Tag | Content |
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CPLM ID | CPLM-000616 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Serine palmitoyltransferase 1 |
Protein Synonyms/Alias | Long chain base biosynthesis protein 1; LCB 1; Serine-palmitoyl-CoA transferase 1; SPT 1; SPT1 |
Gene Name | Sptlc1 |
Gene Synonyms/Alias | Lcb1 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
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222 | ADLERLLKEQEIEDQ | ubiquitination | [1] | 375 | KKCQNIHKSLQGVSG | ubiquitination | [1] |
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Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | Serine palmitoyltransferase (SPT). The heterodimer formed with SPTLC2 or SPTLC3 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates. The SPTLC1-SPTLC2-SPTSSB complex displays a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme has the ability to use a broader range of acyl-CoAs (By similarity). |
Sequence Annotation | |
Keyword | Acyltransferase; Complete proteome; Endoplasmic reticulum; Lipid metabolism; Membrane; Pyridoxal phosphate; Reference proteome; Sphingolipid metabolism; Transferase; Transmembrane; Transmembrane helix. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 473 AA |
Protein Sequence | MATVAEQWVL VEMVQALYEA PAYHLILEGI LILWIIRLVF SKTYKLQERS DLTAKEKEEL 60 IEEWQPEPLV PPVSKNHPAL NYNIVSGPPT HNIVVNGKEC VNFASFNFLG LLANPRVKAT 120 AFSSLKKYGV GTCGPRGFYG TFDVHLDLEE RLAKFMKTEE AIIYSYGFST IASAIPAYSK 180 RGDIIFVDSA ACFAIQKGLQ ASRSDIKLFK HNDVADLERL LKEQEIEDQK NPRKARVTRR 240 FIVVEGLYMN TGTICPLPEL VKLKYKYKAR IFLEESLSFG VLGEHGRGVT EHYGISIDDI 300 DLISANMENA LASVGGFCCG RSFVVDHQRL SGQGYCFSAS LPPLLAAAAI EALNIMEENP 360 DIFAVLKKKC QNIHKSLQGV SGLKVVGESL SPALHLQLEE STGSREKDVK LLQAIVDQCM 420 DKGIALTQAR YLDKEEKCLP PPSIRVVVTV EQTEEELQRA ASTIREAAQA VLL 473 |
Gene Ontology | GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0035339; C:SPOTS complex; ISS:UniProtKB. GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW. GO:0046513; P:ceramide biosynthetic process; IMP:MGI. GO:0046511; P:sphinganine biosynthetic process; IMP:MGI. GO:0006686; P:sphingomyelin biosynthetic process; IMP:MGI. GO:0046512; P:sphingosine biosynthetic process; IMP:MGI. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |