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{{Infobox_gene}}
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The '''ASAH1''' [[gene]] encodes in humans the ''acid [[ceramidase]]'' [[enzyme]].<ref name="pmid8955159">{{cite journal | vauthors = Koch J, Gartner S, Li CM, Quintern LE, Bernardo K, Levran O, Schnabel D, Desnick RJ, Schuchman EH, Sandhoff K | title = Molecular cloning and characterization of a full-length complementary DNA encoding human acid ceramidase. Identification Of the first molecular lesion causing Farber disease | journal = J Biol Chem | volume = 271 | issue = 51 | pages = 33110–5 |date=Jan 1997 | pmid = 8955159 | pmc =  | doi =10.1074/jbc.271.51.33110 }}</ref><ref name="pmid10610716">{{cite journal | vauthors = Li CM, Park JH, He X, Levy B, Chen F, Arai K, Adler DA, Disteche CM, Koch J, Sandhoff K, Schuchman EH | title = The human acid ceramidase gene (ASAH): structure, chromosomal location, mutation analysis, and expression | journal = Genomics | volume = 62 | issue = 2 | pages = 223–31 |date=Feb 2000 | pmid = 10610716 | pmc =  | doi = 10.1006/geno.1999.5940 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ASAH1 N-acylsphingosine amidohydrolase (acid ceramidase) 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=427| accessdate = }}</ref>
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{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = N-acylsphingosine amidohydrolase (acid ceramidase) 1
| HGNCid = 735
| Symbol = ASAH1
| AltSymbols =; AC; ASAH; FLJ21558; FLJ22079; PHP; PHP32
| OMIM = 228000
| ECnumber =
| Homologene = 10504
| MGIid = 1277124
  | GeneAtlas_image1 = PBB_GE_ASAH1_210980_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ASAH1_213702_x_at_tn.png
  | Function = {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0017040 |text = ceramidase activity}} {{GNF_GO|id=GO:0046912 |text = transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer}}
| Component = {{GNF_GO|id=GO:0005764 |text = lysosome}}
| Process = {{GNF_GO|id=GO:0006631 |text = fatty acid metabolic process}} {{GNF_GO|id=GO:0006672 |text = ceramide metabolic process}} {{GNF_GO|id=GO:0019752 |text = carboxylic acid metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 427
    | Hs_Ensembl = ENSG00000104763
    | Hs_RefseqProtein = NP_004306
    | Hs_RefseqmRNA = NM_004315
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 8
    | Hs_GenLoc_start = 17958214
    | Hs_GenLoc_end = 17986757
    | Hs_Uniprot = Q13510
    | Mm_EntrezGene = 11886
    | Mm_Ensembl = ENSMUSG00000031591
    | Mm_RefseqmRNA = NM_019734
    | Mm_RefseqProtein = NP_062708
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 42839468
    | Mm_GenLoc_end = 42873466
    | Mm_Uniprot = Q3TWT5
  }}
}}
'''N-acylsphingosine amidohydrolase (acid ceramidase) 1''', also known as '''ASAH1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ASAH1 N-acylsphingosine amidohydrolase (acid ceramidase) 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=427| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = This gene encodes a heterodimeric protein consisting of a nonglycosylated alpha subunit and a glycosylated beta subunit that is cleaved to the mature enzyme posttranslationally. The encoded protein catalyzes the synthesis and degradation of ceramide into sphingosine and fatty acid. Mutations in this gene have been associated with a lysosomal storage disorder known as [[Farber disease]]. Two transcript variants encoding distinct isoforms have been identified for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: ASAH1 N-acylsphingosine amidohydrolase (acid ceramidase) 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=427| accessdate = }}</ref>
| summary_text = This gene encodes a [[Heterodimeric#Biochemistry|heterodimeric]] protein consisting of a nonglycosylated alpha subunit and a [[Glycosylation|glycosylated]] beta subunit that is cleaved to the mature enzyme [[Posttranslational modification|posttranslationally]]. The encoded protein catalyzes the synthesis and degradation of [[ceramide]] into [[sphingosine]] and fatty acid. Mutations in this gene have been associated with a [[lysosomal storage disorder]] known as [[Farber disease]] and, recently, with a rare neurodegenerative condition known as [[spinal muscular atrophy with progressive myoclonic epilepsy]].