ASAH2
entrez
56624
canonical
uniprot
Q9NR71
canonical
ensembl
ENSG00000188611
resolver
ensp
ENSP00000329886
resolver
ensp
ENSP00000506746
resolver
genesymbol
ASAH2
resolver
genesymbol_syn
HNAC1
resolver
hgnc
HGNC:18860
resolver
uniprot
Q3KNU1
resolver
uniprot
Q5SNT7
resolver
uniprot
Q5SZP6
resolver
uniprot
Q5SZP7
resolver
uniprot
Q5T1D5
resolver
uniprot
Q71ME6
resolver
uniprot_entry
ASAH2_HUMAN
resolver
uniprot_sec
Q3KNU1
resolver
uniprot_sec
Q5SNT7
resolver
uniprot_sec
Q5SZP6
resolver
uniprot_sec
Q5SZP7
resolver
uniprot_sec
Q5T1D5
resolver
uniprot_sec
Q71ME6
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by dithiothreitol (DTT) and 2-mercaptoethanol (PubMed:16229686). Activity is mildly stimulated by Ca(2+) and Mg(2+), but is not inhibited by EDTA (PubMed:10781606, PubMed:16229686). Activity is inhibited by millimolar levels of Fe(2+), Zn(2+) and Cu(2+) (PubMed:16229686, PubMed:17475390). Inhibited by cholesterol (PubMed:17475390). {ECO:0000269|PubMed:10781606, ECO:0000269|PubMed:16229686, ECO:0000269|PubMed:17475390}.
uniprot
proteins
amino_acid_sequence
MAKRTFSNLETFLIFLLVMMSAITVALLSLLFITSGTIENHKDLGGHFFSTTQSPPATQGSTAAQRSTATQHSTATQSSTATQTSPVPLTPESPLFQNFSGYHIGVGRADCTGQVADINLMGYGKSGQNAQGILTRLYSRAFIMAEPDGSNRTVFVSIDIGMVSQRLRLEVLNRLQSKYGSLYRRDNVILSGTHTHSGPAGYFQYTVFVIASEGFSNQTFQHMVTGILKSIDIAHTNMKPGKIFINKGNVDGVQINRSPYSYLQNPQSERARYSSNTDKEMIVLKMVDLNGDDLGLISWFAIHPVSMNNSNHLVNSDNVGYASYLLEQEKNKGYLPGQGPFVAAFASSNLGDVSPNILGPRCINTGESCDNANSTCPIGGPSMCIAKGPGQDMFDSTQIIGRAMYQRAKELYASASQEVTGPLASAHQWVDMTDVTVWLNSTHASKTCKPALGYSFAAGTIDGVGGLNFTQGKTEGDPFWDTIRDQILGKPSEEIKECHKPKPILLHTGELSKPHPWHPDIVDVQIITLGSLAITAIPGEFTTMSGRRLREAVQAEFASHGMQNMTVVISGLCNVYTHYITTYEEYQAQRYEAASTIYGPHTLSAYIQLFRNLAKAIATDTVANLSRGPEPPFFKQLIVPLIPSIVDRAPKGRTFGDVLQPAKPEYRVGEVAEVIFVGANPKNSVQNQTHQTFLTVEKYEATSTSWQIVCNDASWETRFYWHKGLLGLSNATVEWHIPDTAQPGIYRIRYFGHNRKQDILKPAVILSFEGTSPAFEVVTI
uniprot
proteins
ec_number
3.5.1.-
uniprot
proteins
ec_number
3.5.1.23
uniprot
proteins
function
FUNCTION: Plasma membrane ceramidase that hydrolyzes sphingolipid ceramides into sphingosine and free fatty acids at neutral pH (PubMed:10781606, PubMed:16229686, PubMed:26190575). Ceramides, sphingosine, and its phosphorylated form sphingosine-1-phosphate are bioactive lipids that mediate cellular signaling pathways regulating several biological processes including cell proliferation, apoptosis and differentiation (PubMed:15946935, PubMed:19345744, PubMed:24798654). Also catalyzes the reverse reaction allowing the synthesis of ceramides from fatty acids and sphingosine (PubMed:11278489, PubMed:17475390). Together with sphingomyelinase, participates in the production of sphingosine and sphingosine-1-phosphate from the degradation of sphingomyelin, a sphingolipid enriched in the plasma membrane of cells (PubMed:16061940). Also participates in the hydrolysis of ceramides from the extracellular milieu allowing the production of sphingosine-1-phosphate inside and outside cells (By similarity). This is the case for instance with the digestion of dietary sphingolipids in the intestinal tract (By similarity). {ECO:0000250|UniProtKB:Q9JHE3, ECO:0000269|PubMed:10781606, ECO:0000269|PubMed:11278489, ECO:0000269|PubMed:15946935, ECO:0000269|PubMed:16061940, ECO:0000269|PubMed:16229686, ECO:0000269|PubMed:17475390, ECO:0000269|PubMed:19345744, ECO:0000269|PubMed:24798654, ECO:0000269|PubMed:26190575}.
uniprot
proteins
mass_dalton
85516
uniprot
proteins
mutagenesis
MUTAGEN 124; /note="G->R: Loss of ceramide hydrolase activity."; /evidence="ECO:0000269|PubMed:26190575"; MUTAGEN 194; /note="H->A: Loss of ceramide hydrolase activity."; /evidence="ECO:0000269|PubMed:26190575"; MUTAGEN 196; /note="H->A: Loss of ceramide hydrolase activity."; /evidence="ECO:0000269|PubMed:26190575"; MUTAGEN 211; /note="A->R: Loss of ceramide hydrolase activity."; /evidence="ECO:0000269|PubMed:26190575"; MUTAGEN 257; /note="R->A: Loss of ceramide hydrolase activity."; /evidence="ECO:0000269|PubMed:26190575"; MUTAGEN 258; /note="S->A: Decreased ceramide hydrolase activity."; /evidence="ECO:0000269|PubMed:16229686"; MUTAGEN 303; /note="H->A: Loss of ceramide hydrolase activity."; /evidence="ECO:0000269|PubMed:26190575"; MUTAGEN 352; /note="D->S: Loss of ceramide hydrolase activity."; /evidence="ECO:0000269|PubMed:16229686"; MUTAGEN 354; /note="S->A: Loss of ceramide hydrolase activity."; /evidence="ECO:0000269|PubMed:16229686"; MUTAGEN 362; /note="C->A: Loss of ceramide hydrolase activity."; /evidence="ECO:0000269|PubMed:16229686"; MUTAGEN 374; /note="S->A: Decreased ceramide hydrolase activity."; /evidence="ECO:0000269|PubMed:16229686"; MUTAGEN 396; /note="S->A: No effect on ceramide hydrolase activity."; /evidence="ECO:0000269|PubMed:16229686"; MUTAGEN 465; /note="G->R: Loss of ceramide hydrolase activity."; /evidence="ECO:0000269|PubMed:26190575"; MUTAGEN 540; /note="E->A: Loss of ceramide hydrolase activity."; /evidence="ECO:0000269|PubMed:26190575"; MUTAGEN 579; /note="Y->F: Loss of ceramide hydrolase activity."; /evidence="ECO:0000269|PubMed:26190575"; MUTAGEN 591; /note="Y->F: Loss of ceramide hydrolase activity."; /evidence="ECO:0000269|PubMed:26190575"; MUTAGEN 595; /note="S->A: Decreased ceramide hydrolase activity."; /evidence="ECO:0000269|PubMed:16229686"; MUTAGEN 729; /note="S->A: Decreased ceramide hydrolase activity."; /evidence="ECO:0000269|PubMed:16229686
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:15946935, ECO:0000269|PubMed:19345744}.
uniprot
proteins
post_translational_modification
PTM: Proteolytic cleavage of the N-terminus removes the signal-anchor and produces a soluble form of the protein. {ECO:0000250|UniProtKB:Q91XT9}.; PTM: N-glycosylated. Required for enzyme activity. {ECO:0000250|UniProtKB:Q9JHE3}.; PTM: O-glycosylated. Required to retain it as a type II membrane protein at the cell surface. {ECO:0000269|PubMed:15845354}.; PTM: Phosphorylated. May prevent ubiquitination and subsequent degradation. {ECO:0000250|UniProtKB:Q91XT9}.; PTM: Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is triggered by nitric oxide. {ECO:0000250|UniProtKB:Q91XT9}.
uniprot
proteins
protein_family
Neutral ceramidase family
uniprot
proteins
pubmed
10781606
uniprot
proteins
pubmed
11278489
uniprot
proteins
pubmed
14557071
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15845354
uniprot
proteins
pubmed
15946935
uniprot
proteins
pubmed
16061940
uniprot
proteins
pubmed
16229686
uniprot
proteins
pubmed
17334805
uniprot
proteins
pubmed
17475390
uniprot
proteins
pubmed
19345744
uniprot
proteins
pubmed
24798654
uniprot
proteins
pubmed
26190575
uniprot
proteins
pubmed
30154232
uniprot
proteins
sequence_length
780
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Neutral ceramidase]: Cell membrane {ECO:0000269|PubMed:15845354}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q91XT9}. Membrane raft {ECO:0000250|UniProtKB:Q9JHE3}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q91XT9}. Membrane, caveola {ECO:0000250|UniProtKB:Q9JHE3}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q91XT9}. Golgi apparatus membrane {ECO:0000269|PubMed:30154232}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q91XT9}. Mitochondrion {ECO:0000269|PubMed:10781606}. Secreted, extracellular exosome {ECO:0000269|PubMed:24798654}. Note=Enriched in exosomes upon stimulation by cytokine (PubMed:24798654). Enriched in caveolae and lipid rafts (By similarity). The localization to the mitochondrion could not be confirmed (PubMed:15845354). {ECO:0000250|UniProtKB:Q9JHE3, ECO:0000269|PubMed:15845354, ECO:0000269|PubMed:24798654}.; SUBCELLULAR LOCATION: [Neutral ceramidase soluble form]: Secreted {ECO:0000250|UniProtKB:Q91XT9}.
uniprot
proteins
transmembrane_region
TRANSMEM 13..33; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins