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Serine/threonine-protein kinase TAO1 (EC 2.7.11.1) (Kinase from chicken homolog B) (hKFC-B) (MARK Kinase) (MARKK) (Prostate-derived sterile 20-like kinase 2) (PSK-2) (PSK2) (Prostate-derived STE20-like kinase 2) (Thousand and one amino acid protein kinase 1) (TAOK1) (hTAOK1)

 TAOK1_HUMAN             Reviewed;        1001 AA.
Q7L7X3; A2RUT8; B7ZLV6; Q96L75; Q9H2K7; Q9H7S5; Q9P2I6;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
22-NOV-2017, entry version 138.
RecName: Full=Serine/threonine-protein kinase TAO1;
EC=2.7.11.1;
AltName: Full=Kinase from chicken homolog B;
Short=hKFC-B;
AltName: Full=MARK Kinase;
Short=MARKK;
AltName: Full=Prostate-derived sterile 20-like kinase 2;
Short=PSK-2;
Short=PSK2;
Short=Prostate-derived STE20-like kinase 2;
AltName: Full=Thousand and one amino acid protein kinase 1;
Short=TAOK1;
Short=hTAOK1;
Name=TAOK1; Synonyms=KIAA1361, MAP3K16, MARKK;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Jenkins S.G., D'Andrea R.J., Gamble J.R., Vadas M.A.;
"Characterization of human TAO1.";
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Matsuda A., Yoneta S.;
"T cell activating gene.";
Patent number WO2004058805, 15-JUL-2004.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10718198; DOI=10.1093/dnares/7.1.65;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVI.
The complete sequences of 150 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:65-73(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Brain;
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).
[9]
TISSUE SPECIFICITY.
PubMed=9786855; DOI=10.1074/jbc.273.44.28625;
Hutchison M., Berman K.S., Cobb M.H.;
"Isolation of TAO1, a protein kinase that activates MEKs in stress-
activated protein kinase cascades.";
J. Biol. Chem. 273:28625-28632(1998).
[10]
FUNCTION.
PubMed=12665513; DOI=10.1074/jbc.M301173200;
Chen Z., Raman M., Chen L., Lee S.F., Gilman A.G., Cobb M.H.;
"TAO (thousand-and-one amino acid) protein kinases mediate signaling
from carbachol to p38 mitogen-activated protein kinase and ternary
complex factors.";
J. Biol. Chem. 278:22278-22283(2003).
[11]
FUNCTION, PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF LYS-57 AND
ASP-376.
PubMed=16407310; DOI=10.1074/jbc.M513769200;
Zihni C., Mitsopoulos C., Tavares I.A., Ridley A.J., Morris J.D.;
"Prostate-derived sterile 20-like kinase 2 (PSK2) regulates apoptotic
morphology via C-Jun N-terminal kinase and Rho kinase-1.";
J. Biol. Chem. 281:7317-7323(2006).
[12]
INTERACTION WITH MAP3K7.
PubMed=16893890; DOI=10.1074/jbc.M603627200;
Huangfu W.C., Omori E., Akira S., Matsumoto K., Ninomiya-Tsuji J.;
"Osmotic stress activates the TAK1-JNK pathway while blocking TAK1-
mediated NF-kappaB activation: TAO2 regulates TAK1 pathways.";
J. Biol. Chem. 281:28802-28810(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[14]
FUNCTION, PHOSPHORYLATION BY ATM, INDUCTION, AND MUTAGENESIS OF
ASP-169; THR-643; THR-785 AND SER-990.
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).
[15]
POSSIBLE ROLE IN SPINDLE CHECKPOINT.
PubMed=17417629; DOI=10.1038/ncb1569;
Draviam V.M., Stegmeier F., Nalepa G., Sowa M.E., Chen J., Liang A.,
Hannon G.J., Sorger P.K., Harper J.W., Elledge S.J.;
"A functional genomic screen identifies a role for TAO1 kinase in
spindle-checkpoint signalling.";
Nat. Cell Biol. 9:556-564(2007).
[16]
FUNCTION.
PubMed=17900936; DOI=10.1016/j.cellbi.2007.08.006;
Wu M.F., Wang S.G.;
"Human TAO kinase 1 induces apoptosis in SH-SY5Y cells.";
Cell Biol. Int. 32:151-156(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND SER-965, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, 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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND SER-445, 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).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-421 AND THR-669,
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).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-421, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[23]
LACK OF ROLE IN SPINDLE CHECKPOINT.
