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Serine/threonine-protein kinase TAO3 (EC 2.7.11.1) (Cutaneous T-cell lymphoma-associated antigen HD-CL-09) (CTCL-associated antigen HD-CL-09) (Dendritic cell-derived protein kinase) (JNK/SAPK-inhibitory kinase) (Jun kinase-inhibitory kinase) (Kinase from chicken homolog A) (hKFC-A) (Thousand and one amino acid protein 3)

 TAOK3_HUMAN             Reviewed;         898 AA.
Q9H2K8; Q658N1; Q8IUM4; Q9HC79; Q9NZM9; Q9UHG7;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
25-OCT-2005, sequence version 2.
22-NOV-2017, entry version 149.
RecName: Full=Serine/threonine-protein kinase TAO3;
EC=2.7.11.1;
AltName: Full=Cutaneous T-cell lymphoma-associated antigen HD-CL-09;
Short=CTCL-associated antigen HD-CL-09;
AltName: Full=Dendritic cell-derived protein kinase;
AltName: Full=JNK/SAPK-inhibitory kinase;
AltName: Full=Jun kinase-inhibitory kinase;
AltName: Full=Kinase from chicken homolog A;
Short=hKFC-A;
AltName: Full=Thousand and one amino acid protein 3;
Name=TAOK3; Synonyms=DPK, JIK, KDS, MAP3K18;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, MUTAGENESIS OF THR-181
AND TYR-183, AND FUNCTION.
PubMed=10559204; DOI=10.1074/jbc.274.47.33287;
Tassi E., Biesova Z., Di Fiore P.P., Gutkind J.S., Wong W.T.;
"Human JIK, a novel member of the STE20 kinase family that inhibits
JNK and is negatively regulated by epidermal growth factor.";
J. Biol. Chem. 274:33287-33295(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Dendritic cell;
PubMed=10924369; DOI=10.1006/bbrc.2000.3244;
Zhang W., Chen T., Wan T., He L., Li N., Yuan Z., Cao X.;
"Cloning of DPK, a novel dendritic cell-derived protein kinase
activating the ERK1/ERK2 and JNK/SAPK pathways.";
Biochem. Biophys. Res. Commun. 274:872-879(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA], SELF-ASSOCIATION, TISSUE SPECIFICITY,
VARIANT ASN-47, AND SUBCELLULAR LOCATION.
PubMed=13679851; DOI=10.1038/sj.onc.1206605;
Yustein J.T., Xia L., Kahlenburg J.M., Robinson D., Templeton D.,
Kung H.-J.;
"Comparative studies of a new subfamily of human Ste20-like kinases:
homodimerization, subcellular localization, and selective activation
of MKK3 and p38.";
Oncogene 22:6129-6141(2003).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASN-47.
Carter T.G., Benton B., Fruhling D., Monks C.R.F., Windmiller D.,
Kupfer A., Manfredi J., Johnson G.L., Pleiman C.M.;
"KDS and TAO1, two related proteins with kinase domain homology to
STE20, differentially relocate in mitogen stimulated T lymphocytes.";
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
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.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 191-898.
TISSUE=Stomach;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 304-898.
TISSUE=T-cell lymphoma;
PubMed=14996095; DOI=10.1111/j.1365-2133.2004.05651.x;
Hartmann T.B., Thiel D., Dummer R., Schadendorf D., Eichmueller S.;
"SEREX identification of new tumour-associated antigens in cutaneous
T-cell lymphoma.";
Br. J. Dermatol. 150:252-258(2004).
[10]
INTERACTION WITH ERN1 AND TRAF2.
PubMed=11278723; DOI=10.1074/jbc.M010677200;
Yoneda T., Imaizumi K., Oono K., Yui D., Gomi F., Katayama T.,
Tohyama M.;
"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.";
J. Biol. Chem. 276:13935-13940(2001).
[11]
FUNCTION, PHOSPHORYLATION AT SER-324, INDUCTION, AND MUTAGENESIS OF
ASP-165 AND SER-324.
PubMed=17396146; DOI=10.1038/sj.emboj.7601668;
Raman M., Earnest S., Zhang K., Zhao Y., Cobb M.H.;
"TAO kinases mediate activation of p38 in response to DNA damage.";
EMBO J. 26:2005-2014(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-442, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-331, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[15]
PHOSPHORYLATION BY LRRK2.
