CERK

From Wikipedia, the free encyclopedia

Ceramide kinase

Identifiers

CERK; DKFZp434E0211; FLJ21430; FLJ23239; KIAA1646; LK4; MGC131878; dA59H18.2; dA59H18.3; hCERK

External IDs

OMIM: 610307 MGI: 2386052 HomoloGene: 11247

Gene ontology
Molecular Function:	• magnesium ion binding • ceramide kinase activity • diacylglycerol kinase activity • calmodulin-dependent protein kinase activity • calcium ion binding • kinase activity • transferase activity
Cellular Component:	• integral to membrane of membrane fraction
Biological Process:	• ceramide metabolic process • protein kinase C activation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_022766 (mRNA)
NP_073603 (protein)

XM_001002574 (mRNA)
XP_001002574 (protein)

Location

Chr 22: 45.46 - 45.51 Mb

Chr 15: 85.97 - 86.01 Mb

Pubmed search

[1]

[2]

Ceramide kinase, also known as CERK, is a human gene.^[1]

[edit] References

^ Entrez Gene: CERK ceramide kinase.

[edit] Further reading

Hinkovska-Galcheva VT, Boxer LA, Mansfield PJ, et al. (1999). "The formation of ceramide-1-phosphate during neutrophil phagocytosis and its role in liposome fusion.". J. Biol. Chem. 273 (50): 33203–9. PMID 9837889.
Dunham I, Shimizu N, Roe BA, et al. (1999). "The DNA sequence of human chromosome 22.". Nature 402 (6761): 489–95. doi:10.1038/990031. PMID 10591208.
Pitson SM, D'andrea RJ, Vandeleur L, et al. (2001). "Human sphingosine kinase: purification, molecular cloning and characterization of the native and recombinant enzymes.". Biochem. J. 350 Pt 2: 429–41. PMID 10947957.
Hirosawa M, Nagase T, Murahashi Y, et al. (2001). "Identification of novel transcribed sequences on human chromosome 22 by expressed sequence tag mapping.". DNA Res. 8 (1): 1–9. PMID 11258795.
Sugiura M, Kono K, Liu H, et al. (2002). "Ceramide kinase, a novel lipid kinase. Molecular cloning and functional characterization.". J. Biol. Chem. 277 (26): 23294–300. doi:10.1074/jbc.M201535200. PMID 11956206.
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.
Pettus BJ, Bielawska A, Spiegel S, et al. (2003). "Ceramide kinase mediates cytokine- and calcium ionophore-induced arachidonic acid release.". J. Biol. Chem. 278 (40): 38206–13. doi:10.1074/jbc.M304816200. PMID 12855693.
Mitsutake S, Kim TJ, Inagaki Y, et al. (2004). "Ceramide kinase is a mediator of calcium-dependent degranulation in mast cells.". J. Biol. Chem. 279 (17): 17570–7. doi:10.1074/jbc.M312885200. PMID 14769792.
Collins JE, Wright CL, Edwards CA, et al. (2005). "A genome annotation-driven approach to cloning the human ORFeome.". Genome Biol. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMID 15461802.
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.
Hinkovska-Galcheva V, Boxer LA, Kindzelskii A, et al. (2005). "Ceramide 1-phosphate, a mediator of phagocytosis.". J. Biol. Chem. 280 (28): 26612–21. doi:10.1074/jbc.M501359200. PMID 15899891.
Kim TJ, Mitsutake S, Kato M, Igarashi Y (2005). "The leucine 10 residue in the pleckstrin homology domain of ceramide kinase is crucial for its catalytic activity.". FEBS Lett. 579 (20): 4383–8. doi:10.1016/j.febslet.2005.06.079. PMID 16081073.
Wijesinghe DS, Massiello A, Subramanian P, et al. (2006). "Substrate specificity of human ceramide kinase.". J. Lipid Res. 46 (12): 2706–16. doi:10.1194/jlr.M500313-JLR200. PMID 16170208.
Van Overloop H, Gijsbers S, Van Veldhoven PP (2006). "Further characterization of mammalian ceramide kinase: substrate delivery and (stereo)specificity, tissue distribution, and subcellular localization studies.". J. Lipid Res. 47 (2): 268–83. doi:10.1194/jlr.M500321-JLR200. PMID 16269826.
Kim TJ, Mitsutake S, Igarashi Y (2006). "The interaction between the pleckstrin homology domain of ceramide kinase and phosphatidylinositol 4,5-bisphosphate regulates the plasma membrane targeting and ceramide 1-phosphate levels.". Biochem. Biophys. Res. Commun. 342 (2): 611–7. doi:10.1016/j.bbrc.2006.01.170. PMID 16488390.
Mitra P, Maceyka M, Payne SG, et al. (2007). "Ceramide kinase regulates growth and survival of A549 human lung adenocarcinoma cells.". FEBS Lett. 581 (4): 735–40. doi:10.1016/j.febslet.2007.01.041. PMID 17274985.
Lamour NF, Stahelin RV, Wijesinghe DS, et al. (2007). "Ceramide kinase uses ceramide provided by ceramide transport protein: localization to organelles of eicosanoid synthesis.". J. Lipid Res. 48 (6): 1293–304. doi:10.1194/jlr.M700083-JLR200. PMID 17392267.