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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)

 SPTC3_HUMAN             Reviewed;         552 AA.
Q9NUV7; A2A2I4; B9EK64; Q05DQ8; Q5T1U4; Q9H1L1; Q9H1Z0;
10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
02-OCT-2007, sequence version 3.
13-FEB-2019, entry version 145.
RecName: Full=Serine palmitoyltransferase 3 {ECO:0000305};
EC=2.3.1.50 {ECO:0000269|PubMed:19416851};
AltName: Full=Long chain base biosynthesis protein 2b;
Short=LCB2b;
AltName: Full=Long chain base biosynthesis protein 3;
Short=LCB 3;
AltName: Full=Serine-palmitoyl-CoA transferase 3;
Short=SPT 3;
Name=SPTLC3 {ECO:0000312|HGNC:HGNC:16253}; Synonyms=C20orf38, SPTLC2L;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, AND TISSUE
SPECIFICITY.
PubMed=17023427; DOI=10.1074/jbc.M608066200;
Hornemann T., Richard S., Ruetti M.F., Wei Y., von Eckardstein A.;
"Cloning and initial characterization of a new subunit for mammalian
serine-palmitoyltransferase.";
J. Biol. Chem. 281:37275-37281(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
VAL-140.
TISSUE=Brain, Placenta, and Urinary bladder;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
PATHWAY.
PubMed=19648650; DOI=10.1074/jbc.M109.023192;
Hornemann T., Penno A., Ruetti M.F., Ernst D., Kivrak-Pfiffner F.,
Rohrer L., von Eckardstein A.;
"The SPTLC3 subunit of serine palmitoyltransferase generates short
chain sphingoid bases.";
J. Biol. Chem. 284:26322-26330(2009).
[6]
FUNCTION, CATALYTIC ACTIVITY, AND IDENTIFICATION IN THE SPT COMPLEX.
PubMed=19416851; DOI=10.1073/pnas.0811269106;
Han G., Gupta S.D., Gable K., Niranjanakumari S., Moitra P.,
Eichler F., Brown R.H. Jr., Harmon J.M., Dunn T.M.;
"Identification of small subunits of mammalian serine
palmitoyltransferase that confer distinct acyl-CoA substrate
specificities.";
Proc. Natl. Acad. Sci. U.S.A. 106:8186-8191(2009).
-!- FUNCTION: Serine palmitoyltransferase (SPT). The heterodimer
formed with LCB1/SPTLC1 constitutes the catalytic core. The
composition of the serine palmitoyltransferase (SPT) complex
determines the substrate preference. SPT complexes containing
SPTLC3 generate shorter chain sphingoid bases compared to
complexes containing SPTLC2. The SPTLC1-SPTLC3-SPTSSA isozyme uses
C12-CoA, C14-CoA and C16-CoA as substrates, with a slight
preference for C14-CoA. On the other hand, the SPTLC1-SPTLC3-
SPTSSB has the ability to use a broader range of acyl-CoAs without
apparent preference. {ECO:0000269|PubMed:19416851,
ECO:0000269|PubMed:19648650}.
-!- CATALYTIC ACTIVITY:
Reaction=H(+) + hexadecanoyl-CoA + L-serine = 3-oxosphinganine +
CO2 + CoA; Xref=Rhea:RHEA:14761, ChEBI:CHEBI:15378,
ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
ChEBI:CHEBI:57379, ChEBI:CHEBI:58299; EC=2.3.1.50;
Evidence={ECO:0000269|PubMed:17023427,
ECO:0000269|PubMed:19416851, ECO:0000269|PubMed:19648650};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14762;
Evidence={ECO:0000269|PubMed:19648650};
-!- CATALYTIC ACTIVITY:
Reaction=dodecanoyl-CoA + H(+) + L-serine = 3-
oxotetradecasphinganine + CO2 + CoA; Xref=Rhea:RHEA:35679,
ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384,
ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:71008;
Evidence={ECO:0000269|PubMed:19648650};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35680;
Evidence={ECO:0000269|PubMed:19648650};
-!- CATALYTIC ACTIVITY:
Reaction=H(+) + L-serine + tetradecanoyl-CoA = 3-
oxohexadecasphinganine + CO2 + CoA; Xref=Rhea:RHEA:35675,
ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384,
ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:71007;
Evidence={ECO:0000269|PubMed:19648650};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35676;
Evidence={ECO:0000269|PubMed:19648650};
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000250};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.04 mM for hexadecanoyl-CoA {ECO:0000269|PubMed:19648650};
KM=0.03 mM for tetradecanoyl-CoA {ECO:0000269|PubMed:19648650};
Vmax=120 pmol/min/mg enzyme toward hexadecanoyl-CoA
{ECO:0000269|PubMed:19648650};
Vmax=60 pmol/min/mg enzyme toward tetradecanoyl-CoA
{ECO:0000269|PubMed:19648650};
-!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
{ECO:0000269|PubMed:19648650}.
-!- SUBUNIT: Heterodimer with SPTLC1. Component of the serine
palmitoyltransferase (SPT) complex, composed of LCB1/SPTLC1, LCB2
(SPTLC2 or SPTLC3) and ssPT (SPTSSA and SPTSSB).
{ECO:0000269|PubMed:19416851}.
-!- INTERACTION:
O15269:SPTLC1; NbExp=3; IntAct=EBI-11614219, EBI-1044323;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000305|PubMed:19416851}; Single-pass membrane protein
{ECO:0000305|PubMed:19416851}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NUV7-1; Sequence=Displayed;
Name=2;
IsoId=Q9NUV7-2; Sequence=VSP_028167, VSP_028168;
Note=Variant in position: 149:P->A (in dbSNP:rs934335).;
-!- TISSUE SPECIFICITY: Expressed in most tissues, except peripheral
blood cells and bone marrow, with highest levels in heart, kidney,
liver, uterus and skin. {ECO:0000269|PubMed:17023427}.
-!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
aminotransferase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH05205.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK001974; BAA92012.1; -; mRNA.
EMBL; AL133331; CAM13116.1; -; Genomic_DNA.
EMBL; AL050320; CAM13116.1; JOINED; Genomic_DNA.
EMBL; AL109983; CAM13116.1; JOINED; Genomic_DNA.
EMBL; AL445589; CAM13116.1; JOINED; Genomic_DNA.
EMBL; AL445589; CAM16427.1; -; Genomic_DNA.
EMBL; AL050320; CAM16427.1; JOINED; Genomic_DNA.
EMBL; AL109983; CAM16427.1; JOINED; Genomic_DNA.
EMBL; AL133331; CAM16427.1; JOINED; Genomic_DNA.
EMBL; AL050320; CAM27358.1; -; Genomic_DNA.
EMBL; AL109983; CAM27358.1; JOINED; Genomic_DNA.
EMBL; AL133331; CAM27358.1; JOINED; Genomic_DNA.
EMBL; AL445589; CAM27358.1; JOINED; Genomic_DNA.
EMBL; AL109983; CAM28300.1; -; Genomic_DNA.
EMBL; AL050320; CAM28300.1; JOINED; Genomic_DNA.
EMBL; AL133331; CAM28300.1; JOINED; Genomic_DNA.
EMBL; AL445589; CAM28300.1; JOINED; Genomic_DNA.
EMBL; BC005205; AAH05205.1; ALT_SEQ; mRNA.
EMBL; BC020656; AAH20656.1; -; mRNA.
EMBL; BC150644; AAI50645.1; -; mRNA.
CCDS; CCDS13115.2; -. [Q9NUV7-1]
RefSeq; NP_060797.2; NM_018327.2. [Q9NUV7-1]
UniGene; Hs.425023; -.
ProteinModelPortal; Q9NUV7; -.
SMR; Q9NUV7; -.
BioGrid; 120590; 1.
CORUM; Q9NUV7; -.
DIP; DIP-60753N; -.
IntAct; Q9NUV7; 4.
