(data stored in ACNUC26462 zone)

HOGENOM: MOUSE10_PE1368

ID   MOUSE10_PE1368                       STANDARD;      PRT;   448 AA.
AC   MOUSE10_PE1368; O54784;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Death-associated protein kinase 3; Short=DAP kinase 3;
DE   EC=2.7.11 1;AltName: Full=DAP-like kinase; Short=Dlk;AltName:
DE   Full=ZIP-kinase; (MOUSE10.PE1368).
GN   Name=Dapk3; Synonyms=Zipk;
OS   MUS MUSCULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE10.PE1368.
CC       Mus musculus chromosome 10 NCBIM37  sequence 1..129993255 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:DAPK3_MOUSE
CC   -!- FUNCTION: Serine/threonine kinase which acts as a positive
CC       regulator of apoptosis. Phosphorylates histone H3 on 'Thr-11' at
CC       centromeres during mitosis. Regulates myosin light chain
CC       phosphatase through phosphorylation of MYPT1 thereby regulating
CC       the assembly of the actin cytoskeleton, cell migration,
CC       invasiveness of tumor cells, smooth muscle contraction and neurite
CC       outgrowth. Involved in the formation of promyelocytic leukemia
CC       protein nuclear body (PML-NB), one of many subnuclear domains in
CC       the eukaryotic cell nucleus, and which is involved in oncogenesis
CC       and viral infection (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium.
CC   -!- ENZYME REGULATION: Phosphorylated on Thr-265 by ROCK1 which
CC       activates the kinase (By similarity).
CC   -!- SUBUNIT: Homodimer or forms heterodimers with ATF4. Both
CC       interactions require an intact leucine zipper domain and
CC       oligomerization is required for full enzymatic activity. Also
CC       binds to DAXX and PAWR, possibly in a ternary complex which plays
CC       a role in caspase activation. Interacts with AATF and CDC5L.
CC   -!- INTERACTION:
CC       O35613:Daxx; NbExp=2; IntAct=EBI-77359, EBI-77304;
CC       Q925B0:Pawr; NbExp=2; IntAct=EBI-77359, EBI-77397;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Chromosome, centromere.
CC       Note=Relocates to the cytoplasm on binding PAWR where the complex
CC       appears to interact with actin filaments. Associates to
CC       centromeres from prophase to anaphase.
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart, brain, lung,
CC       skeletal muscle, kidney and testis. Lower levels in liver and
CC       spleen.
CC   -!- PTM: Ubiquitinated. Ubiquitination mediated by the UBE2D3 E3
CC       ligase does not lead to proteasomal degradation, but influences
CC       promyelocytic leukemia protein nuclear bodies (PML-NBs) formation
CC       in the nucleus (By similarity).
CC   -!- PTM: Autophosphorylated (By similarity). Phosphorylated by ROCK1
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. DAP kinase subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- GENE_FAMILY: HOG000233016 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000034974;ENSMUST00000047665;ENSMUSP00000035962.
DR   EMBL; AB007143; - ;
DR   EMBL; BC125443; - ;
DR   EMBL; BC137680; - ;
DR   EMBL; CH466553; - ;
DR   UniProtKB/Swiss-Prot; O54784; -.
DR   EMBL; AB007143; BAA24954.1; -; mRNA.
DR   IPI; IPI00117846; -.
DR   RefSeq; NP_001177402.1; NM_001190473.1.
DR   RefSeq; NP_001177403.1; NM_001190474.1.
DR   RefSeq; NP_031854.1; NM_007828.2.
DR   UniGene; Mm.10294; -.
DR   ProteinModelPortal; O54784; -.
DR   SMR; O54784; 2-276.
DR   IntAct; O54784; 6.
DR   STRING; O54784; -.
DR   PhosphoSite; O54784; -.
DR   PRIDE; O54784; -.
DR   Ensembl; ENSMUST00000047665; ENSMUSP00000035962; ENSMUSG00000034974.
DR   GeneID; 13144; -.
DR   KEGG; mmu:13144; -.
DR   CTD; 1613; -.
DR   MGI; MGI:1203520; Dapk3.
DR   eggNOG; maNOG05680; -.
DR   InParanoid; O54784; -.
DR   OMA; FRIVALC; -.
DR   OrthoDB; EOG4VDPZK; -.
DR   PhylomeDB; O54784; -.
DR   Reactome; REACT_100962; Apoptosis.
DR   NextBio; 283230; -.
DR   ArrayExpress; O54784; -.
DR   Bgee; O54784; -.
DR   CleanEx; MM_DAPK3; -.
DR   Genevestigator; O54784; -.
DR   GermOnline; ENSMUSG00000034974; Mus musculus.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0006917; P:induction of apoptosis; IMP:UniProtKB.
DR   GO; GO:0007243; P:intracellular protein kinase cascade; IDA:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR020675; Myosin_light_ch_kinase-rel.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_kinase_dom.
DR   PANTHER; PTHR22964; Myosin_light_chain_kin-rel; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   HOGENOMDNA; MOUSE10.PE1368; -.
KW   ENSMUSG000000349745old_1320000031; ENSMUSP000000359621old_1320000031;
KW   Q05A21_MOUSE; AB007143; BC125443; BC137680; CH466553;
KW   Apoptosis; ATP-binding; Centromere; Chromatin regulator; Chromosome;
KW   Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase; Ubl conjugation.
SQ   SEQUENCE   448 AA;  UNKNOWN MW;  UNKNOWN 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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