Dapk3
entrez
13144
canonical
uniprot
O54784
canonical
ensembl
ENSMUSG00000034974
resolver
ensp
ENSMUSP00000035962
resolver
ensp
ENSMUSP00000137333
resolver
ensp
ENSMUSP00000151577
resolver
ensp
ENSMUSP00000301320
resolver
ensp
ENSMUSP00000301325
resolver
ensp
ENSMUSP00000301329
resolver
enst
ENSMUST00000047665
resolver
enst
ENSMUST00000178422
resolver
enst
ENSMUST00000219850
resolver
genesymbol
Dapk3
resolver
genesymbol_syn
Zipk
resolver
uniprot
Q05A21
resolver
uniprot_entry
DAPK3_MOUSE
resolver
uniprot_entry
Q05A21_MOUSE
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. {ECO:0000250|UniProtKB:O43293}.
uniprot
proteins
amino_acid_sequence
MSTFRQEDVEDHYEMGEELGSGQFAIVRKCQQKGTGMEYAAKFIKKRRLPSSRRGVSREEIEREVSILREIRHPNIITLHDVFENKTDVVLILELVSGGELFDFLAEKESLTEDEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKHAASPRIKLIDFGIAHRIEAGSEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSSTSELAKDFIRRLLVKDPKRRMTIAQSLEHSWIKVRRREDGARKPERRRLRAARLREYSLKSHSSMPRNTSYASFERFSRVLEDVAAAEQGLRELQRGRRQCRERVCALRAAAEQREARCRDGSAGLGRDLRRLRTELGRTEALRTRAQEEARAALLGAGGLKRRLCRLENRYDALAAQVAAEVQFVRDLVRALEQERLQAECGVR
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 (By similarity). 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 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}.
uniprot
proteins
mass_dalton
51422
uniprot
proteins
mutagenesis
MUTAGEN 42; /note="K->A: Loss of activity."; /evidence="ECO:0000269|PubMed:9488481"; MUTAGEN 289..290; /note="RR->AA: Nuclear localization."; /evidence="ECO:0000269|PubMed:20854903"; MUTAGEN 294; /note="A->D: Nuclear colocalization."; /evidence="ECO:0000269|PubMed:20854903"; MUTAGEN 422; /note="V->A: Decreased activity; when associated with A-429 and A-436."; /evidence="ECO:0000269|PubMed:9488481"; MUTAGEN 429; /note="V->A: Decreased activity; when associated with A-422 and A-436."; /evidence="ECO:0000269|PubMed:9488481"; MUTAGEN 436; /note="L->A: Decreased activity; when associated with A-422 and A-429."; /evidence="ECO:0000269|PubMed:9488481
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. {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}.
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
12917339
uniprot
proteins
pubmed
15096528
uniprot
proteins
pubmed
16219639
uniprot
proteins
pubmed
16325270
uniprot
proteins
pubmed
18515077
uniprot
proteins
pubmed
20854903
uniprot
proteins
pubmed
21454679
uniprot
proteins
pubmed
23071094
uniprot
proteins
pubmed
9488481
uniprot
proteins
sequence_length
448
uniprot
proteins
subcellular_location
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}. 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. 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}.
uniprot
proteins