<ref>{{Cite journal | last1 = Zhou | first1 = J. | last2 = Tawk | first2 = M. | last3 = Tiziano | first3 = F. D. | last4 = Veillet | first4 = J. | last5 = Bayes | first5 = M. | last6 = Nolent | first6 = F. | last7 = Garcia | first7 = V. | last8 = Servidei | first8 = S. | last9 = Bertini | first9 = E. | last10 = Castro-Giner | first10 = F. | last11 = Renda | first11 = Y. | last12 = Carpentier | first12 = S. P. | last13 = Andrieu-Abadie | first13 = N. | last14 = Gut | first14 = I. | last15 = Levade | first15 = T. | last16 = Topaloglu | first16 = H. | last17 = Melki | first17 = J. | title = Spinal Muscular Atrophy Associated with Progressive Myoclonic Epilepsy is Caused by Mutations in ASAH1 | doi = 10.1016/j.ajhg.2012.05.001 | journal = The American Journal of Human Genetics | volume = 91 | issue = 1 | pages = 5–14 | year = 2012 | pmid = 22703880 | pmc =3397266 }}</ref> Two transcript variants encoding distinct isoforms have been identified for this gene.<ref name="entrez"/> In [[Melanocyte|melanocytic cells]] ASAH1 gene expression may be regulated by [[Microphthalmia-associated transcription factor|MITF]].<ref name="pmid19067971">{{cite journal | vauthors = Hoek KS, Schlegel NC, Eichhoff OM | title = Novel MITF targets identified using a two-step DNA microarray strategy | journal = Pigment Cell Melanoma Res. | volume = 21 | issue = 6 | pages = 665–76 | year = 2008 | pmid = 19067971 | doi = 10.1111/j.1755-148X.2008.00505.x |display-authors=etal}}</ref>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|ASAH1}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Perry DK, Hannun YA |title=The role of ceramide in cell signaling. |journal=Biochim. Biophys. Acta |volume=1436 |issue= 1-2 |pages= 233-43 |year= 1999 |pmid= 9838138 |doi=  }}
*{{cite journal  | vauthors=Perry DK, Hannun YA |title=The role of ceramide in cell signaling. |journal=Biochim. Biophys. Acta |volume=1436 |issue= 1-2 |pages= 233–43 |year= 1999 |pmid= 9838138 |doi=  10.1016/S0005-2760(98)00145-3}}
*{{cite journal  | author=Bernardo K, Hurwitz R, Zenk T, ''et al.'' |title=Purification, characterization, and biosynthesis of human acid ceramidase. |journal=J. Biol. Chem. |volume=270 |issue= 19 |pages= 11098-102 |year= 1995 |pmid= 7744740 |doi=  }}
*{{cite journal  | vauthors=Bernardo K, Hurwitz R, Zenk T |title=Purification, characterization, and biosynthesis of human acid ceramidase. |journal=J. Biol. Chem. |volume=270 |issue= 19 |pages= 11098–102 |year= 1995 |pmid= 7744740 |doi=10.1074/jbc.270.19.11098 |display-authors=etal}}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal  | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
*{{cite journal  | author=Koch J, Gärtner S, Li CM, ''et al.'' |title=Molecular cloning and characterization of a full-length complementary DNA encoding human acid ceramidase. Identification Of the first molecular lesion causing Farber disease. |journal=J. Biol. Chem. |volume=271 |issue= 51 |pages= 33110-5 |year= 1997 |pmid= 8955159 |doi= }}
*{{cite journal  | vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  |display-authors=etal}}
*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal  | vauthors=Seelan RS, Qian C, Yokomizo A |title=Human acid ceramidase is overexpressed but not mutated in prostate cancer. |journal=Genes Chromosomes Cancer |volume=29 |issue= 2 |pages= 137–46 |year= 2000 |pmid= 10959093 |doi=10.1002/1098-2264(2000)9999:9999<::AID-GCC1018>3.0.CO;2-E |display-authors=etal}}
*{{cite journal  | author=Li CM, Park JH, He X, ''et al.'' |title=The human acid ceramidase gene (ASAH): structure, chromosomal location, mutation analysis, and expression. |journal=Genomics |volume=62 |issue= 2 |pages= 223-31 |year= 2000 |pmid= 10610716 |doi= 10.1006/geno.1999.5940 }}
*{{cite journal  | vauthors=Strelow A, Bernardo K, Adam-Klages S |title=Overexpression of acid ceramidase protects from tumor necrosis factor-induced cell death. |journal=J. Exp. Med. |volume=192 |issue= 5 |pages= 601–12 |year= 2000 |pmid= 10974027 |doi=10.1084/jem.192.5.601  | pmc=2193270 |display-authors=etal}}
*{{cite journal  | author=Seelan RS, Qian C, Yokomizo A, ''et al.'' |title=Human acid ceramidase is overexpressed but not mutated in prostate cancer. |journal=Genes Chromosomes Cancer |volume=29 |issue= 2 |pages= 137-46 |year= 2000 |pmid= 10959093 |doi=  }}
*{{cite journal  | vauthors=Bär J, Linke T, Ferlinz K |title=Molecular analysis of acid ceramidase deficiency in patients with Farber disease. |journal=Hum. Mutat. |volume=17 |issue= 3 |pages= 199–209 |year= 2001 |pmid= 11241842 |doi= 10.1002/humu.5 |display-authors=etal}}
*{{cite journal  | author=Strelow A, Bernardo K, Adam-Klages S, ''et al.'' |title=Overexpression of acid ceramidase protects from tumor necrosis factor-induced cell death. |journal=J. Exp. Med. |volume=192 |issue= 5 |pages= 601-12 |year= 2000 |pmid= 10974027 |doi=  }}
