Sphk2
entrez
56632
canonical
uniprot
Q9JIA7
canonical
ensembl
ENSMUSG00000057342
resolver
ensp
ENSMUSP00000072615
resolver
ensp
ENSMUSP00000103366
resolver
ensp
ENSMUSP00000147391
resolver
ensp
ENSMUSP00000183033
resolver
ensp
ENSMUSP00000183042
resolver
ensp
ENSMUSP00000363548
resolver
enst
ENSMUST00000072836
resolver
enst
ENSMUST00000107737
resolver
enst
ENSMUST00000210060
resolver
genesymbol
Sphk2
resolver
uniprot
Q3U912
resolver
uniprot
Q58E38
resolver
uniprot
Q91VA9
resolver
uniprot
Q9DBH6
resolver
uniprot_entry
Q3U912_MOUSE
resolver
uniprot_entry
Q58E38_MOUSE
resolver
uniprot_entry
SPHK2_MOUSE
resolver
uniprot_sec
Q91VA9
resolver
uniprot_sec
Q9DBH6
resolver
amino_acid_sequence
MAPPPLLPVAASTPILHGEFGSYPANGPRFALTLTTQALHIQRLRPKPEARPRDGLVSLDEVSGCGTLQSRSPEDTAAYFCIYTYPRGRRGGRRRATRTFRADGATTYEENRAEAQRWATALTCLLRGVPLSGDQEITPELLPRKPRLLILVNPFGGRGLAWQRCMDHVVPMISEAGLSFNLIQTERQNHARELVQGLSLSEWEGIVTVSGDGLLYEVLNGLLDRPDWEDAVRMPIGVLPCGSGNALAGAVNHHGGFEQVVGVDLLLNCSLLLCRGGSHPLDLLSVTLASGSRCFSFLSVAWGFLSDVDIHSERFRALGSARFTLGAVLGLASLHTYRGRLSYLPATTEPALPIPGHSLPRAKSELVLAPAPAPAATHSPLHRSVSDLPLPLPQPALVSPGSPEPLPDLSLNGGGPELTGDWGGAGDAPLSPDPLLPSSPNALKTAQLSPIAEGPPEMPASSGFLPPTHSAPEASTWGPVDHLLPPLGSPLPQDWVTIEGEFVLMLGILPSHLCADLMAAPHARFDDGVVHLCWVRSGISRAALLRILLAMEHGNHFSLGCPHLGYAAARAFRLEPLTPRGLLTVDGELVEYGPIQAQVHPGLATLLTGPAGQKPQA
uniprot
proteins
ec_number
2.7.1.91
uniprot
proteins
function
FUNCTION: Catalyzes the phosphorylation of sphingosine to form sphingosine-1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions (PubMed:16118219, PubMed:17346996, PubMed:21084291). Also acts on D-erythro-dihydrosphingosine, D-erythro-sphingosine and L-threo-dihydrosphingosine. Binds phosphoinositides (PubMed:10751414, PubMed:16118219). In contrast to prosurvival SPHK1, has a positive effect on intracellular ceramide levels, inhibits cells growth and enhances apoptosis (PubMed:16118219). In mitochondria, is important for cytochrome-c oxidase assembly and mitochondrial respiration. The SPP produced in mitochondria binds PHB2 and modulates the regulation via PHB2 of complex IV assembly and respiration (PubMed:20959514). In nucleus, plays a role in epigenetic regulation of gene expression. Interacts with HDAC1 and HDAC2 and, through SPP production, inhibits their enzymatic activity, preventing the removal of acetyl groups from lysine residues with histones. Up-regulates acetylation of histone H3-K9, histone H4-K5 and histone H2B-K12. In nucleus, may have an inhibitory effect on DNA synthesis and cell cycle (By similarity). In mast cells, is the main regulator of SPP production which mediates calcium influx, NF-kappa-B activation, cytokine production, such as TNF and IL6, and degranulation of mast cells (PubMed:17346996). In dopaminergic neurons, is involved in promoting mitochondrial functions regulating ATP and ROS levels (PubMed:25637806). Also involved in the regulation of glucose and lipid metabolism (PubMed:30593892). {ECO:0000250|UniProtKB:Q9NRA0, ECO:0000269|PubMed:10751414, ECO:0000269|PubMed:16118219, ECO:0000269|PubMed:17346996, ECO:0000269|PubMed:20959514, ECO:0000269|PubMed:21084291, ECO:0000269|PubMed:25637806, ECO:0000269|PubMed:30593892}.
uniprot
proteins
mass_dalton
65618
uniprot
proteins
mutagenesis
MUTAGEN 93..94; /note="RR->EE: Loss of nuclear location. Loss of DNA synthesis inhibition."; /evidence="ECO:0000269|PubMed:12954646"; MUTAGEN 213; /note="G->E: Abolishes sphingosine kinase activity. Decreases apoptosis induction. Abolishes sphingosine kinase activity. No effect on endoplasmic reticulum location increase upon serum starvation. Abolishes sphingosine kinase activity and decreases apoptosis induction; when associated with A-219."; /evidence="ECO:0000269|PubMed:16118219"; MUTAGEN 219; /note="L->A: Strongly decreases sphingosine kinase activity. Decreases apoptosis induction. No effect on endoplasmic reticulum location increase upon serum starvation. Abolishes sphingosine kinase activity and decreases apoptosis induction; when associated with E-213."; /evidence="ECO:0000269|PubMed:16118219
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by PKD on Ser-384 and Ser-386 upon PMA treatment. Phosphorylation induces export from the nucleus to the cytoplasm. Phosphorylated by MAPK1 and MAPK2 at Thr-578, phosphorylation is induced by agonists such as EGF and PMA and increases kinase activity. {ECO:0000250|UniProtKB:Q9NRA0}.; PTM: Cleaved by CASP1 in apoptotic cells. The truncated form is released from cells. {ECO:0000250|UniProtKB:Q9NRA0}.
uniprot
proteins
pubmed
10751414
uniprot
proteins
pubmed
12954646
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16118219
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16314531
uniprot
proteins
pubmed
17346996
uniprot
proteins
pubmed
20959514
uniprot
proteins
pubmed
21084291
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
25637806
uniprot
proteins
pubmed
30593892
uniprot
proteins
sequence_length
617
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q9NRA0}. Cytoplasm {ECO:0000269|PubMed:12954646, ECO:0000269|PubMed:16118219}. Cell membrane {ECO:0000269|PubMed:16118219}. Endoplasmic reticulum {ECO:0000269|PubMed:16118219}. Nucleus {ECO:0000269|PubMed:12954646, ECO:0000269|PubMed:20959514}. Mitochondrion inner membrane {ECO:0000269|PubMed:20959514, ECO:0000269|PubMed:25637806}. Note=In nucleus, is located in nucleosomes where it associates with core histone proteins such as histone 3. In apoptotic cells, colocalizes with CASP1 in cell membrane where is cleaved and released from cells in an active form. {ECO:0000250|UniProtKB:Q9NRA0}.
uniprot
proteins