SPHK2

Sphingosine kinase 2

Identifiers

SPHK2 ; SK 2; SK-2; SPK 2; SPK-2

External IDs

OMIM: 607092 HomoloGene: 32456 IUPHAR: 2205 ChEMBL: 3023 GeneCards: SPHK2 Gene

2.7.1.91

Gene ontology
Molecular function	• protein binding • ATP binding • sphinganine kinase activity • Ras GTPase binding • D-erythro-sphingosine kinase activity • sphingosine-1-phosphate receptor activity
Cellular component	• lysosomal membrane • cytosol • membrane
Biological process	• blood vessel development • sphingosine-1-phosphate signaling pathway • sphingolipid metabolic process • sphinganine-1-phosphate biosynthetic process • brain development • female pregnancy • cell proliferation • positive regulation of cell proliferation • sphingolipid biosynthetic process • negative regulation of apoptotic process • small molecule metabolic process • sphingosine biosynthetic process • lipid phosphorylation
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 19:
48.62 – 48.63 Mb

Chr 7:
45.71 – 45.72 Mb

PubMed search

Sphingosine kinase 2 is a protein that in humans is encoded by the SPHK2 gene.^[1]

This gene encodes one of two sphingosine kinase isozymes that catalyze the phosphorylation of sphingosine into sphingosine 1-phosphate. Sphingosine 1-phosphate mediates many cellular processes including migration, proliferation and apoptosis, and also plays a role in several types of cancer by promoting angiogenesis and tumorigenesis. The encoded protein may play a role in breast cancer proliferation and chemoresistance. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Aug 2011].^[1]

References

1 2 "Entrez Gene: Sphingosine kinase 2". Retrieved 2011-12-22.

Liu, H.; Sugiura, M.; Nava, V. E.; Edsall, L. C.; Kono, K.; Poulton, S.; Milstien, S.; Kohama, T.; Spiegel, S. (2000). "Molecular Cloning and Functional Characterization of a Novel Mammalian Sphingosine Kinase Type 2 Isoform". Journal of Biological Chemistry 275 (26): 19513–19520. doi:10.1074/jbc.M002759200. PMID 10751414.
Xia, P.; Wang, L.; Moretti, P. A.; Albanese, N.; Chai, F.; Pitson, S. M.; d'Andrea, R. J.; Gamble, J. R.; Vadas, M. A. (2002). "Sphingosine Kinase Interacts with TRAF2 and Dissects Tumor Necrosis Factor-alpha Signaling". Journal of Biological Chemistry 277 (10): 7996–8003. doi:10.1074/jbc.M111423200. PMID 11777919.
Shu, X.; Wu, W.; Mosteller, R. D.; Broek, D. (2002). "Sphingosine Kinase Mediates Vascular Endothelial Growth Factor-Induced Activation of Ras and Mitogen-Activated Protein Kinases". Molecular and Cellular Biology 22 (22): 7758–7768. doi:10.1128/mcb.22.22.7758-7768.2002. PMC 134718. PMID 12391145.
Paugh, S. W.; Payne, S. G.; Barbour, S. E.; Milstien, S.; Spiegel, S. (2003). "The immunosuppressant FTY720 is phosphorylated by sphingosine kinase type 2". FEBS Letters 554 (1–2): 189–193. doi:10.1016/S0014-5793(03)01168-2. PMID 14596938.
Hait, N. C.; Sarkar, S.; Le Stunff, H.; Mikami, A.; MacEyka, M.; Milstien, S.; Spiegel, S. (2005). "Role of Sphingosine Kinase 2 in Cell Migration toward Epidermal Growth Factor". Journal of Biological Chemistry 280 (33): 29462–29469. doi:10.1074/jbc.M502922200. PMID 15951439.
Okada, T.; Ding, G.; Sonoda, H.; Kajimoto, T.; Haga, Y.; Khosrowbeygi, A.; Gao, S.; Miwa, N.; Jahangeer, S.; Nakamura, S. (2005). "Involvement of N-terminal-extended Form of Sphingosine Kinase 2 in Serum-dependent Regulation of Cell Proliferation and Apoptosis". Journal of Biological Chemistry 280 (43): 36318–36325. doi:10.1074/jbc.M504507200. PMID 16103110.
Olivera, A.; Urtz, N.; Mizugishi, K.; Yamashita, Y.; Gilfillan, A. M.; Furumoto, Y.; Gu, H.; Proia, R. L.; Baumruker, T.; Rivera, J. (2005). "IgE-dependent Activation of Sphingosine Kinases 1 and 2 and Secretion of Sphingosine 1-Phosphate Requires Fyn Kinase and Contributes to Mast Cell Responses". Journal of Biological Chemistry 281 (5): 2515–2525. doi:10.1074/jbc.M508931200. PMID 16316995.
Sun, J.; Yan, G.; Ren, A.; You, B.; Liao, J. K. (2006). "FHL2/SLIM3 Decreases Cardiomyocyte Survival by Inhibitory Interaction with Sphingosine Kinase-1". Circulation Research 99 (5): 468–476. doi:10.1161/01.RES.0000239410.65551.b3. PMC 2614439. PMID 16888242.
Hait, N. C.; Bellamy, A.; Milstien, S.; Kordula, T.; Spiegel, S. (2006). "Sphingosine Kinase Type 2 Activation by ERK-mediated Phosphorylation". Journal of Biological Chemistry 282 (16): 12058–12065. doi:10.1074/jbc.M609559200. PMID 17311928.
Ding, G.; Sonoda, H.; Yu, H.; Kajimoto, T.; Goparaju, S. K.; Jahangeer, S.; Okada, T.; Nakamura, S. -I. (2007). "Protein Kinase D-mediated Phosphorylation and Nuclear Export of Sphingosine Kinase 2". Journal of Biological Chemistry 282 (37): 27493–27502. doi:10.1074/jbc.M701641200. PMID 17635916.