*{{cite journal  | vauthors=Ferlinz K, Kopal G, Bernardo K |title=Human acid ceramidase: processing, glycosylation, and lysosomal targeting. |journal=J. Biol. Chem. |volume=276 |issue= 38 |pages= 35352–60 |year= 2001 |pmid= 11451951 |doi= 10.1074/jbc.M103066200 |display-authors=etal}}
*{{cite journal  | author=Bär J, Linke T, Ferlinz K, ''et al.'' |title=Molecular analysis of acid ceramidase deficiency in patients with Farber disease. |journal=Hum. Mutat. |volume=17 |issue= 3 |pages= 199-209 |year= 2001 |pmid= 11241842 |doi= 10.1002/humu.5 }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}}
*{{cite journal  | author=Ferlinz K, Kopal G, Bernardo K, ''et al.'' |title=Human acid ceramidase: processing, glycosylation, and lysosomal targeting. |journal=J. Biol. Chem. |volume=276 |issue= 38 |pages= 35352-60 |year= 2001 |pmid= 11451951 |doi= 10.1074/jbc.M103066200 }}
*{{cite journal  | vauthors=Muramatsu T, Sakai N, Yanagihara I |title=Mutation analysis of the acid ceramidase gene in Japanese patients with Farber disease. |journal=J. Inherit. Metab. Dis. |volume=25 |issue= 7 |pages= 585–92 |year= 2003 |pmid= 12638942 |doi=10.1023/A:1022047408477 |display-authors=etal}}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | vauthors=Zhang H, Li XJ, Martin DB, Aebersold R |title=Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. |journal=Nat. Biotechnol. |volume=21 |issue= 6 |pages= 660–6 |year= 2003 |pmid= 12754519 |doi= 10.1038/nbt827 }}
*{{cite journal  | author=Muramatsu T, Sakai N, Yanagihara I, ''et al.'' |title=Mutation analysis of the acid ceramidase gene in Japanese patients with Farber disease. |journal=J. Inherit. Metab. Dis. |volume=25 |issue= 7 |pages= 585-92 |year= 2003 |pmid= 12638942 |doi=  }}
*{{cite journal  | vauthors=Okino N, He X, Gatt S |title=The reverse activity of human acid ceramidase. |journal=J. Biol. Chem. |volume=278 |issue= 32 |pages= 29948–53 |year= 2003 |pmid= 12764132 |doi= 10.1074/jbc.M303310200 |display-authors=etal}}
*{{cite journal  | author=Zhang H, Li XJ, Martin DB, Aebersold R |title=Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. |journal=Nat. Biotechnol. |volume=21 |issue= 6 |pages= 660-6 |year= 2003 |pmid= 12754519 |doi= 10.1038/nbt827 }}
*{{cite journal  | vauthors=He X, Okino N, Dhami R |title=Purification and characterization of recombinant, human acid ceramidase. Catalytic reactions and interactions with acid sphingomyelinase. |journal=J. Biol. Chem. |volume=278 |issue= 35 |pages= 32978–86 |year= 2003 |pmid= 12815059 |doi= 10.1074/jbc.M301936200 |display-authors=etal}}
*{{cite journal  | author=Okino N, He X, Gatt S, ''et al.'' |title=The reverse activity of human acid ceramidase. |journal=J. Biol. Chem. |volume=278 |issue= 32 |pages= 29948-53 |year= 2003 |pmid= 12764132 |doi= 10.1074/jbc.M303310200 }}
*{{cite journal  | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
*{{cite journal  | author=He X, Okino N, Dhami R, ''et al.'' |title=Purification and characterization of recombinant, human acid ceramidase. Catalytic reactions and interactions with acid sphingomyelinase. |journal=J. Biol. Chem. |volume=278 |issue= 35 |pages= 32978-86 |year= 2003 |pmid= 12815059 |doi= 10.1074/jbc.M301936200 }}
*{{cite journal  | vauthors=Hara S, Nakashima S, Kiyono T |title=p53-Independent ceramide formation in human glioma cells during gamma-radiation-induced apoptosis. |journal=Cell Death Differ. |volume=11 |issue= 8 |pages= 853–61 |year= 2005 |pmid= 15088070 |doi= 10.1038/sj.cdd.4401428 |display-authors=etal}}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}}
*{{cite journal  | author=Hara S, Nakashima S, Kiyono T, ''et al.'' |title=p53-Independent ceramide formation in human glioma cells during gamma-radiation-induced apoptosis. |journal=Cell Death Differ. |volume=11 |issue= 8 |pages= 853-61 |year= 2005 |pmid= 15088070 |doi= 10.1038/sj.cdd.4401428 }}
*{{cite journal  | vauthors=Lewandrowski U, Moebius J, Walter U, Sickmann A |title=Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach. |journal=Mol. Cell. Proteomics |volume=5 |issue= 2 |pages= 226–33 |year= 2006 |pmid= 16263699 |doi= 10.1074/mcp.M500324-MCP200 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Lewandrowski U, Moebius J, Walter U, Sickmann A |title=Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach. |journal=Mol. Cell Proteomics |volume=5 |issue= 2 |pages= 226-33 |year= 2006 |pmid= 16263699 |doi= 10.1074/mcp.M500324-MCP200 }}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{Glycolipid metabolism}}
{{Glycolipid metabolism}}
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Revision as of 07:46, 2 December 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
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Wikidata
View/Edit Human