PubMed=20949042; DOI=10.1371/journal.pone.0013191;
Zach S., Felk S., Gillardon F.;
"Signal transduction protein array analysis links LRRK2 to Ste20
kinases and PKC zeta that modulate neuronal plasticity.";
PLoS ONE 5:E13191-E13191(2010).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-331, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
VARIANTS [LARGE SCALE ANALYSIS] THR-20; ASN-47; TYR-392 AND TYR-727.
PubMed=17344846; DOI=10.1038/nature05610;
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: 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).
{ECO:0000269|PubMed:10559204, ECO:0000269|PubMed:10924369,
ECO:0000269|PubMed:17396146}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:11278723}.
-!- INTERACTION:
O75460:ERN1; NbExp=3; IntAct=EBI-1384100, EBI-371750;
Q12933:TRAF2; NbExp=2; IntAct=EBI-1384100, EBI-355744;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:13679851}.
Cell membrane {ECO:0000269|PubMed:13679851}; Peripheral membrane
protein {ECO:0000269|PubMed:13679851}. Note=Also localized to the
peripheral cell membrane.
-!- TISSUE SPECIFICITY: Ubiquitously expressed at a low level, and
highly expressed in peripheral blood leukocytes (PBLs), thymus,
spleen, kidney, skeletal muscle, heart and liver.
{ECO:0000269|PubMed:10924369, ECO:0000269|PubMed:13679851}.
-!- PTM: 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.
{ECO:0000269|PubMed:10559204, ECO:0000269|PubMed:17396146,
ECO:0000269|PubMed:20949042}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. STE20 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAN09723.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF179867; AAF14559.1; -; mRNA.
EMBL; AF135158; AAG09131.1; -; mRNA.
EMBL; AF263311; AAG38501.1; -; mRNA.
EMBL; AF181985; AAF25817.1; -; mRNA.
EMBL; BT007185; AAP35849.1; -; mRNA.
EMBL; AC026366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002756; AAH02756.1; -; mRNA.
EMBL; AL833731; CAH56239.1; -; mRNA.
EMBL; AF328731; AAN09723.1; ALT_INIT; mRNA.
CCDS; CCDS9188.1; -.
RefSeq; NP_001333417.1; NM_001346488.1.
RefSeq; NP_001333418.1; NM_001346489.1.
RefSeq; NP_057365.3; NM_016281.3.
UniGene; Hs.644420; -.
ProteinModelPortal; Q9H2K8; -.
SMR; Q9H2K8; -.
BioGrid; 119490; 9.
IntAct; Q9H2K8; 7.
MINT; MINT-5005619; -.
STRING; 9606.ENSP00000376317; -.
BindingDB; Q9H2K8; -.
ChEMBL; CHEMBL5701; -.
GuidetoPHARMACOLOGY; 2235; -.
iPTMnet; Q9H2K8; -.
PhosphoSitePlus; Q9H2K8; -.
BioMuta; TAOK3; -.
DMDM; 78099183; -.
EPD; Q9H2K8; -.
MaxQB; Q9H2K8; -.
PaxDb; Q9H2K8; -.
PeptideAtlas; Q9H2K8; -.
PRIDE; Q9H2K8; -.
DNASU; 51347; -.
Ensembl; ENST00000392533; ENSP00000376317; ENSG00000135090.
Ensembl; ENST00000419821; ENSP00000416374; ENSG00000135090.
GeneID; 51347; -.
KEGG; hsa:51347; -.
UCSC; uc001twx.4; human.
CTD; 51347; -.
DisGeNET; 51347; -.
EuPathDB; HostDB:ENSG00000135090.13; -.
GeneCards; TAOK3; -.
HGNC; HGNC:18133; TAOK3.
HPA; HPA017160; -.
MIM; 616711; gene.
neXtProt; NX_Q9H2K8; -.
OpenTargets; ENSG00000135090; -.
PharmGKB; PA134975064; -.
eggNOG; KOG0577; Eukaryota.
eggNOG; ENOG410Y259; LUCA.
GeneTree; ENSGT00900000140838; -.
HOGENOM; HOG000236358; -.
HOVERGEN; HBG088996; -.
InParanoid; Q9H2K8; -.
