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Death-associated protein kinase 3 (DAP kinase 3) (EC 2.7.11.1) (DAP-like kinase) (Dlk) (MYPT1 kinase) (Zipper-interacting protein kinase) (ZIP-kinase)

 DAPK3_HUMAN             Reviewed;         454 AA.
O43293; A0AVN4; B3KQE2; Q05JY4;
28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
22-NOV-2017, entry version 170.
RecName: Full=Death-associated protein kinase 3;
Short=DAP kinase 3;
EC=2.7.11.1 {ECO:0000269|PubMed:10356987, ECO:0000269|PubMed:11384979, ECO:0000269|PubMed:11781833, ECO:0000269|PubMed:15096528, ECO:0000269|PubMed:17126281, ECO:0000269|PubMed:18995835};
AltName: Full=DAP-like kinase;
Short=Dlk;
AltName: Full=MYPT1 kinase;
AltName: Full=Zipper-interacting protein kinase;
Short=ZIP-kinase;
Name=DAPK3; Synonyms=ZIPK;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9488481; DOI=10.1128/MCB.18.3.1642;
Kawai T., Matsumoto M., Takeda K., Sanjo H., Akira S.;
"ZIP kinase, a novel serine/threonine kinase which mediates
apoptosis.";
Mol. Cell. Biol. 18:1642-1651(1998).
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
COFACTOR.
TISSUE=Cervix carcinoma;
PubMed=10356987; DOI=10.1016/S0014-5793(99)00550-5;
Murata-Hori M., Suizu F., Iwasaki T., Kikuchi A., Hosoya H.;
"ZIP kinase identified as a novel myosin regulatory light chain kinase
in HeLa cells.";
FEBS Lett. 451:81-84(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 165-454 (ISOFORM 2), ALTERNATIVE
SPLICING, FUNCTION IN PHOSPHORYLATION OF MYOSIN; PPP1R12A AND MYL12B,
CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL
PROPERTIES, INTERACTION WITH PPP1R12A AND MYOSIN, AUTOPHOSPHORYLATION,
AND TISSUE SPECIFICITY.
TISSUE=Urinary bladder;
PubMed=17126281; DOI=10.1016/j.abb.2006.09.026;
Takamoto N., Komatsu S., Komaba S., Niiro N., Ikebe M.;
"Novel ZIP kinase isoform lacks leucine zipper.";
Arch. Biochem. Biophys. 456:194-203(2006).
[6]
FUNCTION IN PHOSPHORYLATION OF MUSCLE MYL12B, AND CATALYTIC ACTIVITY.
PubMed=11384979; DOI=10.1074/jbc.M102753200;
Niiro N., Ikebe M.;
"Zipper-interacting protein kinase induces Ca(2+)-free smooth muscle
contraction via myosin light chain phosphorylation.";
J. Biol. Chem. 276:29567-29574(2001).
[7]
FUNCTION IN PHOSPHORYLATION OF NON-MUSCLE MYL12B, AND CATALYTIC
ACTIVITY.
PubMed=11781833; DOI=10.1038/sj.onc.1205055;
Murata-Hori M., Fukuta Y., Ueda K., Iwasaki T., Hosoya H.;
"HeLa ZIP kinase induces diphosphorylation of myosin II regulatory
light chain and reorganization of actin filaments in nonmuscle
cells.";
Oncogene 20:8175-8183(2001).
[8] {ECO:0000305}
FUNCTION IN APOPTOSIS, AND INTERACTION WITH DAXX AND PAWR.
PubMed=12917339; DOI=10.1128/MCB.23.17.6174-6186.2003;
Kawai T., Akira S., Reed J.C.;
"ZIP kinase triggers apoptosis from nuclear PML oncogenic domains.";
Mol. Cell. Biol. 23:6174-6186(2003).
[9]
INTERACTION WITH PPP1R12A, AND TISSUE SPECIFICITY.
PubMed=15292222; DOI=10.1074/jbc.M403676200;
Endo A., Surks H.K., Mochizuki S., Mochizuki N., Mendelsohn M.E.;
"Identification and characterization of zipper-interacting protein
kinase as the unique vascular smooth muscle myosin phosphatase-
associated kinase.";
J. Biol. Chem. 279:42055-42061(2004).
[10]
FUNCTION IN PHOSPHORYLATION OF MYL12B, AND CATALYTIC ACTIVITY.
PubMed=15096528; DOI=10.1083/jcb.200309056;
Komatsu S., Ikebe M.;
"ZIP kinase is responsible for the phosphorylation of myosin II and
necessary for cell motility in mammalian fibroblasts.";
J. Cell Biol. 165:243-254(2004).
[11]
FUNCTION, PHOSPHORYLATION AT THR-299; SER-309; SER-311; SER-312;
SER-318 AND SER-326, PHOSPHORYLATION BY DAPK1, AND SUBCELLULAR
LOCATION.
PubMed=15367680; DOI=10.1128/MCB.24.19.8611-8626.2004;
Shani G., Marash L., Gozuacik D., Bialik S., Teitelbaum L., Shohat G.,
Kimchi A.;
"Death-associated protein kinase phosphorylates ZIP kinase, forming a
unique kinase hierarchy to activate its cell death functions.";
Mol. Cell. Biol. 24:8611-8626(2004).
[12]
INTERACTION WITH STAT3.
PubMed=16219639; DOI=10.1093/intimm/dxh331;
Sato N., Kawai T., Sugiyama K., Muromoto R., Imoto S., Sekine Y.,
Ishida M., Akira S., Matsuda T.;
"Physical and functional interactions between STAT3 and ZIP kinase.";
Int. Immunol. 17:1543-1552(2005).
[13]
INTERACTION WITH TCP10L, AND SUBCELLULAR LOCATION.
PubMed=15910542; DOI=10.1111/j.1365-2605.2005.00522.x;
Yu H., Jiang D., Guo Z., Saiyin H., Guo J., Wang X., Yu L.;
"TCP10L is expressed specifically in spermatogenic cells and binds to
death associated protein kinase-3.";
Int. J. Androl. 28:163-170(2005).
[14]
PHOSPHORYLATION AT THR-180; THR-225; THR-265; THR-299; THR-306 AND
SER-311, ENZYME REGULATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
THR-299; 299-THR-THR-300; VAL-427; VAL-434 AND LEU-441.
PubMed=15611134; DOI=10.1074/jbc.M412538200;
Graves P.R., Winkfield K.M., Haystead T.A.;
"Regulation of zipper-interacting protein kinase activity in vitro and
in vivo by multisite phosphorylation.";
J. Biol. Chem. 280:9363-9374(2005).
[15]
REVIEW ON FUNCTION.
PubMed=16756490; DOI=10.1146/annurev.biochem.75.103004.142615;
Bialik S., Kimchi A.;
"The death-associated protein kinases: structure, function, and
beyond.";
Annu. Rev. Biochem. 75:189-210(2006).
[16]
FUNCTION, ENZYME REGULATION, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT
THR-180; THR-265 AND THR-299, AND MUTAGENESIS OF LYS-42; ASP-161;
THR-225; THR-265 AND THR-299.
PubMed=17158456; DOI=10.1074/jbc.M609990200;
Hagerty L., Weitzel D.H., Chambers J., Fortner C.N., Brush M.H.,
Loiselle D., Hosoya H., Haystead T.A.;
"ROCK1 phosphorylates and activates zipper-interacting protein
kinase.";
J. Biol. Chem. 282:4884-4893(2007).
[17]
SUBCELLULAR LOCATION, AND ABSENCE OF INTERACTION WITH PARW.
PubMed=17953487; DOI=10.1371/journal.pgen.0030180;
Shoval Y., Pietrokovski S., Kimchi A.;
"ZIPK: a unique case of murine-specific divergence of a conserved
vertebrate gene.";
PLoS Genet. 3:1884-1893(2007).
[18]
REVIEW ON FUNCTION.
DOI=10.1002/sita.200600112;
Scheidtmann K.H.;
"Dlk/ZIP kinase, a novel Ser/Thr-specific protein kinase with multiple
functions.";
Signal Transduct. 7:248-259(2007).
[19]
FUNCTION IN PHOSPHPRYLATION OF RPL13A, AND CATALYTIC ACTIVITY.
PubMed=18995835; DOI=10.1016/j.molcel.2008.09.019;
Mukhopadhyay R., Ray P.S., Arif A., Brady A.K., Kinter M., Fox P.L.;
"DAPK-ZIPK-L13a axis constitutes a negative-feedback module regulating
inflammatory gene expression.";
Mol. Cell 32:371-382(2008).
[20]
FUNCTION IN ANDROGEN RECEPTOR-MEDIATED TRANSCRIPTION.
PubMed=18084323; DOI=10.1038/sj.onc.1210995;
Leister P., Felten A., Chasan A.I., Scheidtmann K.H.;
"ZIP kinase plays a crucial role in androgen receptor-mediated
transcription.";
Oncogene 27:3292-3300(2008).
[21]
FUNCTION AS TUMOR SUPPRESSOR, CHARACTERIZATION OF VARIANTS MET-112;
ASN-161 AND SER-216, MUTAGENESIS OF THR-180, AND SELF-ASSOCIATION.
PubMed=21487036; DOI=10.1158/0008-5472.CAN-10-3543;
Brognard J., Zhang Y.W., Puto L.A., Hunter T.;
"Cancer-associated loss-of-function mutations implicate DAPK3 as a
tumor-suppressing kinase.";
Cancer Res. 71:3152-3161(2011).
[22]
PHOSPHORYLATION AT THR-299, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
294-ARG-ARG-295.
PubMed=20854903; DOI=10.1016/j.cellsig.2010.09.016;
Weitzel D.H., Chambers J., Haystead T.A.;
"Phosphorylation-dependent control of ZIPK nuclear import is species
specific.";
Cell. Signal. 23:297-303(2011).
[23]
FUNCTION IN REGULATION OF AUTOPHAGY, AND INTERACTION WITH ULK1.
PubMed=21169990; DOI=10.1038/emboj.2010.338;
Tang H.W., Wang Y.B., Wang S.L., Wu M.H., Lin S.Y., Chen G.C.;
"Atg1-mediated myosin II activation regulates autophagosome formation
during starvation-induced autophagy.";
EMBO J. 30:636-651(2011).
[24]
FUNCTION, AND INTERACTION WITH NLK.
PubMed=21454679; DOI=10.1074/jbc.M110.189829;
Togi S., Ikeda O., Kamitani S., Nakasuji M., Sekine Y., Muromoto R.,
Nanbo A., Oritani K., Kawai T., Akira S., Matsuda T.;
"Zipper-interacting protein kinase (ZIPK) modulates canonical
Wnt/beta-catenin signaling through interaction with Nemo-like kinase
and T-cell factor 4 (NLK/TCF4).";
J. Biol. Chem. 286:19170-19177(2011).
[25]
FUNCTION, AND INTERACTION WITH ATF4.
PubMed=21408167; DOI=10.1371/journal.pone.0017344;
Shoval Y., Berissi H., Kimchi A., Pietrokovski S.;
"New modularity of DAP-kinases: alternative splicing of the DRP-1 gene
produces a ZIPk-like isoform.";
PLoS ONE 6:E17344-E17344(2011).
[26]
FUNCTION IN REORGANIZATION OF ACTIN CYTOSKELETON, AND INTERACTION WITH
RHOD.
PubMed=23454120; DOI=10.1016/j.bbrc.2013.02.046;
Nehru V., Almeida F.N., Aspenstrom P.;
"Interaction of RhoD and ZIP kinase modulates actin filament assembly
and focal adhesion dynamics.";
Biochem. Biophys. Res. Commun. 433:163-169(2013).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312, 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).
[28]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-277.
Kursula P., Vahokoski J., Wilmanns M.;
"Crystal structure of human ZIP kinase.";
Submitted (JUN-2006) to the PDB data bank.
[29]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 9-289 IN COMPLEX WITH
PYRIDONE 6, ENZYME REGULATION, SUBUNIT, AND PHOSPHORYLATION AT SER-50
AND THR-265.
PubMed=18239682; DOI=10.1038/emboj.2008.8;
Pike A.C., Rellos P., Niesen F.H., Turnbull A., Oliver A.W.,
Parker S.A., Turk B.E., Pearl L.H., Knapp S.;
"Activation segment dimerization: a mechanism for kinase
autophosphorylation of non-consensus sites.";
EMBO J. 27:704-714(2008).
[30]
VARIANTS [LARGE SCALE ANALYSIS] MET-112; ASN-161 AND SER-216.
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 kinase which is involved in the
regulation of apoptosis, autophagy, transcription, translation and
actin cytoskeleton reorganization. Involved in the regulation of
smooth muscle contraction. Regulates both type I (caspase-
dependent) apoptotic and type II (caspase-independent) autophagic
cell deaths signal, depending on the cellular setting. Involved in
regulation of starvation-induced autophagy. Regulates myosin
phosphorylation in both smooth muscle and non-muscle cells. In
smooth muscle, regulates myosin either directly by phosphorylating
MYL12B and MYL9 or through inhibition of smooth muscle myosin
phosphatase (SMPP1M) via phosphorylation of PPP1R12A; the
inhibition of SMPP1M functions to enhance muscle responsiveness to
Ca(2+) and promote a contractile state. Phosphorylates MYL12B in
non-muscle cells leading to reorganization of actin cytoskeleton.
Isoform 2 can phosphorylate myosin, PPP1R12A and MYL12B.
Overexpression leads to condensation of actin stress fibers into
thick bundles. Involved in actin filament focal adhesion dynamics.
The function in both reorganization of actin cytoskeleton and
focal adhesion dissolution is modulated by RhoD. Positively
regulates canonical Wnt/beta-catenin signaling through interaction
with NLK and TCF7L2. Phosphorylates RPL13A on 'Ser-77' upon
interferon-gamma activation which is causing RPL13A release from
the ribosome, RPL13A association with the GAIT complex and its
subsequent involvement in transcript-selective translation
inhibition. Enhances transcription from AR-responsive promoters in
a hormone- and kinase-dependent manner. Involved in regulation of
cell cycle progression and cell proliferation. May be a tumor
suppressor. {ECO:0000269|PubMed:10356987,
ECO:0000269|PubMed:11384979, ECO:0000269|PubMed:11781833,
ECO:0000269|PubMed:12917339, ECO:0000269|PubMed:15096528,
ECO:0000269|PubMed:15367680, ECO:0000269|PubMed:16219639,
ECO:0000269|PubMed:17126281, ECO:0000269|PubMed:17158456,
ECO:0000269|PubMed:18084323, ECO:0000269|PubMed:18995835,
ECO:0000269|PubMed:21169990, ECO:0000269|PubMed:21408167,
ECO:0000269|PubMed:21454679, ECO:0000269|PubMed:21487036,
ECO:0000269|PubMed:23454120}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:10356987, ECO:0000269|PubMed:11384979,
ECO:0000269|PubMed:11781833, ECO:0000269|PubMed:15096528,
ECO:0000269|PubMed:17126281, ECO:0000269|PubMed:18995835}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:10356987};
-!- ENZYME REGULATION: A sequential activation is proposed:
autophosphorylation at consensus sites is leading to dimerization
of the catalytic domain stabilized by phosphorylation at Ser-50
and activation segment exchange (producing an active confirmation
of both kinase modules in trans) followed by phosphorylation at
Thr-180 in the activation segment and at other regulatory sites
(Probable). Phosphorylation at Thr-180, Thr-225 and Thr-265 is
essential for activity. Oligomerization is required for full
enzymatic activity. Inhibited by pyridone 6 (K00225), a potent,
ATP-competitive inhibitor. {ECO:0000269|PubMed:15611134,
ECO:0000269|PubMed:17158456, ECO:0000269|PubMed:18239682,
ECO:0000303|PubMed:18239682}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=12 uM for myosin (isoform 2) {ECO:0000269|PubMed:17126281};
KM=6.2 uM for myosin (isoform 1) {ECO:0000269|PubMed:17126281};
KM=73 uM for MYL12B (isoform 2) {ECO:0000269|PubMed:17126281};
KM=10.4 uM for MYL12B (isoform 1) {ECO:0000269|PubMed:17126281};
Vmax=248 nmol/min/mg enzyme toward myosin (isoform 2)
{ECO:0000269|PubMed:17126281};
Vmax=120 nmol/min/mg enzyme toward myosin (isoform 1)
{ECO:0000269|PubMed:17126281};
Vmax=1.3 umol/min/mg enzyme toward MYL12B (isoform 2)
{ECO:0000269|PubMed:17126281};
Vmax=271 nmol/min/mg enzyme toward MYL12B (isoform 1)
{ECO:0000269|PubMed:17126281};
-!- SUBUNIT: Homooligomer in its kinase-active form (homotrimers and
homodimers are reported); monomeric in its kinase-inactive form.
