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

 DAPK3_MOUSE             Reviewed;         448 AA.
O54784;
28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
25-APR-2018, entry version 156.
RecName: Full=Death-associated protein kinase 3;
Short=DAP kinase 3;
EC=2.7.11.1 {ECO:0000269|PubMed:15096528, ECO:0000269|PubMed:16219639, ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:9488481};
AltName: Full=DAP-like kinase;
Short=Dlk;
AltName: Full=MYPT1 kinase;
AltName: Full=ZIP-kinase;
Name=Dapk3; Synonyms=Zipk;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000312|EMBL:BAA24954.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, COFACTOR, FUNCTION IN
APOPTOSIS, TISSUE SPECIFICITY, INTERACTION WITH ATF4, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF LYS-42; VAL-422; VAL-429 AND LEU-436.
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}
FUNCTION IN APOPTOSIS, SUBCELLULAR LOCATION, 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).
[3]
FUNCTION IN PHOSPHORYLATION OF MYL12B, CATALYTIC ACTIVITY, AND
FUNCTION IN CYTOSKELETON REORGANIZATION.
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).
[4]
FUNCTION IN PHOSPHORYLATION OF STAT3, CATALYTIC ACTIVITY, AND
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).
[5]
PHOSPHORYLATION AT THR-265.
PubMed=16325270; DOI=10.1016/j.imlet.2005.10.015;
Sato N., Kamada N., Muromoto R., Kawai T., Sugiyama K., Watanabe T.,
Imoto S., Sekine Y., Ohbayashi N., Ishida M., Akira S., Matsuda T.;
"Phosphorylation of threonine-265 in zipper-interacting protein kinase
plays an important role in its activity and is induced by IL-6 family
cytokines.";
Immunol. Lett. 103:127-134(2006).
[6]
INTERACTION WITH UBE2D1; UBE2D2 AND UBE2D3, UBIQUITINATION, AND
SUBCELLULAR LOCATION.
PubMed=18515077; DOI=10.1016/j.bbrc.2008.05.113;
Ohbayashi N., Okada K., Kawakami S., Togi S., Sato N., Ikeda O.,
Kamitani S., Muromoto R., Sekine Y., Kawai T., Akira S., Matsuda T.;
"Physical and functional interactions between ZIP kinase and UbcH5.";
Biochem. Biophys. Res. Commun. 372:708-712(2008).
[7]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF 289-ARG-ARG-290 AND ALA-294.
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).
[8]
FUNCTION, AND INTERACTION WITH NLK AND TCF7L2.
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).
[9]
FUNCTION IN PHOSPHORYLATION OF RPL13A, AND CATALYTIC ACTIVITY.
PubMed=23071094; DOI=10.1128/MCB.01168-12;
Arif A., Chatterjee P., Moodt R.A., Fox P.L.;
"Heterotrimeric GAIT complex drives transcript-selective translation
inhibition in murine macrophages.";
Mol. Cell. Biol. 32:5046-5055(2012).
-!- FUNCTION: Serine/threonine kinase which is involved in the
regulation of apoptosis, autophagy, transcription, translation and
actin cytoskeleton reorganization. Regulates both type I (caspase-
dependent) apoptotic and type II (caspase-independent) autophagic
cell deaths signal, depending on the cellular setting. Involved in
formation of promyelocytic leukemia protein nuclear body (PML-NB).
Involved in apoptosis involving PAWR which mediates cytoplasmic
relocation; in vitro phosphorylates PAWR (By similarity).
Phosphorylates MYL12B in non-muscle cells leading to
reorganization of actin cytoskeleton such as in regulation of cell
polarity and cell migration. Positively regulates canonical
Wnt/beta-catenin signaling through interaction with NLK and
TCF7L2; disrupts the NLK-TCF7L2 complex thereby influencing the
phosphorylation of TCF7L2 by NLK. Phosphorylates STAT3 and
enhances its transcriptional activity. Enhances transcription from
AR-responsive promoters in a hormone- and kinase-dependent manner.
Phosphorylates histone H3 on 'Thr-11' at centromeres during
mitosis (By similarity). 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. {ECO:0000250|UniProtKB:O88764,
ECO:0000269|PubMed:12917339, ECO:0000269|PubMed:15096528,
ECO:0000269|PubMed:16219639, ECO:0000269|PubMed:21454679,
ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:9488481}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:15096528, ECO:0000269|PubMed:16219639,
ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:9488481}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:9488481};
-!- ENZYME REGULATION: A sequential activation is proposed:
autophosphorylation at consensus sites is leading to dimerization
of the catalytic domain 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. Inhibited by
pyridone 6 (K00225), a potent, ATP-competitive inhibitor.
Phosphorylation at Thr-180, Thr-225 and Thr-265 is essential for
activity. {ECO:0000250|UniProtKB:O43293}.
-!- 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 (By similarity). Interacts with DAXX, PAWR,
ATF4, NLK, TCF7L2, UBE2D1, UBE2D2, UBE2D3, and CDC5L. Interacts
with AR; enhanced by AATF. {ECO:0000250|UniProtKB:O43293,
ECO:0000269|PubMed:12917339, ECO:0000269|PubMed:16219639,
ECO:0000269|PubMed:18515077, ECO:0000269|PubMed:21454679,
ECO:0000269|PubMed:9488481}.
-!- INTERACTION:
P18848:ATF4 (xeno); NbExp=2; IntAct=EBI-77359, EBI-492498;
Q06507:Atf4; NbExp=3; IntAct=EBI-77359, EBI-77383;
O35613:Daxx; NbExp=2; IntAct=EBI-77359, EBI-77304;
Q925B0:Pawr; NbExp=2; IntAct=EBI-77359, EBI-77397;
P42227:Stat3; NbExp=8; IntAct=EBI-77359, EBI-602878;
P61077:UBE2D3 (xeno); NbExp=2; IntAct=EBI-77359, EBI-348268;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18515077,
ECO:0000269|PubMed:20854903, ECO:0000269|PubMed:9488481}. Nucleus,
PML body {ECO:0000269|PubMed:12917339}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:O88764}. Chromosome, centromere
{ECO:0000250|UniProtKB:O88764}. Cytoplasm
{ECO:0000250|UniProtKB:O88764}. Note=Predominantly localized to
the nucleus. Relocates to the cytoplasm on binding PAWR where the
complex appears to interact with actin filaments. Associated with
the centrosomes throughout the mitotic cell cycle, with the
centromeres from prophase to anaphase and with the contractile
ring during cytokinesis (By similarity).
{ECO:0000250|UniProtKB:O88764}.
-!- TISSUE SPECIFICITY: Highly expressed in heart, brain, lung,
skeletal muscle, kidney and testis. Lower levels in liver and
spleen. {ECO:0000269|PubMed:9488481}.
-!- PTM: Ubiquitinated. Ubiquitination mediated by the UBE2D3 E3
ligase does not lead to proteasomal degradation, but influences
promyelocytic leukemia protein nuclear bodies (PML-NBs) formation
in the nucleus. {ECO:0000269|PubMed:18515077}.
-!- 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 and 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.
{ECO:0000250|UniProtKB:O43293}.
-!- MISCELLANEOUS: A species-specific loss of a key phosphorylation
site in murine DAPK3 seems to direct it mainly to the nucleus
which is proposed to be compensated by the interaction with PAWR
to maintain at least the cytoplasmic basic membrane blebbing
function in the apoptosis pathway. {ECO:0000250|UniProtKB:O88764}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. DAP kinase subfamily.
{ECO:0000305}.
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EMBL; AB007143; BAA24954.1; -; mRNA.
CCDS; CCDS24045.1; -.
RefSeq; NP_001177402.1; NM_001190473.1.
RefSeq; NP_031854.1; NM_007828.2.
RefSeq; XP_006513258.1; XM_006513195.2.
UniGene; Mm.10294; -.
ProteinModelPortal; O54784; -.
SMR; O54784; -.
BioGrid; 199052; 6.
IntAct; O54784; 11.
STRING; 10090.ENSMUSP00000035962; -.
iPTMnet; O54784; -.
PhosphoSitePlus; O54784; -.
EPD; O54784; -.
PaxDb; O54784; -.
PeptideAtlas; O54784; -.
PRIDE; O54784; -.
Ensembl; ENSMUST00000047665; ENSMUSP00000035962; ENSMUSG00000034974.
Ensembl; ENSMUST00000178422; ENSMUSP00000137333; ENSMUSG00000034974.
Ensembl; ENSMUST00000219850; ENSMUSP00000151577; ENSMUSG00000034974.
GeneID; 13144; -.
KEGG; mmu:13144; -.
UCSC; uc007ggg.2; mouse.
CTD; 1613; -.
MGI; MGI:1203520; Dapk3.
eggNOG; KOG0032; Eukaryota.
eggNOG; ENOG410XRMJ; LUCA.
GeneTree; ENSGT00760000118877; -.
HOGENOM; HOG000233016; -.
HOVERGEN; HBG101549; -.
InParanoid; O54784; -.
KO; K08803; -.
OMA; FRIVALC; -.
OrthoDB; EOG091G0J2O; -.
PhylomeDB; O54784; -.
TreeFam; TF314166; -.
PRO; PR:O54784; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000034974; -.
CleanEx; MM_DAPK3; -.
ExpressionAtlas; O54784; baseline and differential.
Genevisible; O54784; MM.
GO; GO:0005884; C:actin filament; IEA:Ensembl.
GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IDA:MGI.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0016301; F:kinase activity; ISO:MGI.
GO; GO:0043522; F:leucine zipper domain binding; ISO:MGI.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0017048; F:Rho GTPase binding; ISO:MGI.
GO; GO:0006915; P:apoptotic process; ISO:MGI.
GO; GO:0097190; P:apoptotic signaling pathway; IDA:MGI.
GO; GO:0071346; P:cellular response to interferon-gamma; IMP:UniProtKB.
GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
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; ISO:MGI.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; ISO:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
GO; GO:0051893; P:regulation of focal adhesion assembly; ISO:MGI.
GO; GO:0007346; P:regulation of mitotic cell cycle; ISO:MGI.
GO; GO:0043519; P:regulation of myosin II filament organization; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
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;
Activator; Apoptosis; ATP-binding; Centromere; Chromatin regulator;
Chromosome; Complete proteome; Cytoplasm; Cytoskeleton; Kinase;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transcription;
Transcription regulation; Transferase; Ubl conjugation.
CHAIN 1 448 Death-associated protein kinase 3.
/FTId=PRO_0000085915.
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 390 448 Interaction with CDC5L.
{ECO:0000250|UniProtKB:O88764}.
REGION 422 436 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:0000250|UniProtKB:O43293}.
BINDING 96 96 Inhibitor.
{ECO:0000250|UniProtKB:O43293}.
MOD_RES 180 180 Phosphothreonine.
{ECO:0000250|UniProtKB:O43293}.
MOD_RES 225 225 Phosphothreonine.
{ECO:0000250|UniProtKB:O43293}.
MOD_RES 265 265 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:16325270}.
MOD_RES 265 265 Phosphothreonine; by ROCK1.
{ECO:0000250|UniProtKB:O43293}.
MOD_RES 304 304 Phosphoserine; by DAPK1.
{ECO:0000250|UniProtKB:O43293}.
MOD_RES 306 306 Phosphoserine; by autocatalysis and
DAPK1. {ECO:0000250|UniProtKB:O43293}.
MOD_RES 307 307 Phosphoserine; by DAPK1.
{ECO:0000250|UniProtKB:O43293}.
MOD_RES 313 313 Phosphoserine; by DAPK1.
{ECO:0000250|UniProtKB:O43293}.
MOD_RES 321 321 Phosphoserine; by DAPK1.
{ECO:0000250|UniProtKB:O43293}.
MUTAGEN 42 42 K->A: Loss of activity.
{ECO:0000269|PubMed:9488481}.
MUTAGEN 289 290 RR->AA: Nuclear localization.
{ECO:0000269|PubMed:20854903}.
MUTAGEN 294 294 A->D: Nuclear colocalization.
{ECO:0000269|PubMed:20854903}.
MUTAGEN 422 422 V->A: Decreased activity; when associated
with A-429 and A-436.
{ECO:0000269|PubMed:9488481}.
MUTAGEN 429 429 V->A: Decreased activity; when associated
with A-422 and A-436.
{ECO:0000269|PubMed:9488481}.
MUTAGEN 436 436 L->A: Decreased activity; when associated
with A-422 and A-429.
{ECO:0000269|PubMed:9488481}.
SEQUENCE 448 AA; 51422 MW; DA32EF3EB1F20EFC CRC64;
MSTFRQEDVE DHYEMGEELG SGQFAIVRKC QQKGTGMEYA AKFIKKRRLP SSRRGVSREE
IEREVSILRE IRHPNIITLH DVFENKTDVV LILELVSGGE LFDFLAEKES LTEDEATQFL
KQILDGVHYL HSKRIAHFDL KPENIMLLDK HAASPRIKLI DFGIAHRIEA GSEFKNIFGT
PEFVAPEIVN YEPLGLEADM WSIGVITYIL LSGASPFLGE TKQETLTNIS AVNYDFDEEY
FSSTSELAKD FIRRLLVKDP KRRMTIAQSL EHSWIKVRRR EDGARKPERR RLRAARLREY
SLKSHSSMPR NTSYASFERF SRVLEDVAAA EQGLRELQRG RRQCRERVCA LRAAAEQREA
RCRDGSAGLG RDLRRLRTEL GRTEALRTRA QEEARAALLG AGGLKRRLCR LENRYDALAA
QVAAEVQFVR DLVRALEQER LQAECGVR


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EIAAB25228 Dual specificity mitogen-activated protein kinase kinase 1,ERK activator kinase 1,MAP kinase kinase 1,Map2k1,MAPK_ERK kinase 1,MAPKK 1,MEK 1,Mek1,Prkmk1,Rat,Rattus norvegicus


 

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