CERS2
entrez
29956
canonical
uniprot
Q96G23
canonical
ensembl
ENSG00000143418
resolver
ensp
ENSP00000271688
resolver
ensp
ENSP00000357950
resolver
ensp
ENSP00000555894
resolver
ensp
ENSP00000555895
resolver
ensp
ENSP00000555896
resolver
ensp
ENSP00000555907
resolver
ensp
ENSP00000555908
resolver
ensp
ENSP00000555909
resolver
ensp
ENSP00000555910
resolver
ensp
ENSP00000555911
resolver
ensp
ENSP00000555912
resolver
ensp
ENSP00000555913
resolver
ensp
ENSP00000555914
resolver
ensp
ENSP00000581903
resolver
ensp
ENSP00000581904
resolver
ensp
ENSP00000625140
resolver
ensp
ENSP00000625142
resolver
enst
ENST00000271688
resolver
enst
ENST00000368954
resolver
enst
ENST00000885835
resolver
enst
ENST00000885836
resolver
enst
ENST00000885837
resolver
enst
ENST00000885848
resolver
enst
ENST00000885849
resolver
enst
ENST00000885850
resolver
enst
ENST00000885851
resolver
enst
ENST00000885852
resolver
enst
ENST00000885853
resolver
enst
ENST00000885854
resolver
enst
ENST00000885855
resolver
enst
ENST00000911844
resolver
enst
ENST00000911845
resolver
enst
ENST00000955081
resolver
enst
ENST00000955083
resolver
genesymbol
CERS2
resolver
genesymbol_syn
LASS2
resolver
genesymbol_syn
TMSG1
resolver
hgnc
HGNC:14076
resolver
uniprot
D3DV06
resolver
uniprot
Q5SZE5
resolver
uniprot
Q9HD96
resolver
uniprot
Q9NW79
resolver
uniprot_entry
CERS2_HUMAN
resolver
uniprot_sec
D3DV06
resolver
uniprot_sec
Q5SZE5
resolver
uniprot_sec
Q9HD96
resolver
uniprot_sec
Q9NW79
resolver
activity_regulation
ACTIVITY REGULATION: Ceramide synthase activity is inhibited by sphingosine-1-phosphate. {ECO:0000269|PubMed:18165233}.
uniprot
proteins
amino_acid_sequence
MLQTLYDYFWWERLWLPVNLTWADLEDRDGRVYAKASDLYITLPLALLFLIVRYFFELYVATPLAALLNIKEKTRLRAPPNATLEHFYLTSGKQPKQVEVELLSRQSGLSGRQVERWFRRRRNQDRPSLLKKFREASWRFTFYLIAFIAGMAVIVDKPWFYDMKKVWEGYPIQSTIPSQYWYYMIELSFYWSLLFSIASDVKRKDFKEQIIHHVATIILISFSWFANYIRAGTLIMALHDSSDYLLESAKMFNYAGWKNTCNNIFIVFAIVFIITRLVILPFWILHCTLVYPLELYPAFFGYYFFNSMMGVLQLLHIFWAYLILRMAHKFITGKLVEDERSDREETESSEGEEAAAGGGAKSRPLANGHPILNNNHRKND
uniprot
proteins
ec_number
2.3.1.24
uniprot
proteins
ec_number
2.3.1.297
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 very-long-chain fatty acyl-CoA (chain length C22-C27) (PubMed:17977534, PubMed:18165233, PubMed:18541923, PubMed:19728861, PubMed:20937905, PubMed:22144673, PubMed:22661289, PubMed:26887952, PubMed:29632068). N-acylates sphinganine and sphingosine bases to form dihydroceramides and ceramides in de novo synthesis and salvage pathways, respectively (By similarity) (PubMed:17977534, PubMed:18165233, PubMed:18541923, PubMed:19728861, PubMed:20937905, PubMed:22144673, PubMed:22661289, PubMed:26887952, PubMed:29632068). Plays a non-redundant role in the synthesis of ceramides with very-long-chain fatty acids in kidney, liver and brain. Regulates the abundance of myelin-specific sphingolipids galactosylceramide and sulfatide that affects myelin sheath architecture and motor neuron functions (By similarity). {ECO:0000250|UniProtKB:Q924Z4, ECO:0000269|PubMed:17977534, ECO:0000269|PubMed:18165233, ECO:0000269|PubMed:18541923, ECO:0000269|PubMed:19728861, ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:22144673, ECO:0000269|PubMed:22661289, ECO:0000269|PubMed:26887952, ECO:0000269|PubMed:29632068}.
uniprot
proteins
mass_dalton
44876
uniprot
proteins
mutagenesis
MUTAGEN 230; /note="R->A: Abolished inhibition by sphingosine-1-phosphate; when associated with A-325."; /evidence="ECO:0000269|PubMed:18165233"; MUTAGEN 325; /note="R->A: Abolished inhibition by sphingosine-1-phosphate; when associated with A-230."; /evidence="ECO:0000269|PubMed:18165233"; MUTAGEN 341..349; /note="SDREETESS->ADREEAEAA: Strongly decreased phosphorylation leading to reduced ceramide synthase activity."; /evidence="ECO:0000269|PubMed:26887952
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:17977534, ECO:0000269|PubMed:18165233, ECO:0000269|PubMed:18541923, ECO:0000269|PubMed:19728861, ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:22144673, ECO:0000269|PubMed:22661289, ECO:0000269|PubMed:26887952, ECO:0000269|PubMed:29632068}.
uniprot
proteins
post_translational_modification
PTM: Acetylated. Deacetylation by SIRT3 increases enzyme activity and promotes mitochondrial ceramide accumulation. {ECO:0000250|UniProtKB:Q924Z4}.; PTM: Phosphorylated at the C-terminus by CK2, leading to increase the ceramide synthase activity. {ECO:0000269|PubMed:26887952}.
uniprot
proteins
protein_family
Sphingosine N-acyltransferase family
uniprot
proteins
pubmed
11543633
uniprot
proteins
pubmed
12869556
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16263699
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17977534
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18165233
uniprot
proteins
pubmed
18318008
uniprot
proteins
pubmed
18541923
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19728861
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20937905
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22144673
uniprot
proteins
pubmed
22661289
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26887952
uniprot
proteins
pubmed
29632068
uniprot
proteins
pubmed
38961186
uniprot
proteins
sequence_length
380
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18165233}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 41..61; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 140..160; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 181..201; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 209..229; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 264..284; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 304..324; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins