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Serine/threonine-protein kinase TAO2 (EC 2.7.11.1) (Kinase from chicken homolog C) (hKFC-C) (Prostate-derived sterile 20-like kinase 1) (PSK-1) (PSK1) (Prostate-derived STE20-like kinase 1) (Thousand and one amino acid protein kinase 2)

 TAOK2_HUMAN             Reviewed;        1235 AA.
Q9UL54; A5PKY1; A7MCZ2; B2RN35; B7ZM88; O94957; Q6UW73; Q7LC09;
Q9NSW2;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
27-SEP-2017, entry version 154.
RecName: Full=Serine/threonine-protein kinase TAO2;
EC=2.7.11.1;
AltName: Full=Kinase from chicken homolog C;
Short=hKFC-C;
AltName: Full=Prostate-derived sterile 20-like kinase 1;
Short=PSK-1;
Short=PSK1;
Short=Prostate-derived STE20-like kinase 1;
AltName: Full=Thousand and one amino acid protein kinase 2;
Name=TAOK2; Synonyms=KIAA0881, MAP3K17, PSK, PSK1;
ORFNames=UNQ2971/PRO7431;
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 MUTAGENESIS OF LYS-57.
TISSUE=Mammary carcinoma;
PubMed=10660600; DOI=10.1074/jbc.275.6.4311;
Moore T.M., Garg R., Johnson C., Coptcoat M.J., Ridley A.J.,
Morris J.D.H.;
"PSK, a novel STE20-like kinase derived from prostatic carcinoma that
activates the JNK MAPK pathway and regulates actin cytoskeletal
organisation.";
J. Biol. Chem. 275:4311-4322(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SELF-ASSOCIATION,
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=10048485; DOI=10.1093/dnares/5.6.355;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 5:355-364(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Fetal brain;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Testis;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[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; 2 AND 4).
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 957-1235 (ISOFORMS 1/3).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[10]
FUNCTION IN PHOSPHORYLATION OF MAP2K3 AND MAP2K6, AND INTERACTION WITH
MAP2K3 AND MAP2K6.
PubMed=11279118; DOI=10.1074/jbc.M100681200;
Chen Z., Cobb M.H.;
"Regulation of stress-responsive mitogen-activated protein (MAP)
kinase pathways by TAO2.";
J. Biol. Chem. 276:16070-16075(2001).
[11]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TUBULINS, AND
MUTAGENESIS OF LYS-57.
PubMed=12639963; DOI=10.1074/jbc.M213064200;
Mitsopoulos C., Zihni C., Garg R., Ridley A.J., Morris J.D.;
"The prostate-derived sterile 20-like kinase (PSK) regulates
microtubule organization and stability.";
J. Biol. Chem. 278:18085-18091(2003).
[12]
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).
[13]
FUNCTION, INTERACTION WITH MAP3K7, AND MUTAGENESIS OF LYS-57 AND
ASP-169.
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).
[14]
FUNCTION, PHOSPHORYLATION BY ATM, AND INDUCTION.
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]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-181,
AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LYS-57 AND ASP-919.
PubMed=17158878; DOI=10.1074/jbc.M608336200;
Zihni C., Mitsopoulos C., Tavares I.A., Baum B., Ridley A.J.,
Morris J.D.;
"Prostate-derived sterile 20-like kinase 1-alpha induces apoptosis.
JNK-and caspase-dependent nuclear localization is a requirement for
membrane blebbing.";
J. Biol. Chem. 282:6484-6493(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-777, 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).
[17]
ENZYME REGULATION.
PubMed=19226137; DOI=10.1021/jm8005806;
Anand R., Maksimoska J., Pagano N., Wong E.Y., Gimotty P.A.,
Diamond S.L., Meggers E., Marmorstein R.;
"Toward the development of a potent and selective organoruthenium
mammalian sterile 20 kinase inhibitor.";
J. Med. Chem. 52:1602-1611(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-181,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1011 (ISOFORM 2), 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).
[19]
ENZYME REGULATION.
PubMed=20159944; DOI=10.1124/mol.109.061507;
McNeer J.L., Goussetis D.J., Sassano A., Dolniak B., Kroczynska B.,
Glaser H., Altman J.K., Platanias L.C.;
"Arsenic trioxide-dependent activation of thousand-and-one amino acid
kinase 2 and transforming growth factor-beta-activated kinase 1.";
Mol. Pharmacol. 77:828-835(2010).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-825 AND SER-827, 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).
[21]
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).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-827, 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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, AND 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).
-!- FUNCTION: Serine/threonine-protein kinase involved in different
processes such as membrane blebbing and apoptotic bodies formation
DNA damage response and MAPK14/p38 MAPK stress-activated MAPK
cascade. Phosphorylates itself, MBP, activated MAPK8, MAP2K3,
MAP2K6 and tubulins. Activates the MAPK14/p38 MAPK signaling
pathway through the specific activation and phosphorylation of the
upstream MAP2K3 and MAP2K6 kinases. 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. Isoform 1, but not isoform 2, plays a role in apoptotic
morphological changes, including cell contraction, membrane
blebbing and apoptotic bodies formation. This function, which
requires the activation of MAPK8/JNK and nuclear localization of
C-terminally truncated isoform 1, may be linked to the
mitochondrial CASP9-associated death pathway. Isoform 1 binds to
microtubules and affects their organization and stability
independently of its kinase activity. Prevents MAP3K7-mediated
activation of CHUK, and thus NF-kappa-B activation, but not that
of MAPK8/JNK. May play a role in the osmotic stress-MAPK8 pathway.
Isoform 2, but not isoform 1, is required for PCDH8 endocytosis.
Following homophilic interactions between PCDH8 extracellular
domains, isoform 2 phosphorylates and activates MAPK14/p38 MAPK
which in turn phosphorylates isoform 2. This process leads to
PCDH8 endocytosis and CDH2 cointernalization. Both isoforms are
involved in MAPK14 phosphorylation. {ECO:0000269|PubMed:10660600,
ECO:0000269|PubMed:11279118, ECO:0000269|PubMed:12639963,
ECO:0000269|PubMed:12665513, ECO:0000269|PubMed:13679851,
ECO:0000269|PubMed:16893890, ECO:0000269|PubMed:17158878,
ECO:0000269|PubMed:17396146}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Selectively inhibited by the enantiopure
organoruthenium inhibitor 9E1. Activated following arsenic
trioxide (As(2)O(3)) treatment. {ECO:0000269|PubMed:19226137,
ECO:0000269|PubMed:20159944}.
-!- SUBUNIT: Interacts with MAP2K3 and MAP2K6 (By similarity). Self-
associates. Interacts with tubulins through the C-terminal domain.
Interacts with MAP3K7 and interfers with MAP3K7-binding to CHUK
and thus prevents NF-kappa-B activation. Isoform 2 interacts with
PCDH8; this complex may also include CDH2 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000305};
Multi-pass membrane protein {ECO:0000305}. Cytoplasm,
cytoskeleton. Nucleus. Note=Catalytically active full-length
phosphorylated isoform 1 localizes to microtubules in the
cytoplasm predominantly on microtubule cables positioned around
the nucleus. A C-terminally truncated form of isoform 1 is present
in the nucleus; isoform 2 and kinase-defective, as well as full-
length isoform 1 are excluded from the nucleus.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell projection, dendrite.
Note=In dendrites, colocalizes with PCDH8. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=PSK1-alpha, TAO2;
IsoId=Q9UL54-1; Sequence=Displayed;
Name=2; Synonyms=PSK1-beta;
IsoId=Q9UL54-2; Sequence=VSP_015969, VSP_015970;
Note=Contains a phosphoserine at position 1031 (By similarity).
Contains a phosphoserine at position 1011.
{ECO:0000244|PubMed:19369195, ECO:0000250};
Name=3;
IsoId=Q9UL54-3; Sequence=VSP_015967, VSP_015968;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q9UL54-4; Sequence=VSP_044894;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed, with a higher level of
expression in testis and brain. {ECO:0000269|PubMed:10660600,
ECO:0000269|PubMed:13679851}.
-!- PTM: Isoforms 1 and 2 are autophosphorylated.
-!- PTM: C-terminal cleavage of isoform 1 and subsequent nuclear
localization requires CASP9 activity.
-!- PTM: Autophosphorylated. Phosphorylated by ATM.
-!- PTM: Isoform 2: Phosphorylated on Ser-1031 by MAPK14. This
phosphorylation is required PCDH8 for endocytosis (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. STE20 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAQ89301.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA74904.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF061943; AAD45616.1; -; mRNA.
EMBL; AF263313; AAG38503.1; -; mRNA.
EMBL; AB020688; BAA74904.2; ALT_INIT; mRNA.
EMBL; AK291473; BAF84162.1; -; mRNA.
EMBL; AL137701; CAB70882.1; -; mRNA.
EMBL; AC093512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471238; EAW79963.1; -; Genomic_DNA.
EMBL; CH471238; EAW79964.1; -; Genomic_DNA.
EMBL; BC136653; AAI36654.1; -; mRNA.
EMBL; BC136655; AAI36656.1; -; mRNA.
EMBL; BC142663; AAI42664.1; -; mRNA.
EMBL; BC144344; AAI44345.1; -; mRNA.
EMBL; BC151221; AAI51222.1; -; mRNA.
EMBL; BC152413; AAI52414.1; -; mRNA.
EMBL; AY358942; AAQ89301.1; ALT_INIT; mRNA.
CCDS; CCDS10662.1; -. [Q9UL54-2]
CCDS; CCDS10663.1; -. [Q9UL54-1]
CCDS; CCDS58448.1; -. [Q9UL54-4]
PIR; T46444; T46444.
RefSeq; NP_001238972.1; NM_001252043.1. [Q9UL54-4]
RefSeq; NP_004774.1; NM_004783.3. [Q9UL54-2]
RefSeq; NP_057235.2; NM_016151.3. [Q9UL54-1]
UniGene; Hs.291623; -.
ProteinModelPortal; Q9UL54; -.
SMR; Q9UL54; -.
BioGrid; 114750; 19.
IntAct; Q9UL54; 10.
STRING; 9606.ENSP00000310094; -.
BindingDB; Q9UL54; -.
ChEMBL; CHEMBL1075195; -.
DrugBank; DB04522; Phosphonoserine.
GuidetoPHARMACOLOGY; 2234; -.
iPTMnet; Q9UL54; -.
PhosphoSitePlus; Q9UL54; -.
BioMuta; TAOK2; -.
DMDM; 116242813; -.
EPD; Q9UL54; -.
PaxDb; Q9UL54; -.
PeptideAtlas; Q9UL54; -.
PRIDE; Q9UL54; -.
Ensembl; ENST00000279394; ENSP00000279394; ENSG00000149930. [Q9UL54-2]
Ensembl; ENST00000308893; ENSP00000310094; ENSG00000149930. [Q9UL54-1]
Ensembl; ENST00000416441; ENSP00000393048; ENSG00000149930. [Q9UL54-3]
Ensembl; ENST00000543033; ENSP00000440336; ENSG00000149930. [Q9UL54-4]
GeneID; 9344; -.
KEGG; hsa:9344; -.
UCSC; uc002dva.3; human. [Q9UL54-1]
CTD; 9344; -.
DisGeNET; 9344; -.
EuPathDB; HostDB:ENSG00000149930.17; -.
GeneCards; TAOK2; -.
HGNC; HGNC:16835; TAOK2.
HPA; HPA010650; -.
MIM; 613199; gene.
neXtProt; NX_Q9UL54; -.
OpenTargets; ENSG00000149930; -.
PharmGKB; PA134907964; -.
eggNOG; KOG0577; Eukaryota.
eggNOG; ENOG410Y259; LUCA.
GeneTree; ENSGT00880000137869; -.
HOGENOM; HOG000236358; -.
HOVERGEN; HBG094024; -.
InParanoid; Q9UL54; -.
KO; K04429; -.
OMA; LRDHTAW; -.
OrthoDB; EOG091G01CN; -.
PhylomeDB; Q9UL54; -.
TreeFam; TF351444; -.
SignaLink; Q9UL54; -.
SIGNOR; Q9UL54; -.
GeneWiki; TAOK2; -.
GenomeRNAi; 9344; -.
PRO; PR:Q9UL54; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000149930; -.
CleanEx; HS_TAOK2; -.
Genevisible; Q9UL54; HS.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004709; F:MAP kinase kinase kinase activity; IBA:GO_Central.
GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
GO; GO:0000186; P:activation of MAPKK activity; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
GO; GO:0016477; P:cell migration; NAS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0048041; P:focal adhesion assembly; 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:0006612; P:protein targeting to membrane; NAS:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0001558; P:regulation of cell growth; NAS:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IDA:UniProtKB.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0006950; P:response to stress; IDA:UniProtKB.
GO; GO:0051403; P:stress-activated MAPK cascade; IDA:UniProtKB.
InterPro; IPR011009; Kinase-like_dom.
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; ATP-binding; Cell projection; Coiled coil;
Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
Kinase; Magnesium; Membrane; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 1235 Serine/threonine-protein kinase TAO2.
/FTId=PRO_0000086733.
TRANSMEM 965 985 Helical. {ECO:0000255}.
TRANSMEM 987 1007 Helical. {ECO:0000255}.
TRANSMEM 1012 1032 Helical. {ECO:0000255}.
TRANSMEM 1043 1063 Helical. {ECO:0000255}.
TRANSMEM 1166 1186 Helical. {ECO:0000255}.
DOMAIN 28 281 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 34 42 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COILED 486 547 {ECO:0000255}.
COILED 574 601 {ECO:0000255}.
COILED 681 713 {ECO:0000255}.
COMPBIAS 330 336 Poly-Glu.
COMPBIAS 347 370 Ser-rich.
COMPBIAS 378 406 Glu-rich.
COMPBIAS 791 907 Glu-rich.
COMPBIAS 943 1060 Leu-rich.
ACT_SITE 151 151 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 57 57 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 9 9 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163}.
MOD_RES 181 181 Phosphoserine.
{ECO:0000244|PubMed:19369195,
ECO:0000269|PubMed:17158878}.
MOD_RES 414 414 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 656 656 Phosphoserine.
{ECO:0000250|UniProtKB:Q6ZQ29}.
MOD_RES 777 777 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 825 825 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 827 827 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 173 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_015967.
VAR_SEQ 174 218 SIMAPANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSLGIT
CIEL -> MMGTSQGHVARKSRNWGLNPSRLSSIPLSSTPC
HLSPSSLSPFSV (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_015968.
VAR_SEQ 745 1049 VRAGQRPPGLPLPIPGALGPPNTGTPIEQQPCSPGQEAVLD
QRMLGEEEEAVGERRILGKEGATLEPKQQRILGEESGAPSP
SPQKHGSLVDEEVWGLPEEIEELRVPSLVPQERSIVGQEEA
GTWSLWGKEDESLLDEEFELGWVQGPALTPVPEEEEEEEEG
APIGTPRDPGDGCPSPDIPPEPPPTHLRPCPASQLPGLLSH
GLLAGLSFAVGSSSGLLPLLLLLLLPLLAAQGGGGLQAALL
ALEVGLVGLGASYLLLCTALHLPSSLFLLLAQGTALGAVLG
LSWRRGLMGVPLGLGAAW -> SKELQIKKQFQETCKIQTR
QYKALRAHLLETTPKAQHKSLLKRLKEEQTRKLAILAEQYD
QSISEMLSSQALRLDETQEAEFQALRQQLQQELELLNAYQS
KIKIRTESQHERELRELEQRVALRRALLEQRVEEELLALQT
GRSERIRSLLERQAREIEAFDAESMRLGFSSMALGGIPAEA
AAQGYPAPPPAPAWPSRPVPRSGAHWSHGPPPPGMPPPAWR
QPSLLAPPGPPNWLGPPTQSGTPRGGALLLLRNSPQPLRRA
ASGGSGSENVGPPAAAVPGPLSRSTSVASHILNGSSHFYS
(in isoform 2).
{ECO:0000303|PubMed:10048485,
ECO:0000303|PubMed:13679851,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_015969.
VAR_SEQ 745 857 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_044894.
VAR_SEQ 1050 1235 Missing (in isoform 2).
{ECO:0000303|PubMed:10048485,
ECO:0000303|PubMed:13679851,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_015970.
MUTAGEN 57 57 K->A: Loss of kinase activity. In isoform
1, excluded from the nucleus. No effect
on microtubule-binding.
{ECO:0000269|PubMed:10660600,
ECO:0000269|PubMed:12639963,
ECO:0000269|PubMed:16893890,
ECO:0000269|PubMed:17158878}.
MUTAGEN 169 169 D->A: Loss of kinase activity; No effect
on MAP3K7-mediated activation of NF-
kappa-B. {ECO:0000269|PubMed:16893890}.
MUTAGEN 919 919 D->N: No effect on kinase activity, nor
on JNK activation, but severe reduction
in nuclear localization and apoptotic
membrane blebbing.
{ECO:0000269|PubMed:17158878}.
CONFLICT 189 189 M -> T (in Ref. 7; AAI51222/AAI42664).
{ECO:0000305}.
CONFLICT 1211 1211 R -> H (in Ref. 1; AAD45616).
{ECO:0000305}.
SEQUENCE 1235 AA; 138251 MW; 211852E690934307 CRC64;
MPAGGRAGSL KDPDVAELFF KDDPEKLFSD LREIGHGSFG AVYFARDVRN SEVVAIKKMS
YSGKQSNEKW QDIIKEVRFL QKLRHPNTIQ YRGCYLREHT AWLVMEYCLG SASDLLEVHK
KPLQEVEIAA VTHGALQGLA YLHSHNMIHR DVKAGNILLS EPGLVKLGDF GSASIMAPAN
SFVGTPYWMA PEVILAMDEG QYDGKVDVWS LGITCIELAE RKPPLFNMNA MSALYHIAQN
ESPVLQSGHW SEYFRNFVDS CLQKIPQDRP TSEVLLKHRF VLRERPPTVI MDLIQRTKDA
VRELDNLQYR KMKKILFQEA PNGPGAEAPE EEEEAEPYMH RAGTLTSLES SHSVPSMSIS
ASSQSSSVNS LADASDNEEE EEEEEEEEEE EEGPEAREMA MMQEGEHTVT SHSSIIHRLP
GSDNLYDDPY QPEITPSPLQ PPAAPAPTST TSSARRRAYC RNRDHFATIR TASLVSRQIQ
EHEQDSALRE QLSGYKRMRR QHQKQLLALE SRLRGEREEH SARLQRELEA QRAGFGAEAE
KLARRHQAIG EKEARAAQAE ERKFQQHILG QQKKELAALL EAQKRTYKLR KEQLKEELQE
NPSTPKREKA EWLLRQKEQL QQCQAEEEAG LLRRQRQYFE LQCRQYKRKM LLARHSLDQD
LLREDLNKKQ TQKDLECALL LRQHEATREL ELRQLQAVQR TRAELTRLQH QTELGNQLEY
NKRREQELRQ KHAAQVRQQP KSLKVRAGQR PPGLPLPIPG ALGPPNTGTP IEQQPCSPGQ
EAVLDQRMLG EEEEAVGERR ILGKEGATLE PKQQRILGEE SGAPSPSPQK HGSLVDEEVW
GLPEEIEELR VPSLVPQERS IVGQEEAGTW SLWGKEDESL LDEEFELGWV QGPALTPVPE
EEEEEEEGAP IGTPRDPGDG CPSPDIPPEP PPTHLRPCPA SQLPGLLSHG LLAGLSFAVG
SSSGLLPLLL LLLLPLLAAQ GGGGLQAALL ALEVGLVGLG ASYLLLCTAL HLPSSLFLLL
AQGTALGAVL GLSWRRGLMG VPLGLGAAWL LAWPGLALPL VAMAAGGRWV RQQGPRVRRG
ISRLWLRVLL RLSPMAFRAL QGCGAVGDRG LFALYPKTNK DGFRSRLPVP GPRRRNPRTT
QHPLALLARV WVLCKGWNWR LARASQGLAS HLPPWAIHTL ASWGLLRGER PTRIPRLLPR
SQRQLGPPAS RQPLPGTLAG RRSRTRQSRA LPPWR


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