Homodimerization is required for activation segment
autophosphorylation (Probable). Isoform 1 and isoform 2 interact
with myosin and PPP1R12A; interaction of isoform 1 with PPP1R12A
is inhibited by RhoA dominant negative form. Interacts with NLK,
DAXX, STAT3, RHOD (GTP-bound form) and TCP10L. Interacts with
PAWR; the interaction is reported conflictingly: according to
PubMed:17953487 does not interact with PAWR. Interacts with ULK1;
may be a substrate of ULK1. {ECO:0000269|PubMed:12917339,
ECO:0000269|PubMed:15292222, ECO:0000269|PubMed:15910542,
ECO:0000269|PubMed:16219639, ECO:0000269|PubMed:17126281,
ECO:0000269|PubMed:18239682, ECO:0000269|PubMed:21169990,
ECO:0000269|PubMed:21408167, ECO:0000269|PubMed:21454679,
ECO:0000269|PubMed:23454120, ECO:0000303|PubMed:18239682}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-77293, EBI-77293;
Q9UBE8:NLK; NbExp=3; IntAct=EBI-77293, EBI-366978;
O14974:PPP1R12A; NbExp=5; IntAct=EBI-77293, EBI-351726;
Q10728:Ppp1r12a (xeno); NbExp=2; IntAct=EBI-9691390, EBI-918263;
Q8TDR4:TCP10L; NbExp=5; IntAct=EBI-77293, EBI-3923210;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15367680,
ECO:0000269|PubMed:15910542, ECO:0000269|PubMed:20854903}.
Cytoplasm {ECO:0000269|PubMed:15367680,
ECO:0000269|PubMed:15611134, ECO:0000269|PubMed:17953487,
ECO:0000269|PubMed:20854903}. Note=Predominantly localizes to the
cytoplasm but can shuttle between the nucleus and cytoplasm;
cytoplasmic localization is promoted by phosphorylation at Thr-299
and involves Rho/Rock signaling. {ECO:0000269|PubMed:17953487,
ECO:0000269|PubMed:20854903}.
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus
{ECO:0000269|PubMed:17126281}. Cytoplasm
{ECO:0000269|PubMed:17126281}.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus
{ECO:0000269|PubMed:17126281}. Cytoplasm
{ECO:0000269|PubMed:17126281}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=ZIPK-L;
IsoId=O43293-1; Sequence=Displayed;
Name=2; Synonyms=ZIPK-S;
IsoId=O43293-2; Sequence=VSP_042059, VSP_042060;
Note=The internal splice site between exon 8 and the 3' UTR,
which yields this truncated isoform, is non-canonical.;
-!- TISSUE SPECIFICITY: Widely expressed. Isoform 1 and isoform 2 are
expressed in the bladder smooth muscle.
{ECO:0000269|PubMed:15292222, ECO:0000269|PubMed:17126281}.
-!- PTM: The phosphorylation status is critical for kinase activity,
oligomerization and intracellular localization. Phosphorylation at
Thr-180, Thr-225 and Thr-265 is essential for activity. The
phosphorylated form is localized in the cytoplasm promoted by
phosphorylation at Thr-299; nuclear translocation or retention is
maximal when it is not phosphorylated. Phosphorylation increases
the trimeric form, and its dephosphorylation favors a kinase-
inactive monomeric form. Both isoform 1 and isoform 2 can undergo
autophosphorylation. {ECO:0000269|PubMed:15367680,
ECO:0000269|PubMed:15611134, ECO:0000269|PubMed:17158456,
ECO:0000269|PubMed:20854903}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. DAP kinase subfamily.
{ECO:0000305}.
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EMBL; AB007144; BAA24955.1; -; mRNA.
EMBL; AB022341; BAA81746.1; -; mRNA.
EMBL; AK074799; BAG52004.1; -; mRNA.
EMBL; BC126430; AAI26431.1; -; mRNA.
EMBL; BC126432; AAI26433.1; -; mRNA.
EMBL; AB265224; BAF34614.1; -; mRNA.
CCDS; CCDS12116.1; -. [O43293-1]
RefSeq; NP_001339.1; NM_001348.2. [O43293-1]
RefSeq; XP_005259565.1; XM_005259508.1. [O43293-1]
UniGene; Hs.631844; -.
PDB; 1YRP; X-ray; 3.10 A; A/B=1-277.
PDB; 2J90; X-ray; 2.00 A; A/B=9-289.
PDB; 3BHY; X-ray; 1.24 A; A=9-289.
PDB; 3BQR; X-ray; 1.75 A; A=9-289.
PDB; 5A6N; X-ray; 1.70 A; A/B=9-289.
PDB; 5A6O; X-ray; 1.60 A; A/B=9-289.
PDBsum; 1YRP; -.
PDBsum; 2J90; -.
PDBsum; 3BHY; -.
PDBsum; 3BQR; -.
PDBsum; 5A6N; -.
PDBsum; 5A6O; -.
ProteinModelPortal; O43293; -.
SMR; O43293; -.
BioGrid; 107983; 56.
IntAct; O43293; 46.
MINT; MINT-6505325; -.
STRING; 9606.ENSP00000301264; -.
BindingDB; O43293; -.
ChEMBL; CHEMBL2468; -.
GuidetoPHARMACOLOGY; 2004; -.
iPTMnet; O43293; -.
PhosphoSitePlus; O43293; -.
BioMuta; DAPK3; -.
EPD; O43293; -.
MaxQB; O43293; -.
PaxDb; O43293; -.
PeptideAtlas; O43293; -.
PRIDE; O43293; -.
DNASU; 1613; -.
Ensembl; ENST00000301264; ENSP00000301264; ENSG00000167657. [O43293-1]
Ensembl; ENST00000545797; ENSP00000442973; ENSG00000167657. [O43293-1]
GeneID; 1613; -.
KEGG; hsa:1613; -.
UCSC; uc002lzc.2; human. [O43293-1]
CTD; 1613; -.
DisGeNET; 1613; -.
EuPathDB; HostDB:ENSG00000167657.11; -.
GeneCards; DAPK3; -.
HGNC; HGNC:2676; DAPK3.
HPA; HPA028569; -.
HPA; HPA064809; -.
MIM; 603289; gene.
neXtProt; NX_O43293; -.
OpenTargets; ENSG00000167657; -.
PharmGKB; PA27144; -.
eggNOG; KOG0032; Eukaryota.
eggNOG; ENOG410XRMJ; LUCA.
GeneTree; ENSGT00760000118877; -.
HOGENOM; HOG000233016; -.
HOVERGEN; HBG101549; -.
InParanoid; O43293; -.
KO; K08803; -.
OMA; PWIKVIK; -.
OrthoDB; EOG091G0J2O; -.
PhylomeDB; O43293; -.
TreeFam; TF314166; -.
Reactome; R-HSA-418889; Ligand-independent caspase activation via DCC.
SABIO-RK; O43293; -.
SignaLink; O43293; -.
SIGNOR; O43293; -.
ChiTaRS; DAPK3; human.
EvolutionaryTrace; O43293; -.
GeneWiki; DAPK3; -.
GenomeRNAi; 1613; -.
PRO; PR:O43293; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000167657; -.
CleanEx; HS_DAPK3; -.
ExpressionAtlas; O43293; baseline and differential.
Genevisible; O43293; HS.
GO; GO:0005884; C:actin filament; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0016605; C:PML body; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0008140; F:cAMP response element binding protein binding; TAS:ParkinsonsUK-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0043522; F:leucine zipper domain binding; IPI:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0017048; F:Rho GTPase binding; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IDA:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
GO; GO:0010506; P:regulation of autophagy; TAS:UniProtKB.
GO; GO:2000145; P:regulation of cell motility; TAS:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
GO; GO:0051893; P:regulation of focal adhesion assembly; IDA:UniProtKB.
GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0007088; P:regulation of mitotic nuclear division; TAS:UniProtKB.
GO; GO:0043519; P:regulation of myosin II filament organization; IEA:Ensembl.
GO; GO:0006940; P:regulation of smooth muscle contraction; TAS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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;
3D-structure; Activator; Alternative splicing; Apoptosis; ATP-binding;
Chromatin regulator; Complete proteome; Cytoplasm; Kinase;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Serine/threonine-protein kinase; Transcription;
Transcription regulation; Transferase; Translation regulation;
Tumor suppressor.
CHAIN 1 454 Death-associated protein kinase 3.
/FTId=PRO_0000085914.
DOMAIN 13 275 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 19 27 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 161 204 Activation segment.
{ECO:0000250|UniProtKB:O96017}.
REGION 427 441 Leucine-zipper.
{ECO:0000303|PubMed:9488481}.
ACT_SITE 139 139 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 42 42 ATP. {ECO:0000305}.
BINDING 94 94 Inhibitor. {ECO:0000269|PubMed:18239682}.
BINDING 96 96 Inhibitor. {ECO:0000269|PubMed:18239682}.
MOD_RES 50 50 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:18239682}.
MOD_RES 180 180 Phosphothreonine.
{ECO:0000269|PubMed:15611134,
ECO:0000269|PubMed:17158456}.
MOD_RES 225 225 Phosphothreonine.
{ECO:0000269|PubMed:15611134}.
MOD_RES 265 265 Phosphothreonine; by autocatalysis and
ROCK1. {ECO:0000269|PubMed:15611134,
ECO:0000269|PubMed:17158456,
ECO:0000269|PubMed:18239682}.
MOD_RES 299 299 Phosphothreonine; by autocatalysis, DAPK1
and ROCK1. {ECO:0000269|PubMed:15367680,
ECO:0000269|PubMed:15611134,
ECO:0000269|PubMed:17158456,
ECO:0000269|PubMed:20854903}.
MOD_RES 306 306 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:15611134}.
MOD_RES 309 309 Phosphoserine; by DAPK1.
{ECO:0000269|PubMed:15367680}.
MOD_RES 311 311 Phosphoserine; by autocatalysis and
DAPK1. {ECO:0000269|PubMed:15367680,
ECO:0000269|PubMed:15611134}.
MOD_RES 312 312 Phosphoserine; by DAPK1.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15367680}.
MOD_RES 318 318 Phosphoserine; by DAPK1.
{ECO:0000269|PubMed:15367680}.
MOD_RES 326 326 Phosphoserine; by DAPK1.
{ECO:0000269|PubMed:15367680}.
VAR_SEQ 313 322 LPPNNSYADF -> ASPIVAPVDA (in isoform 2).
{ECO:0000303|PubMed:17126281}.
/FTId=VSP_042059.
VAR_SEQ 323 454 Missing (in isoform 2).
{ECO:0000303|PubMed:17126281}.
/FTId=VSP_042060.
VARIANT 112 112 T -> M (in a colorectal adenocarcinoma
sample; somatic mutation; greatly reduces
kinase activity, increases cell
proliferation and cell survival).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:21487036}.
/FTId=VAR_040438.
VARIANT 161 161 D -> N (in an ovarian mucinous carcinoma
sample; somatic mutation; greatly reduces
kinase activity, increases cell
proliferation and cell survival).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:21487036}.
/FTId=VAR_040439.
VARIANT 216 216 P -> S (in a lung neuroendocrine
carcinoma sample; somatic mutation;
greatly reduces kinase activity,
increases cell proliferation, cell
adhesion and cell survival).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:21487036}.
/FTId=VAR_040440.
MUTAGEN 42 42 K->A: Loss of kinase activity at low
concentrations of ATP.
{ECO:0000269|PubMed:17158456}.
MUTAGEN 161 161 D->A: Loss of kinase activity.
{ECO:0000269|PubMed:17158456}.
MUTAGEN 180 180 T->A: Greatly reduced kinase activity.
{ECO:0000269|PubMed:21487036}.
MUTAGEN 225 225 T->A: Loss of kinase activity.
{ECO:0000269|PubMed:17158456}.
MUTAGEN 265 265 T->A: Loss of phosphorylation by ROCK1,
catalytically inactive.
{ECO:0000269|PubMed:17158456}.
MUTAGEN 294 295 RR->AA: Cytoplasmic localization.
{ECO:0000269|PubMed:20854903}.
MUTAGEN 299 300 TT->AA: Predominantly nuclear
localization.
{ECO:0000269|PubMed:15611134}.
MUTAGEN 299 299 T->A: Loss of phosphorylation by ROCK1.
{ECO:0000269|PubMed:17158456}.
MUTAGEN 299 299 T->D: Predominantly cytoplasmic
localization; phosphomimetic.
{ECO:0000269|PubMed:15611134}.
MUTAGEN 427 427 V->A: Predominantly nuclear localization;
when associated with A-434 and A-441.
{ECO:0000269|PubMed:15611134}.
MUTAGEN 434 434 V->A: Predominantly nuclear localization;
when associated with A-427 and A-441.
{ECO:0000269|PubMed:15611134}.
MUTAGEN 441 441 L->A: Predominantly nuclear localization;
when associated with A-427 and A-434.
{ECO:0000269|PubMed:15611134}.
HELIX 9 12 {ECO:0000244|PDB:3BHY}.
STRAND 13 21 {ECO:0000244|PDB:3BHY}.
STRAND 23 32 {ECO:0000244|PDB:3BHY}.
TURN 33 35 {ECO:0000244|PDB:3BHY}.
STRAND 38 46 {ECO:0000244|PDB:3BHY}.
HELIX 49 51 {ECO:0000244|PDB:2J90}.
STRAND 53 56 {ECO:0000244|PDB:3BHY}.
HELIX 58 70 {ECO:0000244|PDB:3BHY}.
STRAND 79 84 {ECO:0000244|PDB:3BHY}.
STRAND 86 94 {ECO:0000244|PDB:3BHY}.
HELIX 101 108 {ECO:0000244|PDB:3BHY}.
HELIX 113 132 {ECO:0000244|PDB:3BHY}.
HELIX 142 144 {ECO:0000244|PDB:3BHY}.
STRAND 145 148 {ECO:0000244|PDB:3BHY}.
STRAND 150 154 {ECO:0000244|PDB:3BHY}.
STRAND 157 159 {ECO:0000244|PDB:3BHY}.
HELIX 171 175 {ECO:0000244|PDB:5A6N}.
HELIX 176 178 {ECO:0000244|PDB:5A6O}.
HELIX 181 183 {ECO:0000244|PDB:3BHY}.
HELIX 186 189 {ECO:0000244|PDB:3BHY}.
HELIX 197 212 {ECO:0000244|PDB:3BHY}.
HELIX 222 230 {ECO:0000244|PDB:3BHY}.
HELIX 238 241 {ECO:0000244|PDB:3BHY}.
HELIX 246 253 {ECO:0000244|PDB:3BHY}.
HELIX 260 262 {ECO:0000244|PDB:3BHY}.
HELIX 266 271 {ECO:0000244|PDB:3BHY}.
HELIX 273 280 {ECO:0000244|PDB:3BHY}.
SEQUENCE 454 AA; 52536 MW; 56773008A6A61CF0 CRC64;
MSTFRQEDVE DHYEMGEELG SGQFAIVRKC RQKGTGKEYA AKFIKKRRLS SSRRGVSREE
IEREVNILRE IRHPNIITLH DIFENKTDVV LILELVSGGE LFDFLAEKES LTEDEATQFL
KQILDGVHYL HSKRIAHFDL KPENIMLLDK NVPNPRIKLI DFGIAHKIEA GNEFKNIFGT
PEFVAPEIVN YEPLGLEADM WSIGVITYIL LSGASPFLGE TKQETLTNIS AVNYDFDEEY
FSNTSELAKD FIRRLLVKDP KRRMTIAQSL EHSWIKAIRR RNVRGEDSGR KPERRRLKTT
RLKEYTIKSH SSLPPNNSYA DFERFSKVLE EAAAAEEGLR ELQRSRRLCH EDVEALAAIY
EEKEAWYREE SDSLGQDLRR LRQELLKTEA LKRQAQEEAK GALLGTSGLK RRFSRLENRY
EALAKQVASE MRFVQDLVRA LEQEKLQGVE CGLR


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