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   24-JAN-2024, entry version 186.
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; 44.
DR   IntAct; Q9H2K8; 19.
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   CPTAC; CPTAC-2949; -.
DR   CPTAC; CPTAC-2950; -.
DR   EPD; Q9H2K8; -.
DR   jPOST; Q9H2K8; -.
DR   MassIVE; Q9H2K8; -.
DR   MaxQB; Q9H2K8; -.
DR   PaxDb; 9606-ENSP00000376317; -.
DR   PeptideAtlas; Q9H2K8; -.
DR   ProteomicsDB; 80560; -.
DR   Pumba; Q9H2K8; -.
DR   Antibodypedia; 2111; 421 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   AGR; HGNC:18133; -.
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; 2879376at2759; -.
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; 12 hits in 1191 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 214 other cell types or tissues.
DR   ExpressionAtlas; Q9H2K8; baseline and differential.
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:DNA damage response; IDA:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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   CDD; cd06633; STKc_TAO3; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   PANTHER; PTHR47167; SERINE/THREONINE-PROTEIN KINASE TAO1-LIKE PROTEIN; 1.
DR   PANTHER; PTHR47167:SF7; TAO KINASE 3; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   Genevisible; Q9H2K8; HS.
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
FT                   stress-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
//