SPHK2

Identifiers

SPHK2, SK 2, SK-2, SPK 2, SPK-2, sphingosine kinase 2

External IDs

MGI: 1861380 HomoloGene: 32456 GeneCards: SPHK2

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

Orthologs

Species

Human

Mouse

Entrez


56848


56632

Ensembl


ENSG00000063176


ENSMUSG00000057342

UniProt


Q9NRA0


Q9JIA7

RefSeq (mRNA)


NM_001204158 NM_001204159 NM_001204160 NM_001243876 NM_020126


NM_001172561 NM_020011 NM_203280

RefSeq (protein)


NP_001191087.1 NP_001191088.1 NP_001191089.1 NP_064511.2


NP_001166032.1 NP_064395.2 NP_975009.1

Location (UCSC)

Chr 19: 48.62 – 48.63 Mb

Chr 7: 45.71 – 45.72 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Sphingosine kinase 2 is a protein that in humans is encoded by the SPHK2 gene.^[3]

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].^[3]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
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

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