KO; K04429; -.
OMA; NHSIPSM; -.
OrthoDB; EOG091G01CN; -.
PhylomeDB; Q9H2K8; -.
TreeFam; TF351444; -.
SignaLink; Q9H2K8; -.
SIGNOR; Q9H2K8; -.
ChiTaRS; TAOK3; human.
GeneWiki; TAOK3; -.
GenomeRNAi; 51347; -.
PRO; PR:Q9H2K8; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000135090; -.
CleanEx; HS_TAOK3; -.
ExpressionAtlas; Q9H2K8; baseline and differential.
Genevisible; Q9H2K8; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004709; F:MAP kinase kinase kinase activity; IBA:GO_Central.
GO; GO:0004860; F:protein kinase inhibitor activity; TAS:ProtInc.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:HGNC.
GO; GO:0016740; F:transferase activity; IDA:HGNC.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0000165; P:MAPK cascade; IMP:HGNC.
GO; GO:0007095; P:mitotic G2 DNA damage checkpoint; IMP:UniProtKB.
GO; GO:0046329; P:negative regulation of JNK cascade; IDA:HGNC.
GO; GO:0007399; P:nervous system development; IBA:GO_Central.
GO; GO:0046330; P:positive regulation of JNK cascade; IMP:HGNC.
GO; GO:0043507; P:positive regulation of JUN kinase activity; IMP:UniProtKB.
GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:HGNC.
GO; GO:0006468; P:protein phosphorylation; IDA:HGNC.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Cell membrane; Coiled coil;
Complete proteome; Cytoplasm; DNA damage; DNA repair; Kinase;
Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism;
Reference proteome; Serine/threonine-protein kinase; Transferase.
CHAIN 1 898 Serine/threonine-protein kinase TAO3.
/FTId=PRO_0000086737.
DOMAIN 24 277 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 30 38 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COILED 452 502 {ECO:0000255}.
COILED 548 649 {ECO:0000255}.
COILED 754 879 {ECO:0000255}.
COMPBIAS 343 393 Ser-rich.
ACT_SITE 147 147 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 53 53 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 324 324 Phosphoserine; by ATM.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17396146}.
MOD_RES 331 331 Phosphoserine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163}.
MOD_RES 343 343 Phosphoserine.
{ECO:0000250|UniProtKB:Q53UA7}.
MOD_RES 346 346 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BYC6}.
MOD_RES 349 349 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BYC6}.
MOD_RES 357 357 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8BYC6}.
MOD_RES 359 359 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BYC6}.
MOD_RES 442 442 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 830 830 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8BYC6}.
VARIANT 20 20 P -> T (in a lung adenocarcinoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041205.
VARIANT 47 47 S -> N (in dbSNP:rs428073).
{ECO:0000269|PubMed:13679851,
ECO:0000269|PubMed:17344846,
ECO:0000269|Ref.4}.
/FTId=VAR_023691.
VARIANT 392 392 S -> Y (in a lung small cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041206.
VARIANT 727 727 C -> Y (in dbSNP:rs55857273).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041207.
MUTAGEN 165 165 D->A: Loss of serine/threonine-protein
kinase activity.
{ECO:0000269|PubMed:17396146}.
MUTAGEN 181 181 T->A: No autophosphorylation and no
kinase activity; when associated with F-
183. {ECO:0000269|PubMed:10559204}.
MUTAGEN 183 183 Y->F: No autophosphorylation and no
kinase activity; when associated with A-
181. {ECO:0000269|PubMed:10559204}.
MUTAGEN 324 324 S->A: Inhibits activation of the
p38/MAPK14 stress-activated MAPK cascade
in response to DNA damage.
{ECO:0000269|PubMed:17396146}.
CONFLICT 136 136 A -> T (in Ref. 3; AAG38501).
{ECO:0000305}.
CONFLICT 173 173 S -> P (in Ref. 3; AAG38501).
{ECO:0000305}.
CONFLICT 356 378 STGSQSSSVNSMQEVMDESSSEL -> TWNQPEQGNGQPGQ
QPFHSKHVR (in Ref. 1; AAF14559).
{ECO:0000305}.
CONFLICT 668 668 Q -> R (in Ref. 3; AAG38501).
{ECO:0000305}.
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


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