PubMed=19904549; DOI=10.1007/s00412-009-0244-2;
Hubner N.C., Wang L.H., Kaulich M., Descombes P., Poser I., Nigg E.A.;
"Re-examination of siRNA specificity questions role of PICH and Tao1
in the spindle checkpoint and identifies Mad2 as a sensitive target
for small RNAs.";
Chromosoma 119:149-165(2010).
[24]
LACK OF ROLE IN SPINDLE CHECKPOINT.
PubMed=20162290; DOI=10.1007/s00412-010-0261-1;
Westhorpe F.G., Diez M.A., Gurden M.D., Tighe A., Taylor S.S.;
"Re-evaluating the role of Tao1 in the spindle checkpoint.";
Chromosoma 119:371-379(2010).
[25]
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).
[26]
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).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, 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).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-421; SER-445 AND
SER-965, 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).
[29]
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).
[30]
VARIANT [LARGE SCALE ANALYSIS] THR-855.
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 involved in various
processes such as p38/MAPK14 stress-activated MAPK cascade, DNA
damage response and regulation of cytoskeleton stability.
Phosphorylates MAP2K3, MAP2K6 and MARK2. Acts as an activator of
the p38/MAPK14 stress-activated MAPK cascade by mediating
phosphorylation and subsequent activation of the upstream MAP2K3
and MAP2K6 kinases. Involved in G-protein coupled receptor
signaling to p38/MAPK14. In response to DNA damage, involved in
the G2/M transition DNA damage checkpoint by activating the
p38/MAPK14 stress-activated MAPK cascade, probably by mediating
phosphorylation of MAP2K3 and MAP2K6. Acts as a regulator of
cytoskeleton stability by phosphorylating 'Thr-208' of MARK2,
leading to activate MARK2 kinase activity and subsequent
phosphorylation and detachment of MAPT/TAU from microtubules. Also
acts as a regulator of apoptosis: regulates apoptotic
morphological changes, including cell contraction, membrane
blebbing and apoptotic bodies formation via activation of the
MAPK8/JNK cascade. {ECO:0000269|PubMed:12665513,
ECO:0000269|PubMed:13679851, ECO:0000269|PubMed:16407310,
ECO:0000269|PubMed:17396146, ECO:0000269|PubMed:17900936}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Serine/threonine-protein kinase activity is
inhibited by SPRED1.
-!- SUBUNIT: Self-associates. Interacts with MAP2K3 (By similarity).
Interacts with SPRED1 and TESK1. Interacts with MAP3K7.
{ECO:0000250, ECO:0000269|PubMed:16893890}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:13679851}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q7L7X3-1; Sequence=Displayed;
Name=2;
IsoId=Q7L7X3-2; Sequence=VSP_015964, VSP_015965, VSP_015966;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q7L7X3-3; Sequence=VSP_043706;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in the testis, and to a lower
extent also expressed in brain, placenta, colon and skeletal
muscle. {ECO:0000269|PubMed:13679851, ECO:0000269|PubMed:9786855}.
-!- INDUCTION: In response to DNA damage.
{ECO:0000269|PubMed:17396146}.
-!- PTM: Proteolytically processed by caspase-3 (CASP3).
{ECO:0000269|PubMed:16407310}.
-!- PTM: Autophosphorylated (By similarity). Phosphorylated by ATM in
response to DNA damage. Phosphorylated by LRRK2. {ECO:0000250,
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}.
-!- CAUTION: Was initially thought to play a role in the spindle
checkpoint (PubMed:17417629). However, it was later shown that it
is not the case and that phenotypes initially observed are the
cause of the siRNA used that has an off-target effect resulting in
MAD2L1 inhibition (PubMed:19904549 and PubMed:20162290).
{ECO:0000305|PubMed:17417629}.
-!- SEQUENCE CAUTION:
Sequence=BAA92599.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF263312; AAG38502.1; -; mRNA.
EMBL; AY049015; AAL12217.1; -; mRNA.
EMBL; CQ834802; CAH05616.1; -; mRNA.
EMBL; AB037782; BAA92599.1; ALT_INIT; mRNA.
EMBL; AK024376; BAB14901.1; -; mRNA.
EMBL; AC068025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC068588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC090698; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471159; EAW51188.1; -; Genomic_DNA.
EMBL; BC133039; AAI33040.1; -; mRNA.
