GO_REF:0000002
Gene Ontology annotation through association of InterPro records with GO terms
GO_REF:0000033
Annotation inferences using phylogenetic trees
GO_REF:0000044
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
GO_REF:0000107
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
GO_REF:0000117
Electronic Gene Ontology annotations created by ARBA machine learning models
GO_REF:0000120
Combined Automated Annotation using Multiple IEA Methods
file:human/SMPD1/SMPD1-uniprot.txt
UniProtKB P17405 (ASM_HUMAN) record for human SMPD1 / acid sphingomyelinase
PMID:12563314
Host defense against Pseudomonas aeruginosa requires ceramide-rich membrane rafts.
PMID:15877209
Acid sphingomyelinase deficiency. Phenotype variability with prevalence of intermediate phenotype in a series of twenty-five Czech and Slovak patients. A multi-approach study.
PMID:16787399
The lysosomal trafficking of acid sphingomyelinase is mediated by sortilin and mannose 6-phosphate receptor.
PMID:1718266
Molecular basis of acid sphingomyelinase deficiency in a patient with Niemann-Pick disease type A.
PMID:17303575
Activation of acid sphingomyelinase by protein kinase Cdelta-mediated phosphorylation.
PMID:1840600
Human acid sphingomyelinase. Isolation, nucleotide sequence and expression of the full-length and alternatively spliced cDNAs.
PMID:18815062
Characterization of common SMPD1 mutations causing types A and B Niemann-Pick disease and generation of mutation-specific mouse models.
PMID:19279008
Acid beta-glucosidase 1 counteracts p38delta-dependent induction of interleukin-6: possible role for ceramide as an anti-inflammatory lipid.
PMID:19279011
Involvement of acid beta-glucosidase 1 in the salvage pathway of ceramide formation.
PMID:20530211
Exocytosis of acid sphingomyelinase by wounded cells promotes endocytosis and plasma membrane repair.
PMID:20807762
Regulated secretion of acid sphingomyelinase: implications for selectivity of ceramide formation.
PMID:20956541
Syntaxin 4 is required for acid sphingomyelinase activity and apoptotic function.
PMID:21098024
A novel mechanism of lysosomal acid sphingomyelinase maturation: requirement for carboxyl-terminal proteolytic processing.
PMID:21157428
Caspase-8 and caspase-7 sequentially mediate proteolytic activation of acid sphingomyelinase in TNF-R1 receptosomes.
PMID:22573858
Ebolavirus requires acid sphingomyelinase activity and plasma membrane sphingomyelin for infection.
PMID:23533145
In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.
PMID:25339683
Acid sphingomyelinase activity is regulated by membrane lipids and facilitates cholesterol transfer by NPC2.
PMID:26084044
Alleged Detrimental Mutations in the SMPD1 Gene in Patients with Niemann-Pick Disease.
PMID:27498570
Endolysosomes Are the Principal Intracellular Sites of Acid Hydrolase Activity.
PMID:27659707
Structural and functional analysis of the ASM p.Ala359Asp mutant that causes acid sphingomyelinase deficiency.
PMID:33163980
Pharmacological Inhibition of Acid Sphingomyelinase Prevents Uptake of SARS-CoV-2 by Epithelial Cells.
PMID:7670466
Acid sphingomyelinase deficient mice: a model of types A and B Niemann-Pick disease.
PMID:8702487
Zn2+-stimulated sphingomyelinase is secreted by many cell types and is a product of the acid sphingomyelinase gene.
PMID:8706124
Acid sphingomyelinase-deficient human lymphoblasts and mice are defective in radiation-induced apoptosis.
PMID:9030779
Functional characterization of the N-glycosylation sites of human acid sphingomyelinase by site-directed mutagenesis.
PMID:9660788
The cellular trafficking and zinc dependence of secretory and lysosomal sphingomyelinase, two products of the acid sphingomyelinase gene.
Reactome:R-HSA-1605797
SMPD1 hydrolyzes SPHM
Reactome:R-HSA-9769740
Coagulation pathway
Reactome:R-HSA-9769742
SMPD1 converts sphingomyelin to ceramide
Reactome:R-HSA-9840310
Glycosphingolipid catabolism