ACER1:Alkaline ceramidase 1

Gene Name
Alkaline ceramidase 1
Protein ID
Chromosome ID
HPP Status
Protein Name
Alkaline ceramidase 1

N-acylsphingosine amidohydrolase (alkaline ceramidase) 3

AlkCDase 1

alkaline CDase 1

alkCDase 1


alkaline ceramidase 1

Acylsphingosine deacylase 3

N-acylsphingosine amidohydrolase 3

Alkaline CDase 1

acylsphingosine deacylase 3



[Reference: ]
Chromosomal Position
19p13.3 | Start:6306142 End:6306142

Entrez Gene Summary for ACER1
Ceramides are synthesized during epidermal differentiation and accumulate within the interstices of the stratum corneum, where they represent critical components of the epidermal permeability barrier. Excess cellular ceramide can trigger antimitogenic signals and induce apoptosis, and the ceramide metabolites sphingosine and sphingosine-1-phosphate (S1P) are important bioregulatory molecules. Ceramide hydrolysis in the nucleated cell layers regulates keratinocyte proliferation and apoptosis in response to external stress. Ceramide hydrolysis also occurs at the stratum corneum, releasing free sphingoid base that functions as an endogenous antimicrobial agent. ACER1 is highly expressed in epidermis and catalyzes the hydrolysis of very long chain ceramides to generate sphingosine (Houben et al., 2006 (PubMed 16477081); Sun et al., 2008 (PubMed 17713573)).(supplied by OMIM, Jul 2010)

UniProtKB Summary for ACER1
Function: Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid at an optimal pH of 8.0. Has a highly restricted substrate specificity for the natural stereoisomer of ceramide with D-erythro-sphingosine but not D-ribo-phytosphingosine or D-erythro-dihydrosphingosine as a backbone. May have a role in regulating the levels of bioactive lipids ceramide and sphingosine 1-phosphate, as well as complex sphingolipids (By similarity)

Tocris Summary for ACER1
Ceramidases (EC are a group of enzymes which catalyze the hydrolysis of ceramides to produce sphingosine, which subsequently undergoes phosphorylation to generate sphingosine-1-phosphate (S1P). Ceramide and its downstream products, sphingosine and S1P, are bioactive lipids that mediate various cellular processes including cell growth arrest, differentiation and apoptosis.

[Reference: ]
External IDs
Hgnc ID: 18356 EntrezGene ID: 125981 Ensembl ID: ENSG00000167769
[Reference: ]
Reference Source

Gene Reference Into Function (GeneRIF)

PubMed IDGeneRIF TextLast Update
11915342regulates the signaling system mediated by sphingolipids2010-01-21
17713573upregulation of haCER1 and AC mediates the Ca2+(o)-induced growth arrest and differentiation of keratinocytes by generating sphingosine and its phosphate2010-01-21


Relevant citations within the PubMed literature


Putative/known Functions


Homologues, Orthologues, Paralogues and Family

Sequence Similarity and Functional Annotation

Sequence Similarity

Db NameQuery UniSubject UniSequence LengthAlignment LengthIdentityCoverageMismatchesGap OpeningsQuery StartQuery EndSubject StartSubject EndEvalueBit Score
Reviewed non-human mammalian with experimental evidenceACER1_HUMANACER1_MOUSE26426479.551005401264102732.00E-124441
Islam MT, Garg G, Hancock WS, Risk BA, Baker MS, Ranganathan S (2014) Protannotator: A Semiautomated Pipeline for Chromosome-Wise Functional Annotation of the "Missing" Human Proteome. J Proteome Res. 13, 76-83.

KEGG Pathways

Pathway IDDatabase NamePathway Name
hsa00600KEGG PATHWAY@@Sphingolipid metabolism
hsa01100KEGG PATHWAYMetabolic pathways
Islam MT, Garg G, Hancock WS, Risk BA, Baker MS, Ranganathan S (2014) Protannotator: A Semiautomated Pipeline for Chromosome-Wise Functional Annotation of the "Missing" Human Proteome. J Proteome Res. 13, 76-83.

Post Translational Modifications

Protein Protein Interactions

Best Available Mass Spectra without FDR


Evidence File
Fenyö, David; Beavis, Ronald C. (2015). "The GPMDB REST interface". Bioinformatics 31 (12): 2056–2058. doi:10.1093/bioinformatics/btv107. ISSN 1367-4803. ">Global Proteome Machine Database - THE GPM


Peptide SequenceScoresPride IDSpectrum IDAnnotation
No results found.
Evidence File
Vizcaino JA, et al. 2016 update of the PRIDE database and related tools. Nucleic Acids Res. 2016 Jan 1;44(D1):D447-D456. ">PRIDE Archive

Proteomics DB

Evidence File
Wilhelm, M et al. (2014) Mass-spectrometry-based draft of the human proteome. Nature. 509:582-7. ">Proteomics DB