The ASAH1 gene encodes in humans the acid ceramidase enzyme.[1][2][3]

This gene encodes a heterodimeric protein consisting of a nonglycosylated alpha subunit and a glycosylated beta subunit that is cleaved to the mature enzyme posttranslationally. The encoded protein catalyzes the synthesis and degradation of ceramide into sphingosine and fatty acid. Mutations in this gene have been associated with a lysosomal storage disorder known as Farber disease and, recently, with a rare neurodegenerative condition known as spinal muscular atrophy with progressive myoclonic epilepsy.[4] Two transcript variants encoding distinct isoforms have been identified for this gene.[3] In melanocytic cells ASAH1 gene expression may be regulated by MITF.[5]

References

  1. ↑ Koch J, Gartner S, Li CM, Quintern LE, Bernardo K, Levran O, Schnabel D, Desnick RJ, Schuchman EH, Sandhoff K (Jan 1997). "Molecular cloning and characterization of a full-length complementary DNA encoding human acid ceramidase. Identification Of the first molecular lesion causing Farber disease". J Biol Chem. 271 (51): 33110–5. doi:10.1074/jbc.271.51.33110. PMID 8955159.
  2. ↑ Li CM, Park JH, He X, Levy B, Chen F, Arai K, Adler DA, Disteche CM, Koch J, Sandhoff K, Schuchman EH (Feb 2000). "The human acid ceramidase gene (ASAH): structure, chromosomal location, mutation analysis, and expression". Genomics. 62 (2): 223–31. doi:10.1006/geno.1999.5940. PMID 10610716.
  3. ↑ 3.0 3.1 "Entrez Gene: ASAH1 N-acylsphingosine amidohydrolase (acid ceramidase) 1".
  4. ↑ Zhou, J.; Tawk, M.; Tiziano, F. D.; Veillet, J.; Bayes, M.; Nolent, F.; Garcia, V.; Servidei, S.; Bertini, E.; Castro-Giner, F.; Renda, Y.; Carpentier, S. P.; Andrieu-Abadie, N.; Gut, I.; Levade, T.; Topaloglu, H.; Melki, J. (2012). "Spinal Muscular Atrophy Associated with Progressive Myoclonic Epilepsy is Caused by Mutations in ASAH1". The American Journal of Human Genetics. 91 (1): 5–14. doi:10.1016/j.ajhg.2012.05.001. PMC 3397266. PMID 22703880.
  5. ↑ Hoek KS, Schlegel NC, Eichhoff OM, et al. (2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell Melanoma Res. 21 (6): 665–76. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971.

External links

Further reading



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