DAPK2

In this article we will explore DAPK2, a topic that has captured the attention of experts and hobbyists alike. With a rich and complex history, DAPK2 is a point of interest in different fields, from science and technology to culture and society. Over the years, DAPK2 has sparked significant debates, controversies and advances, playing a crucial role in the way we understand and experience the world around us. Through this article, we will take a closer look at the different facets of DAPK2, exploring its origins, its impact, and its relevance in today's world.

Protein-coding gene in the species Homo sapiens

DAPK2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1WMK, 1WRZ, 1Z9X, 1ZUZ, 1ZWS, 2A27, 2A2A, 2CKE
Identifiers
Aliases	DAPK2, DRP-1, DRP1, death-associated protein kinase 2, death associated protein kinase 2
External IDs	OMIM: 616567; MGI: 1341297; HomoloGene: 74940; GeneCards: DAPK2; OMA:DAPK2 - orthologs
Gene location (Human) Chr. Chromosome 15 (human)[1] Band 15q22.31 Start 63,907,036 bp[1] End 64,072,033 bp[1]
Gene location (Mouse) Chr. Chromosome 9 (mouse)[2] Band 9 C|9 35.75 cM Start 66,158,223 bp[2] End 66,272,242 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of thyroid gland left lobe of thyroid gland right auricle of heart right lung gastrocnemius muscle muscle of thigh upper lobe of left lung left ventricle blood sural nerve Top expressed in muscle of thigh membranous bone body of femur lumbar spinal ganglion Dermatocranium maxilla lip right lung right lung lobe tibiofemoral joint More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity nucleotide binding protein kinase activity calmodulin binding kinase activity protein serine/threonine kinase activity protein binding identical protein binding ATP binding Cellular component cytoplasm autophagosome lumen cytoplasmic vesicle Golgi apparatus intracellular membrane-bounded organelle nucleus Biological process regulation of apoptotic process intracellular signal transduction regulation of intrinsic apoptotic signaling pathway phosphorylation protein phosphorylation positive regulation of eosinophil chemotaxis regulation of autophagy anoikis positive regulation of neutrophil chemotaxis protein autophosphorylation neutrophil migration apoptotic process peptidyl-serine phosphorylation peptidyl-threonine phosphorylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 23604 13143 Ensembl ENSG00000035664 ENSMUSG00000032380 UniProt Q9UIK4 Q8VDF3 RefSeq (mRNA) NM_014326 NM_001363730 NM_001384997 NM_001384998 NM_001384999 NM_001385000 NM_010019 RefSeq (protein) NP_055141 NP_001350659 NP_034149 NP_001391612 Location (UCSC) Chr 15: 63.91 – 64.07 Mb Chr 9: 66.16 – 66.27 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Death-associated protein kinase 2 is an enzyme that in humans is encoded by the DAPK2 gene.^[5][6]

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. Gene overexpression induces cell apoptosis. It uses multiple polyadenylation sites.^[6]

The DAPK2 mRNA may undergo alternative splicing to produce a DAPK3-like encoding transcript.^[7]

References

1. ^ ^{a b c} GRCh38: Ensembl release 89: ENSG00000035664 – Ensembl, May 2017
2. ^ ^{a b c} GRCm38: Ensembl release 89: ENSMUSG00000032380 – Ensembl, May 2017
3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. ^ Kawai T, Nomura F, Hoshino K, Copeland NG, Gilbert DJ, Jenkins NA, Akira S (Jun 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. S2CID 19035227.
6. ^ ^{a b} "Entrez Gene: DAPK2 death-associated protein kinase 2".
7. ^ Shoval Y, Berissi H, Kimchi A, Pietrokovski S (2011). "New Modularity of DAP-Kinases: Alternative Splicing of the DRP-1 Gene Produces a ZIPk-Like Isoform". PLOS ONE. 6 (2): e17344. Bibcode:2011PLoSO...617344S. doi:10.1371/journal.pone.0017344. PMC 3050894. PMID 21408167.

Further reading

• 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. doi:10.1128/MCB.20.3.1044-1054.2000. PMC 85221. 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. PMC 145456. 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. PMC 2173279. 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. PMC 2375414. 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. 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. PMC 528928. 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. Bibcode:2005Sci...307.1621B. doi:10.1126/science.1105776. PMID 15761153. S2CID 39457788.
• 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.

This article on a gene on human chromosome 15 is a stub. You can help Wikipedia by expanding it.

• v
• t
• e