Rabbit anti-Human death-associated protein kinase 3 Polyclonal Antibody | anti-DAPK3 antibody
Rabbit anti-human death-associated protein kinase 3 polyclonal Antibody
NCBI and Uniprot Product Information
NCBI Description
Death-associated protein kinase 3 (DAPK3) induces morphological changes in apoptosis when overexpressed in mammalian cells. These results suggest that DAPK3 may play a role in the induction of apoptosis. [provided by RefSeq, Jul 2008]
Uniprot Description
DAPK3: Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, actin cytoskeleton reorganization, cell motility, smooth muscle contraction, and mitosis, particularly cytokinesis. Regulates both type I apoptotic and type II autophagic cell deaths signal, depending on the cellular setting. The former is caspase- dependent, while the latter is caspase-independent and is characterized by the accumulation of autophagic vesicles. 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, and the inhibition of SMPP1M functions to enhance muscle responsiveness to Ca(2+) and promote a contractile state. Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Phosphorylates STAT3 and enhances its transcriptional activity. Positively regulates the canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2. Can disrupt the NLK-TCF7L2 complex thereby influencing the phosphorylation of TCF7L2 by NLK. Phosphorylates histone H3 on 'Thr-11' at centromeres during mitosis. Involved in the formation of promyelocytic leukemia protein nuclear body (PML-NB), one of many subnuclear domains in the eukaryotic cell nucleus, and which is involved in oncogenesis and viral infection. Monomer and homotrimer. Can also exist as homodimer or form heterodimers with ATF4. Homodimerization is required for activation segment autophosphorylation Both interactions require an intact leucine zipper domain and oligomerization is required for full enzymatic activity. Also binds to DAXX and PAWR, possibly in a ternary complex which plays a role in caspase activation. According to PubMed:17953487, does not interact with PARW. Interacts with AATF, CDC5L, UBE2D1, UBE2D2 AND UBE2D3. Interacts with AR and this interaction is enhanced by AATF. Interacts (via leucine zipper) with TCP10L (via leucine zipper). Interacts (via kinase domain) with DAPK1 (via kinase domain).Interacts with STAT3, NLK and TCF7L2. Isoform 1 and isoform 2 can interact with myosin and PPP1R12A. Isoform 2 is expressed in the bladder smooth muscle. Inhibited by pyridone 6 (K00225), a potent, ATP-competitive inhibitor. Phosphorylation at Thr-180, Thr-225 and Thr-265 is essential for activity. Oligomerization is required for full enzymatic activity. Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. DAP kinase subfamily. 2 isoforms of the human protein are produced by alternative splicing.
Protein type: EC 2.7.11.1; Kinase, protein; Protein kinase, CAMK; Tumor suppressor; Protein kinase, Ser/Thr (non-receptor); CAMK group; DAPK family
Chromosomal Location of Human Ortholog: 19p13.3
Cellular Component: PML body; cytoplasm; nucleus; lipid raft
Molecular Function: identical protein binding; protein serine/threonine kinase activity; protein binding; leucine zipper domain binding; protein homodimerization activity; Rho GTPase binding; calmodulin-dependent protein kinase activity; cAMP response element binding protein binding; ATP binding
Biological Process: regulation of smooth muscle contraction; transcription, DNA-dependent; apoptosis; positive regulation of apoptosis; protein amino acid autophosphorylation; regulation of mitotic cell cycle; regulation of myosin II filament assembly or disassembly; cytokinesis; chromatin modification; protein amino acid phosphorylation; regulation of apoptosis; neuron differentiation; regulation of cell shape; regulation of transcription, DNA-dependent; negative regulation of translation; regulation of focal adhesion formation; regulation of mitosis; regulation of autophagy; positive regulation of cell migration