SCUBA

SPTLC1 — Serine palmitoyltransferase long chain base subunit 1

SPTLC1 belongs to a gene co-expression module in 1 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.

SPTLC1's module in each cell type

Cell typeModuleShares the module with
MacrophagesHypoxia-driven Activation
Inflammatory
ACVR1B, ADAM10, ADAM9, ALCAM, ANO6, B3GNT2, BTG1, C5AR1 +33 moreView in SCUBA

About the gene

SynonymshLCB1, HSAN1, HSN1, LCB1, SPTI
Chromosome9: 92000087-92115413
Predicted locationMembrane
Essential geneYes
Protein classDisease related genes, Enzymes, Essential proteins, Human disease related genes, Metabolic proteins, Plasma proteins, Potential drug targets, Predicted membrane proteins
Molecular functionAcyltransferase, Transferase
Biological processLipid metabolism, Sphingolipid metabolism

Function

Component of the serine palmitoyltransferase multisubunit enzyme (SPT) that catalyzes the initial and rate-limiting step in sphingolipid biosynthesis by condensing L-serine and activated acyl-CoA (most commonly palmitoyl-CoA) to form long-chain bases. The SPT complex is also composed of SPTLC2 or SPTLC3 and SPTSSA or SPTSSB. Within this complex, the heterodimer with SPTLC2 or SPTLC3 forms 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, with a slight preference for C14-CoA. The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference. Required for adipocyte cell viability and metabolic homeostasis (By similarity).

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.