ZAK

ZAK
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 5HES
Identifiers
Aliases	ZAK, AZK, MLK7, MLT, MLTK, MRK, mlklak, pk, SFMMP, sterile alpha motif and leucine zipper containing kinase AZK
External IDs	MGI: 2443258 HomoloGene: 32331 GeneCards: ZAK
Gene ontology Molecular function • transferase activity • nucleotide binding • protein kinase activity • metal ion binding • kinase activity • protein serine/threonine kinase activity • protein binding • poly(A) RNA binding • MAP kinase kinase kinase activity • ATP binding • magnesium ion binding Cellular component • cytoplasm • nucleus Biological process • cell differentiation • intracellular signal transduction • cell cycle checkpoint • activation of JUN kinase activity • phosphorylation • activation of MAPKK activity • DNA damage checkpoint • response to stress • cell death • protein phosphorylation • cytoskeleton organization • cell cycle arrest • positive regulation of apoptotic process • cell cycle • response to radiation • cell proliferation • limb development • embryonic digit morphogenesis Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	51776	65964
Ensembl	ENSG00000091436	ENSMUSG00000004085
UniProt	Q9NYL2	Q9ESL4
RefSeq (mRNA)	NM_016653 NM_133646	NM_001164791 NM_023057 NM_178084
RefSeq (protein)	NP_057737.2 NP_598407.1	NP_001158263.1 NP_075544.1 NP_835185.2
Location (UCSC)	Chr 2: 173.08 – 173.27 Mb	Chr 2: 72.29 – 72.44 Mb
PubMed search	[1]	[2]
Wikidata

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Sterile alpha motif and leucine zipper containing kinase AZK, also known as ZAK, is a human gene.^[3]

This gene is a member of the MAPKKK family of signal transduction molecules and encodes a protein with an N-terminal kinase catalytic domain, followed by a leucine zipper motif and a sterile-alpha motif (SAM). This magnesium-binding protein forms homodimers and is located in the cytoplasm. The protein mediates gamma radiation signaling leading to cell cycle arrest and activity of this protein plays a role in cell cycle checkpoint regulation in cells. The protein also has pro-apoptotic activity. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.^[3]

Interactions

ZAK has been shown to interact with ZNF33A.^[4]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. "Entrez Gene: ZAK sterile alpha motif and leucine zipper containing kinase AZK".
4. Yang, Jaw-Ji (Jan 2003). "A novel zinc finger protein, ZZaPK, interacts with ZAK and stimulates the ZAK-expressing cells re-entering the cell cycle". Biochem. Biophys. Res. Commun. United States. 301 (1): 71–7. doi:10.1016/S0006-291X(02)02980-7. ISSN 0006-291X. PMID 12535642.

Further reading

• Liu TC, Huang CJ, Chu YC, et al. (2000). "Cloning and expression of ZAK, a mixed lineage kinase-like protein containing a leucine-zipper and a sterile-alpha motif.". Biochem. Biophys. Res. Commun. 274 (3): 811–6. doi:10.1006/bbrc.2000.3236. PMID 10924358.
• Gotoh I, Adachi M, Nishida E (2001). "Identification and characterization of a novel MAP kinase kinase kinase, MLTK.". J. Biol. Chem. 276 (6): 4276–86. doi:10.1074/jbc.M008595200. PMID 11042189.
• Bloem LJ, Pickard TR, Acton S, et al. (2002). "Tissue distribution and functional expression of a cDNA encoding a novel mixed lineage kinase.". J. Mol. Cell. Cardiol. 33 (9): 1739–50. doi:10.1006/jmcc.2001.1437. PMID 11549352.
• Gross EA, Callow MG, Waldbaum L, et al. (2002). "MRK, a mixed lineage kinase-related molecule that plays a role in gamma-radiation-induced cell cycle arrest.". J. Biol. Chem. 277 (16): 13873–82. doi:10.1074/jbc.M111994200. PMID 11836244.
• Yang JJ (2002). "Mixed lineage kinase ZAK utilizing MKK7 and not MKK4 to activate the c-Jun N-terminal kinase and playing a role in the cell arrest.". Biochem. Biophys. Res. Commun. 297 (1): 105–10. doi:10.1016/S0006-291X(02)02123-X. PMID 12220515.
• 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.
• Yang JJ (2003). "A novel zinc finger protein, ZZaPK, interacts with ZAK and stimulates the ZAK-expressing cells re-entering the cell cycle.". Biochem. Biophys. Res. Commun. 301 (1): 71–7. doi:10.1016/S0006-291X(02)02980-7. PMID 12535642.
• Takahashi M, Gotoh Y, Isagawa T, et al. (2004). "Regulation of a mitogen-activated protein kinase kinase kinase, MLTK by PKN.". J. Biochem. 133 (2): 181–7. doi:10.1093/jb/mvg022. PMID 12761180.
• 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.
• Cho YY, Bode AM, Mizuno H, et al. (2004). "A novel role for mixed-lineage kinase-like mitogen-activated protein triple kinase alpha in neoplastic cell transformation and tumor development.". Cancer Res. 64 (11): 3855–64. doi:10.1158/0008-5472.CAN-04-0201. PMID 15172994.
• Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization.". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
• Tosti E, Waldbaum L, Warshaw G, et al. (2005). "The stress kinase MRK contributes to regulation of DNA damage checkpoints through a p38gamma-independent pathway.". J. Biol. Chem. 279 (46): 47652–60. doi:10.1074/jbc.M409961200. PMID 15342622.
• Huang CY, Kuo WW, Chueh PJ, et al. (2004). "Transforming growth factor-beta induces the expression of ANF and hypertrophic growth in cultured cardiomyoblast cells through ZAK.". Biochem. Biophys. Res. Commun. 324 (1): 424–31. doi:10.1016/j.bbrc.2004.09.067. PMID 15465036.
• Huang CY, Chueh PJ, Tseng CT, et al. (2004). "ZAK re-programs atrial natriuretic factor expression and induces hypertrophic growth in H9c2 cardiomyoblast cells.". Biochem. Biophys. Res. Commun. 324 (3): 973–80. doi:10.1016/j.bbrc.2004.09.156. PMID 15485649.
• 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.
• Choi HS, Choi BY, Cho YY, et al. (2005). "Phosphorylation of Ser28 in histone H3 mediated by mixed lineage kinase-like mitogen-activated protein triple kinase alpha.". J. Biol. Chem. 280 (14): 13545–53. doi:10.1074/jbc.M410521200. PMID 15684425.
• Wang X, Mader MM, Toth JE, et al. (2005). "Complete inhibition of anisomycin and UV radiation but not cytokine induced JNK and p38 activation by an aryl-substituted dihydropyrrolopyrazole quinoline and mixed lineage kinase 7 small interfering RNA.". J. Biol. Chem. 280 (19): 19298–305. doi:10.1074/jbc.M413059200. PMID 15737997.
• Benzinger A, Muster N, Koch HB, et al. (2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer.". Mol. Cell Proteomics. 4 (6): 785–95. doi:10.1074/mcp.M500021-MCP200. PMID 15778465.
• Hillier LW, Graves TA, Fulton RS, et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4.". Nature. 434 (7034): 724–31. doi:10.1038/nature03466. PMID 15815621.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.