ASAHL

NAAA
Identifiers
AliasesNAAA, ASAHL, PLT, N-acylethanolamine acid amidase
External IDsMGI: 1914361 HomoloGene: 8686 GeneCards: NAAA
Gene location (Human)
Chr.Chromosome 4 (human)[1]
Band4q21.1Start75,913,657 bp[1]
End75,941,051 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

27163

67111

Ensembl

ENSG00000138744

ENSMUSG00000029413

UniProt

Q02083

Q9D7V9

RefSeq (mRNA)

NM_001042402
NM_014435
NM_001363719

NM_001163687
NM_025972

RefSeq (protein)

NP_001035861
NP_055250
NP_001350648

NP_001157159
NP_080248

Location (UCSC)Chr 4: 75.91 – 75.94 MbChr 5: 92.26 – 92.28 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

N-acylethanolamine-hydrolyzing acid amidase is an enzyme that in humans is encoded by the NAAA gene.[5][6][7]

This gene encodes an N-acylethanolamine-hydrolyzing enzyme which is highly similar to acid ceramidase. Multiple transcript variants encoding different isoforms have been found for this gene.[7]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000138744 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000029413 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ Hong SB, Li CM, Rhee HJ, Park JH, He X, Levy B, Yoo OJ, Schuchman EH (Feb 2000). "Molecular cloning and characterization of a human cDNA and gene encoding a novel acid ceramidase-like protein". Genomics. 62 (2): 232–41. doi:10.1006/geno.1999.5953. PMID 10610717.
  6. ↑ Goodchild NL, Wilkinson DA, Mager DL (Dec 1992). "A human endogenous long terminal repeat provides a polyadenylation signal to a novel, alternatively spliced transcript in normal placenta". Gene. 121 (2): 287–94. doi:10.1016/0378-1119(92)90133-A. PMID 1446826.
  7. 1 2 "Entrez Gene: ASAHL N-acylsphingosine amidohydrolase (acid ceramidase)-like".

Further reading

  • Schulze H, Schepers U, Sandhoff K (2008). "Overexpression and mass spectrometry analysis of mature human acid ceramidase". Biol. Chem. 388 (12): 1333–43. doi:10.1515/BC.2007.152. PMID 18020949.
  • Zhao LY, Tsuboi K, Okamoto Y, et al. (2008). "Proteolytic activation and glycosylation of N-acylethanolamine-hydrolyzing acid amidase, a lysosomal enzyme involved in the endocannabinoid metabolism". Biochim. Biophys. Acta. 1771 (11): 1397–405. doi:10.1016/j.bbalip.2007.10.002. PMID 17980170.
  • Oh JH, Yang JO, Hahn Y, et al. (2006). "Transcriptome analysis of human gastric cancer". Mamm. Genome. 16 (12): 942–54. doi:10.1007/s00335-005-0075-2. PMID 16341674.
  • Tsuboi K, Sun YX, Okamoto Y, et al. (2005). "Molecular characterization of N-acylethanolamine-hydrolyzing acid amidase, a novel member of the choloylglycine hydrolase family with structural and functional similarity to acid ceramidase". J. Biol. Chem. 280 (12): 11082–92. doi:10.1074/jbc.M413473200. PMID 15655246.
  • Huang Y, Tanimukai H, Liu F, et al. (2005). "Elevation of the level and activity of acid ceramidase in Alzheimer's disease brain". Eur. J. Neurosci. 20 (12): 3489–97. doi:10.1111/j.1460-9568.2004.03852.x. PMID 15610181.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.


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