DAPK3

Death-associated protein kinase 3

PDB rendering based on 1yrp.

Available structures
PDB	1YRP, 2J90, 3BHY, 3BQR

Identifiers

Symbols

DAPK3; FLJ36473; ZIP; ZIPK

External IDs

OMIM: 603289 MGI: 1203520 HomoloGene: 20353 GeneCards: DAPK3 Gene

EC number

2.7.11.1

Gene Ontology
Molecular function	• nucleotide binding • protein serine/threonine kinase activity • protein binding • ATP binding • leucine zipper domain binding
Cellular component	• nucleus • cytoplasm • PML body
Biological process	• protein phosphorylation • apoptosis • induction of apoptosis • induction of apoptosis • intracellular protein kinase cascade • chromatin modification • neuron differentiation
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 19:
3.96 – 3.97 Mb

Chr 10:
80.65 – 80.66 Mb

PubMed search

[1]

[2]

Death-associated protein kinase 3 is an enzyme that in humans is encoded by the DAPK3 gene.^[1]^[2]

1 Function
2 Interactions
3 References
4 Further reading

Function

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.^[2]

Unlike most other mammalian genes, murine (rat and mouse) DAPK3 has undergone accelerated evolution and diverged from the tightly conserved consensus that is maintained from fish to human^[3]

Interactions

DAPK3 has been shown to interact with PAWR^[4] and Death associated protein 6.^[4]

References

^ Kawai T, Matsumoto M, Takeda K, Sanjo H, Akira S (Mar 1998). "ZIP kinase, a novel serine/threonine kinase which mediates apoptosis". Mol Cell Biol 18 (3): 1642–51. PMC 108879. PMID 9488481. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=108879.
^ ^a ^b "Entrez Gene: DAPK3 death-associated protein kinase 3". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1613.
^ Shoval Y, Pietrokovski S, Kimchi A (October 2007). "ZIPK: a unique case of murine-specific divergence of a conserved vertebrate gene". PLoS Genet. 3 (10): 1884–93. doi:10.1371/journal.pgen.0030180. PMC 2041995. PMID 17953487. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2041995.
^ ^a ^b Kawai T, Akira S, Reed JC (September 2003). "ZIP kinase triggers apoptosis from nuclear PML oncogenic domains". Mol. Cell. Biol. 23 (17): 6174–86. doi:10.1128/MCB.23.17.6174-6186.2003. PMC 180930. PMID 12917339. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=180930.

Saito T, Seki N, Ohira M, et al. (1998). "Assignment of the ZIP kinase gene to human chromosome 19p13.3 by somatic hybrid analysis and fluorescence in-situ hybridization.". J. Hum. Genet. 43 (3): 209–11. doi:10.1007/s100380050073. PMID 9747039.
Murata-Hori M, Suizu F, Iwasaki T, et al. (1999). "ZIP kinase identified as a novel myosin regulatory light chain kinase in HeLa cells.". FEBS Lett. 451 (1): 81–4. doi:10.1016/S0014-5793(99)00550-5. PMID 10356987.
Page G, Lödige I, Kögel D, Scheidtmann KH (2000). "AATF, a novel transcription factor that interacts with Dlk/ZIP kinase and interferes with apoptosis.". FEBS Lett. 462 (1-2): 187–91. doi:10.1016/S0014-5793(99)01529-X. PMID 10580117.
Page G, Kögel D, Rangnekar V, Scheidtmann KH (2000). "Interaction partners of Dlk/ZIP kinase: co-expression of Dlk/ZIP kinase and Par-4 results in cytoplasmic retention and apoptosis.". Oncogene 18 (51): 7265–73. doi:10.1038/sj.onc.1203170. PMID 10602480.
Cariou B, Perdereau D, Cailliau K, et al. (2002). "The adapter protein ZIP binds Grb14 and regulates its inhibitory action on insulin signaling by recruiting protein kinase Czeta.". Mol. Cell. Biol. 22 (20): 6959–70. doi:10.1128/MCB.22.20.6959-6970.2002. PMC 139806. PMID 12242277. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139806.
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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Preuss U, Landsberg G, Scheidtmann KH (2003). "Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinase.". Nucleic Acids Res. 31 (3): 878–85. doi:10.1093/nar/gkg176. PMC 149197. PMID 12560483. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=149197.
Kawai T, Akira S, Reed JC (2003). "ZIP kinase triggers apoptosis from nuclear PML oncogenic domains.". Mol. Cell. Biol. 23 (17): 6174–86. doi:10.1128/MCB.23.17.6174-6186.2003. PMC 180930. PMID 12917339. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=180930.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Burch LR, Scott M, Pohler E, et al. (2004). "Phage-peptide display identifies the interferon-responsive, death-activated protein kinase family as a novel modifier of MDM2 and p21WAF1.". J. Mol. Biol. 337 (1): 115–28. doi:10.1016/j.jmb.2003.10.081. PMID 15001356.
Endo A, Surks HK, Mochizuki S, et al. (2004). "Identification and characterization of zipper-interacting protein kinase as the unique vascular smooth muscle myosin phosphatase-associated kinase.". J. Biol. Chem. 279 (40): 42055–61. doi:10.1074/jbc.M403676200. PMID 15292222.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
Schaaf CP, Benzing J, Schmitt T, et al. (2005). "Novel interaction partners of the TPR/MET tyrosine kinase.". FASEB J. 19 (2): 267–9. doi:10.1096/fj.04-1558fje. PMID 15546961.
Yu H, Jiang D, Guo Z, et al. (2005). "TCP10L is expressed specifically in spermatogenic cells and binds to death associated protein kinase-3.". Int. J. Androl. 28 (3): 163–70. doi:10.1111/j.1365-2605.2005.00522.x. PMID 15910542.
Shoval Y, Pietrokovski S, Kimchi A. (2007). "ZIPK: a unique case of murine-specific divergence of a conserved vertebrate gene.". PLoS Genet. 3 (10): 1884–93. doi:10.1371/journal.pgen.0030180. PMC 2041995. PMID 17953487. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2041995.
Takamoto N, Komatsu S, Komaba S, et al. (2007). "Novel ZIP kinase isoform lacks leucine zipper.". Arch. Biochem. Biophys. 456 (2): 194–203. doi:10.1016/j.abb.2006.09.026. PMC 2758612. PMID 17126281. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2758612.

PDB gallery

1yrp: Catalytic domain of human ZIP kinase phosphorylated at Thr265

2j90: CRYSTAL STRUCTURE OF HUMAN ZIP KINASE IN COMPLEX WITH A TETRACYCLIC PYRIDONE INHIBITOR (PYRIDONE 6)

Kinases: Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1, LATS2, MAST1, MAST2, STK38, STK38L, CIT, ROCK1, SGK, SGK2, SGK3, Protein kinase B (AKT1, AKT2, AKT3), Ataxia telangiectasia mutated, Mammalian target of rapamycin, EIF-2 kinases (PKR, HRI, EIF2AK3, EIF2AK4), Wee1 (WEE1)

Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1, PDK2, PDK3

Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α (PRKAA1, PRKAA2) · β (PRKAB1, PRKAB2) · γ (PRKAG1, PRKAG2, PRKAG3)

(3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)) (EC 2.7.11.4)	BCKDK, BCKDHA, BCKDHB

(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2, IDH3A, IDH3B, IDH3G

(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4

Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase (Aurora A kinase, Aurora B kinase)

Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK, STK10

Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-

IκB kinase (EC 2.7.11.10)	CHUK, IKK2, TBK1, IKBKE, IKBKG, IKBKAP

cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A, PRKACG, PRKACB, PRKACA, PRKY

cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G, PRKG1

Protein kinase C (EC 2.7.11.13)	Protein kinase C, Protein kinase Cζ, PKC alpha, PRKCB1, PRKCD, PRKCE, PRKCH, PRKCG, PRKCI, PRKCQ, Protein kinase N1, PKN2, PKN3,

Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase

Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase, Beta adrenergic receptor kinase-2

G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4, GRK5, GRK6

Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2, CAMK1, CAMK2A, CAMK2B, CAMK2D, CAMK2G, CAMK4, MLCK, CASK, CHEK1, CHEK2, DAPK1, DAPK2, DAPK3, STK11, MAPKAPK2, MAPKAPK3, MAPKAPK5, MARK1, MARK2, MARK3, MARK4, MELK, MKNK1, MKNK2, NUAK1, NUAK2, OBSCN, PASK, PHKG1, PHKG2, PIM1, PIM2, PKD1, PRKD2, PRKD3, PSKH1, SNF1LK2, KIAA0999, STK40, SNF1LK, SNRK, SPEG, TSSK2, Kalirin, TRIB1, TRIB2, TRIB3, TRIO, Titin, DCLK1

Myosin light-chain kinase (EC 2.7.11.18)	MYLK, MYLK2, MYLK3, MYLK4

Phosphorylase kinase (EC 2.7.11.19)	PHKA1, PHKA2, PHKB, PHKG1, PHKG2

Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K, STK19

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1, PLK2, PLK3, PLK4

Cyclin-dependent kinase (EC 2.7.11.22)	CDK1, CDK2, CDKL2, CDK3, CDK4, CDK5, CDKL5, CDK6, CDK7, CDK8, CDK9, CDK10, CDC2L5, CRKRS, PCTK1, PCTK2, PCTK3, PFTK1, CDC2L1

(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5, RPS6KA4, P70S6 kinase, P70-S6 Kinase 1, RPS6KB2, RPS6KA2, RPS6KA3, RPS6KA1, RPS6KC1

Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated (MAPK1, MAPK3, MAPK4, MAPK6, MAPK7, MAPK12, MAPK15), C-Jun N-terminal (MAPK8, MAPK9, MAPK10), P38 mitogen-activated protein (MAPK11, MAPK13, MAPK14)

MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases (MAP3K1, MAP3K2, MAP3K3, MAP3K4, MAP3K5, MAP3K6, MAP3K7, MAP3K8) RAFs (ARAF, BRAF, KSR1, KSR2), MLKs (MAP3K12, MAP3K13, MAP3K9, MAP3K10, MAP3K11, MAP3K7, ZAK), CDC7, MAP3K14

Tau-protein kinase (EC 2.7.11.26)	TPK1, TTK, GSK-3

(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)	-

Tropomyosin kinase (EC 2.7.11.28)	-

Low-density-lipoprotein receptor kinase (EC 2.7.11.29)	-

Receptor protein serine/threonine kinase (EC 2.7.11.30)	Bone morphogenetic protein receptors (BMPR1, BMPR1A, BMPR1B, BMPR2), ACVR1, ACVR1B, ACVR1C, ACVR2A, ACVR2B, ACVRL1, Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1, MAP2K2, MAP2K3, MAP2K4, MAP2K5, MAP2K6, MAP2K7

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6

DAPK3

Contents

Function

Interactions

References

Further reading