##gff-version 3 Q9NRA0 UniProtKB Chain 1 654 . . . ID=PRO_0000181358;Note=Sphingosine kinase 2 Q9NRA0 UniProtKB Domain 178 325 . . . Note=DAGKc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783 Q9NRA0 UniProtKB Region 1 175 . . . Note=Required for binding to sulfatide and phosphoinositides and for membrane localizatione;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19168031;Dbxref=PMID:19168031 Q9NRA0 UniProtKB Region 1 28 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9NRA0 UniProtKB Region 400 509 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9NRA0 UniProtKB Motif 122 130 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9JIA7 Q9NRA0 UniProtKB Motif 416 425 . . . Note=Nuclear export signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17635916;Dbxref=PMID:17635916 Q9NRA0 UniProtKB Compositional bias 1 15 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9NRA0 UniProtKB Active site 247 247 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NYA1 Q9NRA0 UniProtKB Binding site 188 190 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783 Q9NRA0 UniProtKB Binding site 220 224 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783 Q9NRA0 UniProtKB Binding site 245 248 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NYA1 Q9NRA0 UniProtKB Binding site 252 252 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783 Q9NRA0 UniProtKB Binding site 277 279 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783 Q9NRA0 UniProtKB Binding site 344 344 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9NYA1 Q9NRA0 UniProtKB Binding site 351 351 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783 Q9NRA0 UniProtKB Binding site 357 357 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783 Q9NRA0 UniProtKB Binding site 622 624 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00783 Q9NRA0 UniProtKB Modified residue 387 387 . . . Note=Phosphoserine%3B by MAPK;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:17311928,ECO:0007744|PubMed:23186163;Dbxref=PMID:17311928,PMID:23186163 Q9NRA0 UniProtKB Modified residue 393 393 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9JIA7 Q9NRA0 UniProtKB Modified residue 399 399 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q9NRA0 UniProtKB Modified residue 419 419 . . . Note=Phosphoserine%3B by PKD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17635916;Dbxref=PMID:17635916 Q9NRA0 UniProtKB Modified residue 421 421 . . . Note=Phosphoserine%3B by PKD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17635916;Dbxref=PMID:17635916 Q9NRA0 UniProtKB Modified residue 477 477 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 Q9NRA0 UniProtKB Modified residue 614 614 . . . Note=Phosphothreonine%3B by MAPK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17311928;Dbxref=PMID:17311928 Q9NRA0 UniProtKB Alternative sequence 1 36 . . . ID=VSP_006217;Note=In isoform 2 and isoform 3. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:10751414,ECO:0000303|PubMed:11230166,ECO:0000303|PubMed:14702039,ECO:0000303|PubMed:15489334;Dbxref=PMID:10751414,PMID:11230166,PMID:14702039,PMID:15489334 Q9NRA0 UniProtKB Alternative sequence 1 12 . . . ID=VSP_047721;Note=In isoform 5. MNGHLEAEEQQD->MIGCLHARVSGPLWDAGLCPASSRSAHTCLSLSVSDAPVSPATAPHCLLLSTAPAPPCPCHGVLNSHPFSPPFP;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.2 Q9NRA0 UniProtKB Alternative sequence 13 71 . . . ID=VSP_046910;Note=In isoform 4. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q9NRA0 UniProtKB Alternative sequence 292 390 . . . ID=VSP_006218;Note=In isoform 3. FEPALGLDLLLNCSLLLCRGGGHPLDLLSVTLASGSRCFSFLSVAWGFVSDVDIQSERFRALGSARFTLGTVLGLATLHTYRGRLSYLPATVEPASPTP->PREDSDSSTSSSACPLWTTARSCPRAAASMPGSCPLLPQQLALGFSRFIQDRVNGGGGRIGSLTCRGHTQRTLPAPAREGGGSLFLKNINVFICKKKKK;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q9NRA0 UniProtKB Alternative sequence 640 654 . . . ID=VSP_047722;Note=In isoform 5. GTLLTGPPGCPGREP->ARGRTQTPALPAAPALYGRQPGAAHGLQPVCQGAALFFHNSWLWGSQDLFRIVLTEAVGG;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.2 Q9NRA0 UniProtKB Natural variant 652 652 . . . ID=VAR_060112;Note=R->Q;Dbxref=dbSNP:rs11881285 Q9NRA0 UniProtKB Mutagenesis 138 138 . . . Note=Abolishes cleavage and secretion in apoptotic cells. No effect on kinase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20197547;Dbxref=PMID:20197547 Q9NRA0 UniProtKB Mutagenesis 212 212 . . . Note=Decreases SPP production in nucleus. Abolishes increase of histone acetylation. No effect on association with histone 3. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19729656;Dbxref=PMID:19729656 Q9NRA0 UniProtKB Mutagenesis 220 220 . . . Note=Loss of location to cell membrane. Not secreted. No effect on kinase activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20197547;Dbxref=PMID:20197547 Q9NRA0 UniProtKB Mutagenesis 387 387 . . . Note=Strongly reduces phosphorylation levels. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17311928;Dbxref=PMID:17311928 Q9NRA0 UniProtKB Mutagenesis 419 421 . . . Note=Abolishes nuclear export in response to PMA treatment. SVS->AVA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17635916;Dbxref=PMID:17635916 Q9NRA0 UniProtKB Mutagenesis 423 425 . . . Note=Abolishes nuclear export. LPL->APA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17635916;Dbxref=PMID:17635916 Q9NRA0 UniProtKB Mutagenesis 437 437 . . . Note=Reduces phosphorylation levels. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17311928;Dbxref=PMID:17311928 Q9NRA0 UniProtKB Mutagenesis 466 466 . . . Note=Reduces phosphorylation levels. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17311928;Dbxref=PMID:17311928 Q9NRA0 UniProtKB Mutagenesis 477 477 . . . Note=Reduces phosphorylation levels. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17311928;Dbxref=PMID:17311928 Q9NRA0 UniProtKB Mutagenesis 552 552 . . . Note=No effect on cleavage and secretion in apoptotic cells. No effect on kinase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20197547;Dbxref=PMID:20197547 Q9NRA0 UniProtKB Mutagenesis 614 614 . . . Note=Abolishes phosphorylation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17311928;Dbxref=PMID:17311928 Q9NRA0 UniProtKB Sequence conflict 49 49 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305