SPHK1

From Wikipedia, the free encyclopedia

Sphingosine kinase 1

Identifiers

External IDs

OMIM: 603730 MGI: 1316649 HomoloGene: 40294

Gene ontology
Molecular Function:	• nucleotide binding • magnesium ion binding • DNA binding • diacylglycerol kinase activity • protein binding • calmodulin binding • ATP binding • sphinganine kinase activity • transferase activity • D-erythro-sphingosine kinase activity
Cellular Component:	• membrane fraction • soluble fraction • cytoplasm • cytosol
Biological Process:	• blood vessel development • sphingosine metabolic process • anti-apoptosis • G-protein coupled receptor protein signaling pathway • protein kinase C activation • intracellular signaling cascade • brain development • calcium-mediated signaling • positive regulation of cell growth • positive regulation of cell migration • positive regulation of angiogenesis • positive regulation of progression through mitotic cell cycle • positive regulation of smooth muscle contraction • sphingoid catabolic process • positive regulation of fibroblast proliferation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

NM_021972 (mRNA)
NP_068807 (protein)

NM_011451 (mRNA)
NP_035581 (protein)

Location

Chr 17: 71.89 - 71.9 Mb

Chr 11: 116.35 - 116.35 Mb

Pubmed search

[1]

[2]

Sphingosine kinase 1, also known as SPHK1, is a human gene.^[1]

Sphingosine-1-phosphate (SPP) is a novel lipid messenger with both intracellular and extracellular functions. Intracellularly, it regulates proliferation and survival, and extracellularly, it is a ligand for EDG1 (MIM 601974). Various stimuli increase cellular levels of SPP by activation of sphingosine kinase (SPHK), the enzyme that catalyzes the phosphorylation of sphingosine. Competitive inhibitors of SPHK block formation of SPP and selectively inhibit cellular proliferation induced by a variety of factors, including platelet-derived growth factor (e.g., MIM 173430) and serum.[supplied by OMIM]^[1]

[edit] References

^ ^a ^b Entrez Gene: SPHK1 sphingosine kinase 1.

[edit] Further reading

Tsukahara T, Mizuno H, Igarashi Y (2002). "[Molecular diversity of sphingosine kinase]". Tanpakushitsu Kakusan Koso 47 (4 Suppl): 509-13. PMID 11915350.
Sudo K, Chinen K, Nakamura Y (1995). "2058 expressed sequence tags (ESTs) from a human fetal lung cDNA library.". Genomics 24 (2): 276-9. doi:10.1006/geno.1994.1616. PMID 7698749.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171-4. PMID 8125298.
Hillier LD, Lennon G, Becker M, et al. (1997). "Generation and analysis of 280,000 human expressed sequence tags.". Genome Res. 6 (9): 807-28. PMID 8889549.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149-56. PMID 9373149.
Kohama T, Olivera A, Edsall L, et al. (1998). "Molecular cloning and functional characterization of murine sphingosine kinase.". J. Biol. Chem. 273 (37): 23722-8. PMID 9726979.
Liu H, Sugiura M, Nava VE, et al. (2000). "Molecular cloning and functional characterization of a novel mammalian sphingosine kinase type 2 isoform.". J. Biol. Chem. 275 (26): 19513-20. doi:10.1074/jbc.M002759200. PMID 10751414.
Nava VE, Lacana E, Poulton S, et al. (2000). "Functional characterization of human sphingosine kinase-1.". FEBS Lett. 473 (1): 81-4. PMID 10802064.
Melendez AJ, Carlos-Dias E, Gosink M, et al. (2000). "Human sphingosine kinase: molecular cloning, functional characterization and tissue distribution.". Gene 251 (1): 19-26. PMID 10863092.
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.
Xia P, Wang L, Moretti PA, et al. (2002). "Sphingosine kinase interacts with TRAF2 and dissects tumor necrosis factor-alpha signaling.". J. Biol. Chem. 277 (10): 7996-8003. doi:10.1074/jbc.M111423200. PMID 11777919.
Melendez AJ, Khaw AK (2002). "Dichotomy of Ca2+ signals triggered by different phospholipid pathways in antigen stimulation of human mast cells.". J. Biol. Chem. 277 (19): 17255-62. doi:10.1074/jbc.M110944200. PMID 11856736.
Hayashi S, Okada T, Igarashi N, et al. (2002). "Identification and characterization of RPK118, a novel sphingosine kinase-1-binding protein.". J. Biol. Chem. 277 (36): 33319-24. doi:10.1074/jbc.M201442200. PMID 12077123.
Lacaná E, Maceyka M, Milstien S, Spiegel S (2002). "Cloning and characterization of a protein kinase A anchoring protein (AKAP)-related protein that interacts with and regulates sphingosine kinase 1 activity.". J. Biol. Chem. 277 (36): 32947-53. doi:10.1074/jbc.M202841200. PMID 12080051.
Johnson KR, Becker KP, Facchinetti MM, et al. (2002). "PKC-dependent activation of sphingosine kinase 1 and translocation to the plasma membrane. Extracellular release of sphingosine-1-phosphate induced by phorbol 12-myristate 13-acetate (PMA).". J. Biol. Chem. 277 (38): 35257-62. doi:10.1074/jbc.M203033200. PMID 12124383.
Pitson SM, Moretti PA, Zebol JR, et al. (2003). "The nucleotide-binding site of human sphingosine kinase 1.". J. Biol. Chem. 277 (51): 49545-53. doi:10.1074/jbc.M206687200. PMID 12393916.
Nava VE, Hobson JP, Murthy S, et al. (2002). "Sphingosine kinase type 1 promotes estrogen-dependent tumorigenesis of breast cancer MCF-7 cells.". Exp. Cell Res. 281 (1): 115-27. PMID 12441135.
MacKinnon AC, Buckley A, Chilvers ER, et al. (2002). "Sphingosine kinase: a point of convergence in the action of diverse neutrophil priming agents.". J. Immunol. 169 (11): 6394-400. PMID 12444147.
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.