EMBL; BC144067; AAI44068.1; -; mRNA.
CCDS; CCDS32601.1; -. [Q7L7X3-1]
CCDS; CCDS56024.1; -. [Q7L7X3-3]
RefSeq; NP_065842.1; NM_020791.2. [Q7L7X3-1]
RefSeq; NP_079418.1; NM_025142.1. [Q7L7X3-3]
RefSeq; XP_011523362.1; XM_011525060.2. [Q7L7X3-1]
UniGene; Hs.597434; -.
UniGene; Hs.735869; -.
ProteinModelPortal; Q7L7X3; -.
SMR; Q7L7X3; -.
BioGrid; 121607; 14.
DIP; DIP-39709N; -.
IntAct; Q7L7X3; 11.
MINT; MINT-5006389; -.
STRING; 9606.ENSP00000261716; -.
BindingDB; Q7L7X3; -.
ChEMBL; CHEMBL5261; -.
GuidetoPHARMACOLOGY; 2233; -.
iPTMnet; Q7L7X3; -.
PhosphoSitePlus; Q7L7X3; -.
BioMuta; TAOK1; -.
DMDM; 74759012; -.
EPD; Q7L7X3; -.
MaxQB; Q7L7X3; -.
PaxDb; Q7L7X3; -.
PeptideAtlas; Q7L7X3; -.
PRIDE; Q7L7X3; -.
Ensembl; ENST00000261716; ENSP00000261716; ENSG00000160551. [Q7L7X3-1]
Ensembl; ENST00000536202; ENSP00000438819; ENSG00000160551. [Q7L7X3-3]
GeneID; 57551; -.
KEGG; hsa:57551; -.
UCSC; uc002hdz.3; human. [Q7L7X3-1]
CTD; 57551; -.
DisGeNET; 57551; -.
EuPathDB; HostDB:ENSG00000160551.9; -.
GeneCards; TAOK1; -.
HGNC; HGNC:29259; TAOK1.
HPA; HPA007669; -.
MIM; 610266; gene.
neXtProt; NX_Q7L7X3; -.
OpenTargets; ENSG00000160551; -.
PharmGKB; PA134872946; -.
eggNOG; KOG0577; Eukaryota.
eggNOG; ENOG410Y259; LUCA.
GeneTree; ENSGT00900000140838; -.
HOGENOM; HOG000236358; -.
HOVERGEN; HBG088996; -.
InParanoid; Q7L7X3; -.
KO; K04429; -.
OMA; PQAMRRT; -.
OrthoDB; EOG091G01CN; -.
PhylomeDB; Q7L7X3; -.
TreeFam; TF351444; -.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-68877; Mitotic Prometaphase.
SignaLink; Q7L7X3; -.
SIGNOR; Q7L7X3; -.
ChiTaRS; TAOK1; human.
GeneWiki; TAOK1; -.
GenomeRNAi; 57551; -.
PRO; PR:Q7L7X3; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000160551; -.
CleanEx; HS_TAOK1; -.
ExpressionAtlas; Q7L7X3; baseline and differential.
Genevisible; Q7L7X3; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; NAS:HGNC.
GO; GO:0016301; F:kinase activity; NAS:HGNC.
GO; GO:0004709; F:MAP kinase kinase kinase activity; IBA:GO_Central.
GO; GO:0004672; F:protein kinase activity; NAS:HGNC.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0016740; F:transferase activity; NAS:HGNC.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0097194; P:execution phase of apoptosis; IDA:UniProtKB.
GO; GO:0031572; P:G2 DNA damage checkpoint; IMP:UniProtKB.
GO; GO:0007399; P:nervous system development; IBA:GO_Central.
GO; GO:0046330; P:positive regulation of JNK cascade; IDA:UniProtKB.
GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; NAS:HGNC.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0051493; P:regulation of cytoskeleton organization; ISS:UniProtKB.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0007062; P:sister chromatid cohesion; TAS:Reactome.
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;
Alternative splicing; Apoptosis; ATP-binding; Coiled coil;
Complete proteome; Cytoplasm; DNA damage; DNA repair; Kinase;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 1001 Serine/threonine-protein kinase TAO1.
/FTId=PRO_0000086728.
DOMAIN 28 281 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 34 42 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COILED 458 651 {ECO:0000255}.
COILED 754 877 {ECO:0000255}.
COMPBIAS 330 334 Poly-Glu.
