DAPK2

From Wikipedia, the free encyclopedia

Death-associated protein kinase 2

PDB rendering based on 1wmk.

Available structures: 1wmk, 1z9x, 1zws, 2a27, 2a2a, 2cke

Identifiers

Symbol(s)

DAPK2; DRP-1; MGC119312

External IDs

MGI: 1341297 HomoloGene: 74940

Gene ontology
Molecular Function:	• nucleotide binding • protein kinase activity • calmodulin-dependent protein kinase activity • calmodulin binding • ATP binding • transferase activity • identical protein binding
Cellular Component:	• cytoplasm
Biological Process:	• protein amino acid phosphorylation • apoptosis • induction of apoptosis • protein kinase cascade

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_014326 (mRNA)
NP_055141 (protein)

NM_010019 (mRNA)
NP_034149 (protein)

Location

Chr 15: 61.99 - 62.12 Mb

Chr 9: 65.96 - 66.07 Mb

Pubmed search

[1]

[2]

Death-associated protein kinase 2, also known as DAPK2, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: DAPK2 death-associated protein kinase 2.

[edit] Further reading

Kawai T, Nomura F, Hoshino K, et al. (1999). "Death-associated protein kinase 2 is a new calcium/calmodulin-dependent protein kinase that signals apoptosis through its catalytic activity.". Oncogene 18 (23): 3471–80. doi:10.1038/sj.onc.1202701. PMID 10376525.
Inbal B, Shani G, Cohen O, et al. (2000). "Death-associated protein kinase-related protein 1, a novel serine/threonine kinase involved in apoptosis.". Mol. Cell. Biol. 20 (3): 1044–54. PMID 10629061.
Shani G, Henis-Korenblit S, Jona G, et al. (2001). "Autophosphorylation restrains the apoptotic activity of DRP-1 kinase by controlling dimerization and calmodulin binding.". EMBO J. 20 (5): 1099–113. doi:10.1093/emboj/20.5.1099. PMID 11230133.
Wong TS, Chang HW, Tang KC, et al. (2002). "High frequency of promoter hypermethylation of the death-associated protein-kinase gene in nasopharyngeal carcinoma and its detection in the peripheral blood of patients.". Clin. Cancer Res. 8 (2): 433–7. PMID 11839660.
Chan MW, Chan LW, Tang NL, et al. (2002). "Hypermethylation of multiple genes in tumor tissues and voided urine in urinary bladder cancer patients.". Clin. Cancer Res. 8 (2): 464–70. PMID 11839665.
Inbal B, Bialik S, Sabanay I, et al. (2002). "DAP kinase and DRP-1 mediate membrane blebbing and the formation of autophagic vesicles during programmed cell death.". J. Cell Biol. 157 (3): 455–68. doi:10.1083/jcb.200109094. PMID 11980920.
Satoh A, Toyota M, Itoh F, et al. (2002). "DNA methylation and histone deacetylation associated with silencing DAP kinase gene expression in colorectal and gastric cancers.". Br. J. Cancer 86 (11): 1817–23. doi:10.1038/sj.bjc.6600319. PMID 12087472.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Barrios-Rodiles M, Brown KR, Ozdamar B, et al. (2005). "High-throughput mapping of a dynamic signaling network in mammalian cells.". Science 307 (5715): 1621–5. doi:10.1126/science.1105776. PMID 15761153.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
Rizzi M, Tschan MP, Britschgi C, et al. (2007). "The death-associated protein kinase 2 is up-regulated during normal myeloid differentiation and enhances neutrophil maturation in myeloid leukemic cells.". J. Leukoc. Biol. 81 (6): 1599–608. doi:10.1189/jlb.0606400. PMID 17347302.