NP_055141.2
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NCBI GenBank Nucleotide #
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UniProt Primary Accession #
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UniProt Secondary Accession #
UniProt Related Accession #
NCBI Official Full Name
death-associated protein kinase 2
NCBI Official Synonym Full Names
death-associated protein kinase 2
NCBI Official Synonym Symbols
NCBI Protein Information
death-associated protein kinase 2; DAP kinase 2; DAP-kinase-related protein 1 beta isoform
UniProt Protein Name
Death-associated protein kinase 2
UniProt Synonym Protein Names
DAP-kinase-related protein 1
UniProt Synonym Gene Names
UniProt Entry Name
DAPK2_HUMAN
NCBI Summary for DAPK2
This gene encodes a protein that belongs to the serine/threonine protein kinase family. This protein contains a N-terminal protein kinase domain followed by a conserved calmodulin-binding domain with significant similarity to that of death-associated protein kinase 1 (DAPK1), a positive regulator of programmed cell death. Overexpression of this gene was shown to induce cell apoptosis. It uses multiple polyadenylation sites. [provided by RefSeq, Jul 2008]
UniProt Comments for DAPK2
Function: Calcium/calmodulin-dependent serine/threonine kinase involved in multiple cellular signaling pathways that trigger cell survival, apoptosis, and autophagy. 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. Acts as a mediator of anoikis and a suppressor of beta-catenin-dependent anchorage-independent growth of malignant epithelial cells. May play a role in granulocytic maturation. Ref.1 Ref.2 Ref.3 Ref.6 Ref.8 Ref.10 Ref.12Isoform 2 is not regulated by calmodulin. It can phosphorylate MYL9. It can induce membrane blebbing and autophagic cell death. Ref.1 Ref.2 Ref.3 Ref.6 Ref.8 Ref.10 Ref.12
Catalytic activity: ATP + a protein = ADP + a phosphoprotein.
Cofactor: Magnesium.
Enzyme regulation: Activated by Ca2+/calmodulin. Regulated by a double locking mechanism, involving autophosphorylation at Ser-318, calmodulin binding, and dimerization. In the inactive state, Ser-318 is phosphorylated, and the kinase is dimeric. Activation involves: dephosphorylation at Ser-318, release-of-autoinhibition mechanism where calmodulin binding induces a conformational change that relieves the steric block of the active site by the autoinhibitory domain, and generation of the monomeric active form of the kinase. Ref.1
Subunit structure: Homodimer in its autoinhibited state. Active as monomer
By similarity. Isoform 2 but not isoform 1 can interact with ATF4. Ref.2 Ref.6
Subcellular location: Cytoplasm. Cytoplasmic vesicle › autophagosome lumen Ref.2 Ref.8.
Tissue specificity: Isoform 2 is expressed in embryonic stem cells (at protein level). Isoform 1 is ubiquitously expressed in all tissue types examined with high levels in heart, lung and skeletal muscle. It is expressed abundantly in cells differentiated toward granulocytes and low in undifferentiated, normal and leukemic hematopoietic cells and monocytes/macrophages. Ref.1 Ref.3 Ref.10
Induction: Up-regulated during granulocytic maturation. Ref.1 Ref.10
Domain: The autoinhibitory domain sterically blocks the substrate peptide-binding site by making both hydrophobic and electrostatic contacts with the kinase core
By similarity.
Post-translational modification: Autophosphorylation at Ser-318 inhibits its catalytic activity. Dephosphorylated at Ser-318 in response to activated Fas and TNF-alpha receptors. Ref.6
Sequence similarities: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. DAP kinase subfamily.Contains 1 protein kinase domain.
Research Articles on DAPK2
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Products associated with DAPK2 peptide
Pathways associated with DAPK2 peptide
Diseases associated with DAPK2 peptide
Organs/Tissues associated with DAPK2 peptide
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