Transferases: phosphorus-containing groups (EC 2.7)

2.7.1-2.7.4:
phosphotransferase/kinase
(PO₄)

2.7.1: OH acceptor	Hexo- Gluco- Fructo- Hepatic Galacto- Phosphofructo- 1 Liver Muscle Platelet 2 Riboflavin Shikimate Thymidine ADP-thymidine NAD⁺ Glycerol Pantothenate Mevalonate Pyruvate Deoxycytidine PFP Diacylglycerol Phosphoinositide 3 Class I PI 3 Class II PI 3 Sphingosine Glucose-1,6-bisphosphate synthase

2.7.2: COOH acceptor	Phosphoglycerate Aspartate kinase

2.7.3: N acceptor	Creatine

2.7.4: PO₄ acceptor	Phosphomevalonate Adenylate Nucleoside-diphosphate Uridylate Guanylate Thiamine-diphosphate

2.7.6: diphosphotransferase
(P₂O₇)

2.7.7: nucleotidyltransferase
(PO₄-nucleoside)

Polymerase

DNA polymerase	DNA-directed DNA polymerase I II III IV V RNA-directed DNA polymerase Reverse transcriptase Telomerase DNA nucleotidylexotransferase/Terminal deoxynucleotidyl transferase

RNA nucleotidyltransferase	RNA polymerase/DNA-directed RNA polymerase RNA polymerase I RNA polymerase II RNA polymerase III RNA polymerase IV Primase RNA-dependent RNA polymerase PNPase

Phosphorolytic
3' to 5' exoribonuclease

Nucleotidyltransferase

Guanylyltransferase

mRNA capping enzyme

Other

2.7.8: miscellaneous

Phosphatidyltransferases	CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase CDP-diacylglycerol—serine O-phosphatidyltransferase CDP-diacylglycerol—inositol 3-phosphatidyltransferase CDP-diacylglycerol—choline O-phosphatidyltransferase

Glycosyl-1-phosphotransferase	N-acetylglucosamine-1-phosphate transferase

2.7.10-2.7.13: protein kinase
(PO₄; protein acceptor)

2.7.10: protein-tyrosine	see tyrosine kinases

2.7.11: protein-serine/threonine	see serine/threonine-specific protein kinases

2.7.12: protein-dual-specificity	see serine/threonine-specific protein kinases

2.7.13: protein-histidine	Protein-histidine pros-kinase Protein-histidine tele-kinase Histidine kinase

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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SPHK2

References

Further reading