Dapk3
entrez
64391
canonical
uniprot
O88764
canonical
ensembl
ENSRNOG00000020383
resolver
ensembl
ENSRNOG00055032768
resolver
ensembl
ENSRNOG00060030872
resolver
ensembl
ENSRNOG00065022007
resolver
ensp
ENSRNOP00000027634
resolver
ensp
ENSRNOP00000081984
resolver
enst
ENSRNOT00000096134
resolver
genesymbol
Dapk3
resolver
genesymbol_syn
Zipk
resolver
uniprot
A0A8I5ZTC3
resolver
uniprot_entry
A0A8I5ZTC3_RAT
resolver
uniprot_entry
DAPK3_RAT
resolver
activity_regulation
ACTIVITY 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 (By similarity). {ECO:0000250|UniProtKB:O43293}.
uniprot
proteins
amino_acid_sequence
MSTFRQEDVEDHYEMGEELGSGQFAIVRKCQQKGTGMEYAAKFIKKRRLPSSRRGVSREEIEREVSILREIRHPNIITLHDVFENKTDVVLILELVSGGELFDFLAEKESLTEDEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKHAASPRIKLIDFGIAHRIEAGSEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSSTSELAKDFIRRLLVKDPKRRMTIAQSLEHSWIKVRRREDGARKPERRRLRAARLREYSLKSHSSMPRNTSYASFERFSRVLEDVAAAEQGLRELQRGRRQCRERVCALRVAAEQREARCRDGSAGLGRDLRRLRTELGRTEALRTRAQEEARAALLGAGGLKRRLCRLENRYDALAAQVAAEVQFVRDLVRALEQERLQAECGVR
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
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. 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 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 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 (By similarity). Phosphorylates STAT3 and enhances its transcriptional activity (By similarity). Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Phosphorylates histone H3 on 'Thr-11' at centromeres during mitosis. {ECO:0000250|UniProtKB:O43293, ECO:0000250|UniProtKB:O54784, ECO:0000269|PubMed:10602480, ECO:0000269|PubMed:11384979, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15096528, ECO:0000269|PubMed:18084323, ECO:0000269|PubMed:9840928}.
uniprot
proteins
mass_dalton
51450
uniprot
proteins
mutagenesis
MUTAGEN 42; /note="K->A: Loss of kinase activity, loss of PAWR-linked translocation into the cytoplasm; maintains nuclear localization but loss of localization to PML-NB."; /evidence="ECO:0000269|PubMed:10602474, ECO:0000269|PubMed:10602480"; MUTAGEN 294; /note="A->T: Causes dissociation from promyelocytic leukemia oncogenic bodies and increased blebbing-inducing potency; when associated with T-300."; /evidence="ECO:0000269|PubMed:17953487"; MUTAGEN 295; /note="A->T: Causes dissociation from promyelocytic leukemia oncogenic bodies and increased blebbing-inducing potency; when associated with T-299."; /evidence="ECO:0000269|PubMed:17953487"; MUTAGEN 406..407; /note="RR->AL: Cytoplasmic localization."; /evidence="ECO:0000269|PubMed:10602474
uniprot
proteins
post_translational_modification
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 (By similarity). {ECO:0000250|UniProtKB:O54784}.; 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}.
uniprot
proteins
protein_family
CAMK Ser/Thr protein kinase family
uniprot
proteins
protein_family
DAP kinase subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
10580117
uniprot
proteins
pubmed
10602474
uniprot
proteins
pubmed
10602480
uniprot
proteins
pubmed
11384979
uniprot
proteins
pubmed
11884640
uniprot
proteins
pubmed
12560483
uniprot
proteins
pubmed
14582533
uniprot
proteins
pubmed
15096528
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17953487
uniprot
proteins
pubmed
18084323
uniprot
proteins
pubmed
18505470
uniprot
proteins
pubmed
20854903
uniprot
proteins
pubmed
9840928
uniprot
proteins
sequence_length
448
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10602474, ECO:0000269|PubMed:10602480, ECO:0000269|PubMed:17953487, ECO:0000269|PubMed:20854903, ECO:0000269|PubMed:9840928}. Nucleus, PML body {ECO:0000269|PubMed:10602474}. Cytoplasm {ECO:0000303|PubMed:10602480}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:14582533}. Chromosome, centromere {ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:14582533}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15096528}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O43293}. Midbody {ECO:0000250|UniProtKB:O43293}. Note=Predominantly localized to the nucleus. Relocates to the cytoplasm on binding PAWR where the complex appears to interact with actin filaments (Probable). Associated with the centrosomes throughout the mitotic cell cycle, with the centromeres from prophase to anaphase and with the contractile ring during cytokinesis. {ECO:0000269|PubMed:14582533, ECO:0000269|PubMed:17953487, ECO:0000303|PubMed:10602474}.
uniprot
proteins