SCUBA

SPTSSA — Serine palmitoyltransferase small subunit A

SPTSSA belongs to a gene co-expression module in 3 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.

SPTSSA's module in each cell type

Cell typeModuleShares the module with
EndothelialActin Vesicle Trafficking
Cytoskeletal
ABRACL, ACTR3, ADRM1, ANKRD9, C3orf14, CISD2, CLIC1, EIF2S1 +10 moreView in SCUBA
FibroblastsTGF-beta Fibrosis
ECM production
ATP1B3, FKBP10, LOXL2, PLOD1, PMEPA1, TGFBI, WNT5AView in SCUBA
Gamma-delta T cellsBasal Lipid Metabolism
Housekeeping
ACOT7, ADCY3, AHCY, CLN6, DENND6B, FANCL, MGLL, MPST +6 more

About the gene

SynonymsC14orf147, ssSPTa
Chromosome14: 34432788-34462240
Predicted locationMembrane
Essential geneNo
Protein classPredicted membrane proteins
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 composed of SPTLC1, SPTLC2 or SPTLC3 and SPTSSA or SPTSSB. Within this complex, the heterodimer consisting of SPTLC1 and SPTLC2/SPTLC3 forms the catalytic core. Within the SPT complex, SPTSSA stimulates the catalytic activity and plays a role in substrate specificity, which depends upon the overall complex composition. 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. Independently of its action as a SPT component, may be involved in MBOAT7 localization to mitochondria-associated membranes, a membrane bridge between the endoplasmic reticulum and mitochondria, may hence affect MBOAT7- catalyzed incorporation of arachidonic acid into phosphatidylinositol.

Human Protein Atlas · Open Targets · UniProt

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