STRING; 9606.ENSP00000381968; -.
DrugBank; DB00114; Pyridoxal Phosphate.
SwissLipids; SLP:000000153; -.
iPTMnet; Q9NUV7; -.
PhosphoSitePlus; Q9NUV7; -.
SwissPalm; Q9NUV7; -.
BioMuta; SPTLC3; -.
DMDM; 158931158; -.
EPD; Q9NUV7; -.
jPOST; Q9NUV7; -.
MaxQB; Q9NUV7; -.
PaxDb; Q9NUV7; -.
PeptideAtlas; Q9NUV7; -.
PRIDE; Q9NUV7; -.
ProteomicsDB; 82722; -.
ProteomicsDB; 82723; -. [Q9NUV7-2]
Ensembl; ENST00000399002; ENSP00000381968; ENSG00000172296. [Q9NUV7-1]
GeneID; 55304; -.
KEGG; hsa:55304; -.
UCSC; uc002wod.2; human. [Q9NUV7-1]
CTD; 55304; -.
DisGeNET; 55304; -.
EuPathDB; HostDB:ENSG00000172296.12; -.
GeneCards; SPTLC3; -.
H-InvDB; HIX0019548; -.
HGNC; HGNC:16253; SPTLC3.
HPA; HPA044247; -.
HPA; HPA048079; -.
MIM; 611120; gene.
neXtProt; NX_Q9NUV7; -.
OpenTargets; ENSG00000172296; -.
PharmGKB; PA162404677; -.
eggNOG; KOG1357; Eukaryota.
eggNOG; COG0156; LUCA.
GeneTree; ENSGT00940000158513; -.
HOVERGEN; HBG002230; -.
InParanoid; Q9NUV7; -.
KO; K00654; -.
OMA; IDDAHAV; -.
OrthoDB; 438936at2759; -.
PhylomeDB; Q9NUV7; -.
TreeFam; TF300452; -.
BioCyc; MetaCyc:HS16070-MONOMER; -.
BRENDA; 2.3.1.50; 2681.
Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
UniPathway; UPA00222; -.
ChiTaRS; SPTLC3; human.
GenomeRNAi; 55304; -.
PRO; PR:Q9NUV7; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000172296; Expressed in 184 organ(s), highest expression level in chorionic villus.
ExpressionAtlas; Q9NUV7; baseline and differential.
Genevisible; Q9NUV7; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0017059; C:serine C-palmitoyltransferase complex; IDA:UniProtKB.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0004758; F:serine C-palmitoyltransferase activity; IDA:UniProtKB.
GO; GO:0046520; P:sphingoid biosynthetic process; IDA:MGI.
GO; GO:0030148; P:sphingolipid biosynthetic process; TAS:UniProtKB.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
InterPro; IPR004839; Aminotransferase_I/II.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
Pfam; PF00155; Aminotran_1_2; 1.
SUPFAM; SSF53383; SSF53383; 1.
PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
1: Evidence at protein level;
Acyltransferase; Alternative splicing; Complete proteome;
Endoplasmic reticulum; Lipid metabolism; Membrane; Polymorphism;
Pyridoxal phosphate; Reference proteome; Sphingolipid metabolism;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 552 Serine palmitoyltransferase 3.
/FTId=PRO_0000079426.
TRANSMEM 59 79 Helical. {ECO:0000255}.
MOD_RES 371 371 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
VAR_SEQ 102 175 DFVPLYQDFENFYTRNLYMRIRDNWNRPICSAPGPLFDLME
RVSDDYNWTFRFTGRVIKDVINMGSYNFLGLAA -> VRMR
TSLDLCQCLLLSKVFSEVVMQVQILESMRCSGTIQGKFHSS
PPPKPHYPWAYGPVFTNISWATTICHIPN (in isoform
2). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_028167.
VAR_SEQ 176 552 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_028168.
VARIANT 140 140 L -> V (in dbSNP:rs243887).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_048230.
SEQUENCE 552 AA; 62049 MW; EED341220DCA683A CRC64;
MANPGGGAVC NGKLHNHKKQ SNGSQSRNCT KNGIVKEAQQ NGKPHFYDKL IVESFEEAPL
HVMVFTYMGY GIGTLFGYLR DFLRNWGIEK CNAAVERKEQ KDFVPLYQDF ENFYTRNLYM
RIRDNWNRPI CSAPGPLFDL MERVSDDYNW TFRFTGRVIK DVINMGSYNF LGLAAKYDES
MRTIKDVLEV YGTGVASTRH EMGTLDKHKE LEDLVAKFLN VEAAMVFGMG FATNSMNIPA
LVGKGCLILS DELNHTSLVL GARLSGATIR IFKHNNTQSL EKLLRDAVIY GQPRTRRAWK
KILILVEGVY SMEGSIVHLP QIIALKKKYK AYLYIDEAHS IGAVGPTGRG VTEFFGLDPH
EVDVLMGTFT KSFGASGGYI AGRKDLVDYL RVHSHSAVYA SSMSPPIAEQ IIRSLKLIMG
LDGTTQGLQR VQQLAKNTRY FRQRLQEMGF IIYGNENASV VPLLLYMPGK VAAFARHMLE
KKIGVVVVGF PATPLAEARA RFCVSAAHTR EMLDTVLEAL DEMGDLLQLK YSRHKKSARP
ELYDETSFEL ED


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Kits Elisa; taq POLYMERASE

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Pathways :
WP1996: Linoleate Biosynthesis
WP2347: vitamin B5 (pantothenate) and CoA biosynthesis Pathway
WP2434: very-long-chain-fatty-acid-biosynthesis
WP1502: Mitochondrial biogenesis
WP1625: Base excision repair
WP1647: Fatty acid biosynthesis
WP1654: gamma-Hexachlorocyclohexane degradation
WP1659: Glycine, serine and threonine metabolism
WP1665: Limonene and pinene degradation
WP1673: Naphthalene and anthracene degradation
WP1685: Peptidoglycan biosynthesis
WP1708: Terpenoid backbone biosynthesis
WP218: Serine and Glycine biosynthesis
WP2199: Seed Development
WP459: Serine Biosynthesis
WP1614: 1- and 2-Methylnaphthalene degradation
WP1626: Benzoate degradation via CoA ligation
WP1669: Lysine biosynthesis
WP1714: Tyrosine metabolism
WP2248: anthocyanin biosynthesis
WP2349: vitamin B3 (niacin), NAD and NADP biosynthesis pathway
WP1002: Electron Transport Chain
WP102: Heme Biosynthesis
WP1020: Fatty Acid Biosynthesis
WP1024: Steroid Biosynthesis

Related Genes :
[LCB2b LCB2.2 SPT1 At3g48780 T21J18_50] Long chain base biosynthesis protein 2b (AtLCB2b) (EC 2.3.1.50) (Serine palmitoyltransferase 1) (AtSPT1)
[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)
[Sptlc3 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-palmityl-CoA transferase 3) (SPT 3)
[LCB2a LCB2 At5g23670 MQM1.6] Long chain base biosynthesis protein 2a (AtLCB2a) (EC 2.3.1.50) (Long chain base biosynthesis protein 2) (AtLCB2)
[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)
[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)
[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)
[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 END8 TSC2 YMR296C] Serine palmitoyltransferase 1 (SPT 1) (SPT1) (EC 2.3.1.50) (Long chain base biosynthesis protein 1)
[LCB2 SCS1 TSC1 YDR062W D4246 YD9609.16] Serine palmitoyltransferase 2 (SPT 2) (EC 2.3.1.50) (Long chain base biosynthesis protein 2)
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[pol] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[pol] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Non-structural protein 2A-alpha (NS2A-alpha); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[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)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[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)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (NS5)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[GP1 MZ11_60484gpGP1 MZ11_60553gpGP1] Genome polyprotein [Cleaved into: Peptide 2k; Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (NS5)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]

Bibliography :
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