CERS1
entrez
10715
canonical
uniprot
P27544
canonical
ensembl
ENSG00000223802
resolver
ensp
ENSP00000389044
resolver
ensp
ENSP00000437648
resolver
ensp
ENSP00000471428
resolver
ensp
ENSP00000485308
resolver
enst
ENST00000542296
resolver
genesymbol
CERS1
resolver
genesymbol
LASS1
resolver
genesymbol_syn
LAG1
resolver
genesymbol_syn
LASS1
resolver
genesymbol_syn
UOG1
resolver
hgnc
HGNC:14253
resolver
uniprot
B4DE47
resolver
uniprot
F6WFW5
resolver
uniprot
Q5XG75
resolver
uniprot_entry
B4DE47_HUMAN
resolver
uniprot_entry
CERS1_HUMAN
resolver
uniprot_entry
F6WFW5_HUMAN
resolver
uniprot_entry
Q5XG75_HUMAN
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by fumonisin B1. {ECO:0000250|UniProtKB:P27545}.
uniprot
proteins
amino_acid_sequence
MAAAGPAAGPTGPEPMPSYAQLVQRGWGSALAAARGCTDCGWGLARRGLAEHAHLAPPELLLLALGALGWTALRSAATARLFRPLAKRCCLQPRDAAKMPESAWKFLFYLGSWSYSAYLLFGTDYPFFHDPPSVFYDWTPGMAVPRDIAAAYLLQGSFYGHSIYATLYMDTWRKDSVVMLLHHVVTLILIVSSYAFRYHNVGILVLFLHDISDVQLEFTKLNIYFKSRGGSYHRLHALAADLGCLSFGFSWFWFRLYWFPLKVLYATSHCSLRTVPDIPFYFFFNALLLLLTLMNLYWFLYIVAFAAKVLTGQVHELKDLREYDTAEAQSLKPSKAEKPLRNGLVKDKRF
uniprot
proteins
disease_involvement
DISEASE: Epilepsy, progressive myoclonic 8 (EPM8) [MIM:616230]: A form of progressive myoclonic epilepsy, a clinically and genetically heterogeneous group of disorders defined by the combination of action and reflex myoclonus, other types of epileptic seizures, and progressive neurodegeneration and neurocognitive impairment. EPM8 is an autosomal recessive form characterized by myoclonus, generalized tonic-clonic seizures and moderate to severe cognitive impairment. {ECO:0000269|PubMed:24782409, ECO:0000269|PubMed:33798445}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.3.1.24
uniprot
proteins
ec_number
2.3.1.299
uniprot
proteins
function
FUNCTION: Ceramide synthase that catalyzes the transfer of the acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward stearoyl-CoA (octadecanoyl-CoA; C18:0-CoA) (PubMed:17977534, PubMed:23530041, PubMed:26887952, PubMed:31916624). N-acylates sphinganine and sphingosine bases to form dihydroceramides and ceramides in de novo synthesis and salvage pathways, respectively (PubMed:17977534, PubMed:23530041, PubMed:24782409, PubMed:26887952, PubMed:31916624). Plays a predominant role in skeletal muscle in regulating C18 ceramide and dihydroceramide levels with an impact on whole-body glucose metabolism and insulin sensitivity. Protects from diet-induced obesity by suppressing the uptake of glucose in multiple organs in a FGF21-dependent way (By similarity). Generates C18 ceramides in the brain, playing a critical role in cerebellar development and Purkinje cell function (By similarity). In response to cellular stress mediates mitophagy, a known defense mechanism against cell transformation and aging. Upon mitochondria fission, generates C18 ceramides that anchor lipidated MAP1LC3B/LC3B-II autophagolysosomes to outer mitochondrial membranes to eliminate damaged mitochondria (PubMed:22922758). {ECO:0000250|UniProtKB:P27545, ECO:0000269|PubMed:17977534, ECO:0000269|PubMed:22922758, ECO:0000269|PubMed:23530041, ECO:0000269|PubMed:24782409, ECO:0000269|PubMed:26887952, ECO:0000269|PubMed:31916624}.
uniprot
proteins
mass_dalton
39536
uniprot
proteins
mutagenesis
MUTAGEN 183; /note="H->A: Loss of ceramide synthase activity."; /evidence="ECO:0000269|PubMed:22922758
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:17977534, ECO:0000269|PubMed:23530041, ECO:0000269|PubMed:26887952}.
uniprot
proteins
post_translational_modification
PTM: Acetylated. Deacetylation by SIRT3 increases enzyme activity and promotes mitochondrial ceramide accumulation. {ECO:0000250|UniProtKB:P27545}.
uniprot
proteins
protein_family
Sphingosine N-acyltransferase family
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17977534
uniprot
proteins
pubmed
2034669
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22922758
uniprot
proteins
pubmed
23530041
uniprot
proteins
pubmed
24782409
uniprot
proteins
pubmed
26887952
uniprot
proteins
pubmed
31916624
uniprot
proteins
pubmed
33798445
uniprot
proteins
pubmed
9872981
uniprot
proteins
sequence_length
350
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24782409}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 53..73; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 103..123; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 148..168; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 176..196; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 239..259; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 287..307; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins