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Sphingolipid long chain base-responsive protein PIL1

 PIL1_YEAST              Reviewed;         339 AA.
P53252; D6VUL8;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
26-FEB-2020, entry version 154.
RecName: Full=Sphingolipid long chain base-responsive protein PIL1;
Name=PIL1; OrderedLocusNames=YGR086C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
G3 (Bethesda) 4:389-398(2014).
[3]
PROTEIN SEQUENCE OF 45-56; 85-103; 166-192 AND 197-221, AND IDENTIFICATION
BY MASS SPECTROMETRY.
Bienvenut W.V., Peters C.;
Submitted (JUN-2005) to UniProtKB.
[4]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[6]
FUNCTION, AND PHOSPHORYLATION BY PKH1 AND PHK2.
PubMed=15016821; DOI=10.1074/jbc.m400299200;
Zhang X., Lester R.L., Dickson R.C.;
"Pil1p and Lsp1p negatively regulate the 3-phosphoinositide-dependent
protein kinase-like kinase Pkh1p and downstream signaling pathways Pkc1p
and Ypk1p.";
J. Biol. Chem. 279:22030-22038(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-233, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone signaling
pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND THR-233, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-233, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 76625 / YPH499;
PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
"Profiling phosphoproteins of yeast mitochondria reveals a role of
phosphorylation in assembly of the ATP synthase.";
Mol. Cell. Proteomics 6:1896-1906(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163; SER-230 AND THR-233, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome
analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; SER-16; SER-45; SER-98;
SER-163; THR-233 AND SER-299, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides insights
into evolution.";
Science 325:1682-1686(2009).
[12]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-29, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
-!- FUNCTION: Negative regulator of cell wall integrity (CWI) in unstressed
cells, probably by inhibiting protein kinase PKH1/PHK2 activity and
regulating their downstream CWI pathways PKC1-MAP kinase pathway and
protein kinase YPK1 pathway. Activity may be regulated by the transient
increase of sphingolipid long chain bases (LCBs) during heat stress.
{ECO:0000269|PubMed:15016821}.
-!- INTERACTION:
Q05050:EIS1; NbExp=3; IntAct=EBI-23225, EBI-28061;
Q12230:LSP1; NbExp=6; IntAct=EBI-23225, EBI-34978;
P35719:MRP8; NbExp=3; IntAct=EBI-23225, EBI-16255;
Q03407:PKH1; NbExp=4; IntAct=EBI-23225, EBI-32467;
-!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:14562095}.
-!- PTM: Phosphorylated by PKH1 and PKH2. Phosphorylation is inhibited by
sphingolipid long chain bases (LCBs). {ECO:0000269|PubMed:15016821}.
-!- MISCELLANEOUS: Present with 2157 molecules/cell in log phase SD medium.
{ECO:0000269|PubMed:14562106}.
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EMBL; Z72871; CAA97088.1; -; Genomic_DNA.
EMBL; BK006941; DAA08179.1; -; Genomic_DNA.
PIR; S64381; S64381.
RefSeq; NP_011600.3; NM_001181215.3.
SMR; P53252; -.
BioGrid; 33328; 267.
DIP; DIP-4618N; -.
IntAct; P53252; 45.
MINT; P53252; -.
STRING; 4932.YGR086C; -.
iPTMnet; P53252; -.
MaxQB; P53252; -.
PaxDb; P53252; -.
PRIDE; P53252; -.
EnsemblFungi; YGR086C_mRNA; YGR086C; YGR086C.
GeneID; 852977; -.
KEGG; sce:YGR086C; -.
EuPathDB; FungiDB:YGR086C; -.
SGD; S000003318; PIL1.
HOGENOM; CLU_046464_0_0_1; -.
InParanoid; P53252; -.
OMA; DCENSLA; -.
BioCyc; YEAST:G3O-30798-MONOMER; -.
PRO; PR:P53252; -.
Proteomes; UP000002311; Chromosome VII.
RNAct; P53252; protein.
GO; GO:0071944; C:cell periphery; HDA:SGD.
GO; GO:0005737; C:cytoplasm; HDA:SGD.
GO; GO:0032126; C:eisosome; IDA:SGD.
GO; GO:0036286; C:eisosome filament; IBA:GO_Central.
GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
GO; GO:0005739; C:mitochondrion; HDA:SGD.
GO; GO:0005886; C:plasma membrane; HDA:SGD.
GO; GO:0008289; F:lipid binding; IDA:SGD.
GO; GO:0070941; P:eisosome assembly; IMP:SGD.
GO; GO:0006897; P:endocytosis; IMP:SGD.
GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:SGD.
GO; GO:0008104; P:protein localization; IMP:SGD.
GO; GO:0097446; P:protein localization to eisosome filament; IMP:SGD.
GO; GO:0009408; P:response to heat; IMP:SGD.
Gene3D; 1.20.1270.60; -; 1.
InterPro; IPR027267; AH/BAR_dom_sf.
InterPro; IPR028245; PIL1/LSP1.
PANTHER; PTHR31962; PTHR31962; 1.
Pfam; PF13805; Pil1; 1.
1: Evidence at protein level;
Direct protein sequencing; Isopeptide bond; Lipid droplet; Phosphoprotein;
Reference proteome; Ubl conjugation.
CHAIN 1..339
/note="Sphingolipid long chain base-responsive protein
PIL1"
/id="PRO_0000058441"
COMPBIAS 21..25
/note="Poly-Pro"
COMPBIAS 279..323
/note="Glu-rich"
MOD_RES 14
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:19779198"
MOD_RES 16
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19779198"
MOD_RES 45
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19779198"
MOD_RES 98
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19779198"
MOD_RES 163
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956, ECO:0000244|PubMed:19779198"
MOD_RES 230
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18407956"
MOD_RES 233
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:17330950, ECO:0000244|PubMed:17761666,
ECO:0000244|PubMed:18407956, ECO:0000244|PubMed:19779198"
MOD_RES 299
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19779198"
CROSSLNK 29
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000244|PubMed:22106047"
SEQUENCE 339 AA; 38349 MW; C86AE5ABB508EA03 CRC64;
MHRTYSLRNS RAPTASQLQN PPPPPSTTKG RFFGKGGLAY SFRRSAAGAF GPELSRKLSQ
LVKIEKNVLR SMELTANERR DAAKQLSIWG LENDDDVSDI TDKLGVLIYE VSELDDQFID
RYDQYRLTLK SIRDIEGSVQ PSRDRKDKIT DKIAYLKYKD PQSPKIEVLE QELVRAEAES
LVAEAQLSNI TRSKLRAAFN YQFDSIIEHS EKIALIAGYG KALLELLDDS PVTPGETRPA
YDGYEASKQI IIDAESALNE WTLDSAQVKP TLSFKQDYED FEPEEGEEEE EEDGQGRWSE
DEQEDGQIEE PEQEEEGAVE EHEQVGHQQS ESLPQQTTA


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Pathways :
WP1673: Naphthalene and anthracene degradation
WP1625: Base excision repair
WP1654: gamma-Hexachlorocyclohexane degradation
WP1502: Mitochondrial biogenesis
WP2347: vitamin B5 (pantothenate) and CoA biosynthesis Pathway
WP1665: Limonene and pinene degradation
WP2434: very-long-chain-fatty-acid-biosynthesis
WP1996: Linoleate Biosynthesis
WP1002: Electron Transport Chain
WP2371: Parkinsons Disease Pathway
WP1614: 1- and 2-Methylnaphthalene degradation
WP1892: Protein folding
WP1939: Unfolded Protein Response
WP1119: Electron Transport Chain
WP1678: Nucleotide excision repair
WP346: Protein Modifications
WP1371: G Protein Signaling Pathways
WP1690: Propanoate metabolism
WP525: Mitochondrial Unfolded-Protein Response
WP1644: DNA replication
WP210: Cytoplasmic Ribosomal Proteins
WP2203: TSLP Signaling Pathway
WP1424: Globo Sphingolipid Metabolism
WP1694: Pyrimidine metabolism
WP622: Long-Day Flowering Time Pathway

Related Genes :
[PIL1 YGR086C] Sphingolipid long chain base-responsive protein PIL1
[LSP1 YPL004C] Sphingolipid long chain base-responsive protein LSP1
[pil1 SPCC736.15] Probable sphingolipid long chain base-responsive protein pil1 (Protein kinase inhibitor pil1)
[LCB3 LBP1 YSR2 YJL134W J0671] Dihydrosphingosine 1-phosphate phosphatase LCB3 (EC 3.1.3.-) (Long-chain base protein 3) (Sphingolipid resistance protein 2)
[SLD1 At3g61580 F2A19.180] Delta(8)-fatty-acid desaturase 1 (EC 1.14.19.29) (Delta(8)-sphingolipid desaturase 1) (Sphingoid long-chain base desaturase 1) (Sphingoid LCB desaturase 1) (Sphingolipid 8-(E/Z)-desaturase 1)
[PIL1 BHLH124 EN110 At2g46970 F14M4.20] Transcription factor PIL1 (Basic helix-loop-helix protein 124) (AtbHLH124) (bHLH 124) (Protein PHYTOCHROME INTERACTING FACTOR 3-LIKE 1) (Transcription factor EN 110) (bHLH transcription factor bHLH124)
[SLD2 At2g46210 T3F17.14] Delta(8)-fatty-acid desaturase 2 (EC 1.14.19.29) (Delta(8)-sphingolipid desaturase 2) (Sphingoid long-chain base desaturase 2) (Sphingoid LCB desaturase 2) (Sphingolipid 8-(E/Z)-desaturase 2)
[LCB2a LCB2 At5g23670 MQM1.6] Long chain base biosynthesis protein 2a (AtLCB2a) (EC 2.3.1.50) (Long chain base biosynthesis protein 2) (AtLCB2)
[LCB4 YOR171C O3615] Sphingoid long chain base kinase 4 (LCB kinase 4) (EC 2.7.1.91) (Sphinganine kinase 4)
[LCB1 END8 TSC2 YMR296C] Serine palmitoyltransferase 1 (SPT 1) (SPT1) (EC 2.3.1.50) (Long chain base biosynthesis protein 1)
[SPTLC1 LCB1] Serine palmitoyltransferase 1 (EC 2.3.1.50) (Long chain base biosynthesis protein 1) (LCB 1) (Serine-palmitoyl-CoA transferase 1) (SPT 1) (SPT1)
[LCB1 EMB2779 FBR11 At4g36480 AP22 C7A10.880] Long chain base biosynthesis protein 1 (AtLCB1) (EC 2.3.1.50) (Protein EMBRYO DEFECTIVE 2779) (Protein FUMONISIN B1 RESISTANT 11)
[LCB2 SCS1 TSC1 YDR062W D4246 YD9609.16] Serine palmitoyltransferase 2 (SPT 2) (EC 2.3.1.50) (Long chain base biosynthesis protein 2)
[LCB5 YLR260W] Sphingoid long chain base kinase 5 (LCB kinase 5) (EC 2.7.1.91) (Sphinganine kinase 5)
[LCB2b LCB2.2 SPT1 At3g48780 T21J18_50] Long chain base biosynthesis protein 2b (AtLCB2b) (EC 2.3.1.50) (Serine palmitoyltransferase 1) (AtSPT1)
[Sptlc2 Lcb2] Serine palmitoyltransferase 2 (EC 2.3.1.50) (Long chain base biosynthesis protein 2) (LCB 2) (Long chain base biosynthesis protein 2a) (LCB2a) (Serine-palmitoyl-CoA transferase 2) (SPT 2)
[SPTLC2 KIAA0526 LCB2] Serine palmitoyltransferase 2 (EC 2.3.1.50) (Long chain base biosynthesis protein 2) (LCB 2) (Long chain base biosynthesis protein 2a) (LCB2a) (Serine-palmitoyl-CoA transferase 2) (SPT 2)
[SPTLC3 C20orf38 SPTLC2L] Serine palmitoyltransferase 3 (EC 2.3.1.50) (Long chain base biosynthesis protein 2b) (LCB2b) (Long chain base biosynthesis protein 3) (LCB 3) (Serine-palmitoyl-CoA transferase 3) (SPT 3)
[SCS7 FAH1 YMR272C YM8156.14C] Ceramide very long chain fatty acid hydroxylase SCS7 (Ceramide VLCFA hydroxylase SCS7) (4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase SCS7) (EC 1.14.18.6) (Dihydroceramide fatty acyl 2-hydroxylase SCS7) (EC 1.14.18.7) (Sphingolipid alpha-hydroxylase) (Suppressor of calcium sensitivity 7)
[YSR3 LBP2 YKR053C] Dihydrosphingosine 1-phosphate phosphatase YSR3 (EC 3.1.3.-) (Long-chain base protein 2) (Sphingolipid resistance protein 3)
[PHS1 YJL097W J0902] Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase PHS1 (EC 4.2.1.134) (3-hydroxyacyl-CoA dehydratase PHS1) (HACD) (PTPLA homolog involved in sphingolipid biosynthesis protein 1)
[Sptlc1 Lcb1] Serine palmitoyltransferase 1 (EC 2.3.1.50) (Long chain base biosynthesis protein 1) (LCB 1) (Serine-palmitoyl-CoA transferase 1) (SPT 1) (SPT1)
[RSB1 YOR049C O2787] Sphingoid long-chain base transporter RSB1
[Sptlc1 Lcb1 rCG_44191] Serine palmitoyltransferase 1 (EC 2.3.1.50) (Long chain base biosynthesis protein 1) (LCB 1) (Serine-palmitoyl-CoA transferase 1) (SPT 1) (SPT1)
[PIL13 BHLH152 PIL1 Os03g0782500 LOC_Os03g56950] Transcription factor PHYTOCHROME INTERACTING FACTOR-LIKE 13 (OsPIL13) (PIF-like protein 13) (Basic helix-loop-helix protein 152) (OsbHLH152) (OsPIL1)
[ELOVL6 FACE LCE] Elongation of very long chain fatty acids protein 6 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL6) (ELOVL fatty acid elongase 6) (ELOVL FA elongase 6) (Fatty acid elongase 2) (hELO2) (Fatty acyl-CoA elongase) (Long-chain fatty-acyl elongase) (Very long chain 3-ketoacyl-CoA synthase 6) (Very long chain 3-oxoacyl-CoA synthase 6)
[pil2 SPAC3C7.02c] Probable sphingolipid long chain base-responsive protein pil2 (Protein kinase inhibitor pil2)
[Elovl1 Ssc1] Elongation of very long chain fatty acids protein 1 (EC 2.3.1.199) (3-keto acyl-CoA synthase Elovl1) (ELOVL fatty acid elongase 1) (ELOVL FA elongase 1) (Very long chain 3-ketoacyl-CoA synthase 1) (Very long chain 3-oxoacyl-CoA synthase 1)
[ELOVL1 SSC1 CGI-88] Elongation of very long chain fatty acids protein 1 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL1) (ELOVL fatty acid elongase 1) (ELOVL FA elongase 1) (Very long chain 3-ketoacyl-CoA synthase 1) (Very long chain 3-oxoacyl-CoA synthase 1)
[ELOVL5 ELOVL2 PRO0530] Elongation of very long chain fatty acids protein 5 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL5) (ELOVL fatty acid elongase 5) (ELOVL FA elongase 5) (Fatty acid elongase 1) (hELO1) (Very long chain 3-ketoacyl-CoA synthase 5) (Very long chain 3-oxoacyl-CoA synthase 5)

Bibliography :