COMPBIAS 347 379 Ser-rich.
ACT_SITE 151 151 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 57 57 ATP. {ECO:0000305}.
MOD_RES 9 9 Phosphoserine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 421 421 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 445 445 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 669 669 Phosphothreonine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 965 965 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 174 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_015964.
VAR_SEQ 569 716 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043706.
VAR_SEQ 569 572 ELNE -> VLMS (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_015965.
VAR_SEQ 573 1001 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_015966.
VARIANT 855 855 A -> T (in dbSNP:rs34151057).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041204.
MUTAGEN 57 57 K->A: Abolishes kinase activity, ability
to activate the MAPK8/JNK cascade and
cleavage by caspase-3 (CASP3).
{ECO:0000269|PubMed:16407310}.
MUTAGEN 169 169 D->A: Loss of serine/threonine-protein
kinase activity.
{ECO:0000269|PubMed:17396146}.
MUTAGEN 376 376 D->N: Does not abolish cleavage by
caspase-3 (CASP3).
{ECO:0000269|PubMed:16407310}.
MUTAGEN 643 643 T->A: Abolishes phosphorylation by ATM;
when associated with A-785 and A-990.
{ECO:0000269|PubMed:17396146}.
MUTAGEN 785 785 T->A: Abolishes phosphorylation by ATM;
when associated with A-643 and A-990.
{ECO:0000269|PubMed:17396146}.
MUTAGEN 990 990 S->A: Abolishes phosphorylation by ATM;
when associated with A-643 and A-785.
{ECO:0000269|PubMed:17396146}.
CONFLICT 251 251 S -> T (in Ref. 5; BAB14901).
{ECO:0000305}.
CONFLICT 257 257 F -> S (in Ref. 1; AAG38502).
{ECO:0000305}.
CONFLICT 860 860 R -> C (in Ref. 1; AAG38502).
{ECO:0000305}.
SEQUENCE 1001 AA; 116070 MW; 82941DEAEADC7651 CRC64;
MPSTNRAGSL KDPEIAELFF KEDPEKLFTD LREIGHGSFG AVYFARDVRT NEVVAIKKMS
YSGKQSTEKW QDIIKEVKFL QRIKHPNSIE YKGCYLREHT AWLVMEYCLG SASDLLEVHK
KPLQEVEIAA ITHGALQGLA YLHSHTMIHR DIKAGNILLT EPGQVKLADF GSASMASPAN
SFVGTPYWMA PEVILAMDEG QYDGKVDVWS LGITCIELAE RKPPLFNMNA MSALYHIAQN
ESPTLQSNEW SDYFRNFVDS CLQKIPQDRP TSEELLKHIF VLRERPETVL IDLIQRTKDA
VRELDNLQYR KMKKLLFQEA HNGPAVEAQE EEEEQDHGVG RTGTVNSVGS NQSIPSMSIS
ASSQSSSVNS LPDVSDDKSE LDMMEGDHTV MSNSSVIHLK PEEENYREEG DPRTRASDPQ
SPPQVSRHKS HYRNREHFAT IRTASLVTRQ MQEHEQDSEL REQMSGYKRM RRQHQKQLMT
LENKLKAEMD EHRLRLDKDL ETQRNNFAAE MEKLIKKHQA AMEKEAKVMS NEEKKFQQHI
QAQQKKELNS FLESQKREYK LRKEQLKEEL NENQSTPKKE KQEWLSKQKE NIQHFQAEEE
ANLLRRQRQY LELECRRFKR RMLLGRHNLE QDLVREELNK RQTQKDLEHA MLLRQHESMQ
ELEFRHLNTI QKMRCELIRL QHQTELTNQL EYNKRREREL RRKHVMEVRQ QPKSLKSKEL
QIKKQFQDTC KIQTRQYKAL RNHLLETTPK SEHKAVLKRL KEEQTRKLAI LAEQYDHSIN
EMLSTQALRL DEAQEAECQV LKMQLQQELE LLNAYQSKIK MQAEAQHDRE LRELEQRVSL
RRALLEQKIE EEMLALQNER TERIRSLLER QAREIEAFDS ESMRLGFSNM VLSNLSPEAF
SHSYPGASGW SHNPTGGPGP HWGHPMGGPP QAWGHPMQGG PQPWGHPSGP MQGVPRGSSM
GVRNSPQALR RTASGGRTEQ GMSRSTSVTS QISNGSHMSY T


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