT HELIX 62..77
FT /evidence="ECO:0007829|PDB:6BDN"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:6BDN"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:6BDN"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:6BDN"
FT HELIX 108..115
FT /evidence="ECO:0007829|PDB:6BDN"
FT HELIX 121..140
FT /evidence="ECO:0007829|PDB:6BDN"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:6BDN"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:6BDN"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:6BDN"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:6BDN"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:6BDN"
FT HELIX 187..192
FT /evidence="ECO:0007829|PDB:6BDN"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:6BDN"
FT HELIX 201..216
FT /evidence="ECO:0007829|PDB:6BDN"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:6BDN"
FT HELIX 226..235
FT /evidence="ECO:0007829|PDB:6BDN"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:6BDN"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:6BDN"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:6BDN"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:6BDN"
FT HELIX 285..298
FT /evidence="ECO:0007829|PDB:6BDN"
FT HELIX 302..308
FT /evidence="ECO:0007829|PDB:6BDN"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:6BDN"
SQ SEQUENCE 898 AA; 105406 MW; AE7E30745B09763C CRC64;
MRKGVLKDPE IADLFYKDDP EELFIGLHEI GHGSFGAVYF ATNAHTSEVV AIKKMSYSGK
QTHEKWQDIL KEVKFLRQLK HPNTIEYKGC YLKEHTAWLV MEYCLGSASD LLEVHKKPLQ
EVEIAAITHG ALHGLAYLHS HALIHRDIKA GNILLTEPGQ VKLADFGSAS MASPANSFVG
TPYWMAPEVI LAMDEGQYDG KVDIWSLGIT CIELAERKPP LFNMNAMSAL YHIAQNDSPT
LQSNEWTDSF RRFVDYCLQK IPQERPTSAE LLRHDFVRRD RPLRVLIDLI QRTKDAVREL
DNLQYRKMKK ILFQETRNGP LNESQEDEED SEHGTSLNRE MDSLGSNHSI PSMSVSTGSQ
SSSVNSMQEV MDESSSELVM MHDDESTINS SSSVVHKKDH VFIRDEAGHG DPRPEPRPTQ
SVQSQALHYR NRERFATIKS ASLVTRQIHE HEQENELREQ MSGYKRMRRQ HQKQLIALEN
KLKAEMDEHR LKLQKEVETH ANNSSIELEK LAKKQVAIIE KEAKVAAADE KKFQQQILAQ
QKKDLTTFLE SQKKQYKICK EKIKEEMNED HSTPKKEKQE RISKHKENLQ HTQAEEEAHL
LTQQRLYYDK NCRFFKRKIM IKRHEVEQQN IREELNKKRT QKEMEHAMLI RHDESTRELE
YRQLHTLQKL RMDLIRLQHQ TELENQLEYN KRRERELHRK HVMELRQQPK NLKAMEMQIK
KQFQDTCKVQ TKQYKALKNH QLEVTPKNEH KTILKTLKDE QTRKLAILAE QYEQSINEMM
ASQALRLDEA QEAECQALRL QLQQEMELLN AYQSKIKMQT EAQHERELQK LEQRVSLRRA
HLEQKIEEEL AALQKERSER IKNLLERQER EIETFDMESL RMGFGNLVTL DFPKEDYR
