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Q9NR71

- ASAH2_HUMAN

UniProt

Q9NR71 - ASAH2_HUMAN

Protein

Neutral ceramidase

Gene

ASAH2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 2 (25 Jul 2006)
      Previous versions | rss
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    Functioni

    Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid at an optimal pH of 6.5-8.5. Acts as a key regulator of sphingolipid signaling metabolites by generating sphingosine at the cell surface. Acts as a repressor of apoptosis both by reducing C16-ceramide, thereby preventing ceramide-induced apoptosis, and generating sphingosine, a precursor of the antiapoptotic factor sphingosine 1-phosphate. Probably involved in the digestion of dietary sphingolipids in intestine by acting as a key enzyme for the catabolism of dietary sphingolipids and regulating the levels of bioactive sphingolipid metabolites in the intestinal tract.2 Publications

    Catalytic activityi

    N-acylsphingosine + H2O = a carboxylate + sphingosine.2 Publications

    Enzyme regulationi

    Inhibited by dithiothreitol (DTT), 2-mercaptoethanol, Zn2+, Cu2+ and Fe2+. Enhanced by Na+ and Ca2+, and at lower level Mg2+ and Mn2+.

    Kineticsi

    1. KM=71.4 µM for octanoyl-sphingosine2 Publications
    2. KM=66 µM for palmitoyl-sphingosine2 Publications
    3. KM=60.1 µM for D-erythro-C12-NBD-ceramide2 Publications

    Vmax=160 µmol/min/mg enzyme with octanoyl-sphingosine as substrate2 Publications

    Vmax=16 µmol/min/mg enzyme with palmitoyl-sphingosine as substrate2 Publications

    Vmax=0.68 nmol/min/mg enzyme with D-erythro-C12-NBD-ceramide as substrate2 Publications

    pH dependencei

    Optimum pH is 7.5-9.5.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei354 – 3541Nucleophile1 Publication

    GO - Molecular functioni

    1. ceramidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. ceramide metabolic process Source: ProtInc
    3. glycosphingolipid metabolic process Source: Reactome
    4. signal transduction Source: ProtInc
    5. small molecule metabolic process Source: Reactome
    6. sphingolipid metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Apoptosis, Lipid metabolism, Sphingolipid metabolism

    Enzyme and pathway databases

    BRENDAi3.5.1.23. 2681.
    ReactomeiREACT_116105. Glycosphingolipid metabolism.
    SABIO-RKQ9NR71.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neutral ceramidase (EC:3.5.1.23)
    Short name:
    N-CDase
    Short name:
    NCDase
    Alternative name(s):
    Acylsphingosine deacylase 2
    BCDase
    LCDase
    Short name:
    hCD
    N-acylsphingosine amidohydrolase 2
    Non-lysosomal ceramidase
    Cleaved into the following chain:
    Gene namesi
    Name:ASAH2
    Synonyms:HNAC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:18860. ASAH2.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type II membrane protein 1 Publication
    Note: The neutral ceramidase soluble form is a secreted protein. According to PubMed:10781606, it is mitochondrial. However, they used a shorter form in its N-terminus, which may explain this localization which probably does not exist in vivo.

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. mitochondrion Source: ProtInc
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi258 – 2581S → A: Impairs enzyme activity. 1 Publication
    Mutagenesisi352 – 3521D → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi354 – 3541S → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi362 – 3621C → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi374 – 3741S → A: Impairs enzyme activity. 1 Publication
    Mutagenesisi396 – 3961S → A: No effect. 1 Publication
    Mutagenesisi595 – 5951S → A: Impairs enzyme activity. 1 Publication
    Mutagenesisi729 – 7291S → A: Impairs enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA134977109.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 780780Neutral ceramidasePRO_0000247099Add
    BLAST
    Chaini99 – 780682Neutral ceramidase soluble formBy similarityPRO_0000247100Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi62 – 621O-linked (GalNAc...)Sequence Analysis
    Glycosylationi67 – 671O-linked (GalNAc...)Sequence Analysis
    Glycosylationi68 – 681O-linked (GalNAc...)Sequence Analysis
    Glycosylationi70 – 701O-linked (GalNAc...)Sequence Analysis
    Glycosylationi73 – 731O-linked (GalNAc...)Sequence Analysis
    Glycosylationi74 – 741O-linked (GalNAc...)Sequence Analysis
    Glycosylationi76 – 761O-linked (GalNAc...)Sequence Analysis
    Glycosylationi78 – 781O-linked (GalNAc...)Sequence Analysis
    Glycosylationi79 – 791O-linked (GalNAc...)Sequence Analysis
    Glycosylationi80 – 801O-linked (GalNAc...)Sequence Analysis
    Glycosylationi82 – 821O-linked (GalNAc...)Sequence Analysis
    Glycosylationi84 – 841O-linked (GalNAc...)Sequence Analysis
    Glycosylationi98 – 981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi217 – 2171N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi468 – 4681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi564 – 5641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi730 – 7301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi779 – 7791O-linked (GalNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated. Required for enzyme activity By similarity.By similarity
    O-glycosylated. Required to retain it as a type II membrane protein at the cell surface.1 Publication
    Phosphorylated. May prevent ubiquitination and subsequent degradation By similarity.By similarity
    Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is triggered by nitric oxid By similarity.By similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9NR71.
    PaxDbiQ9NR71.
    PRIDEiQ9NR71.

    Expressioni

    Tissue specificityi

    Primarily expressed in the intestine (PubMed:17334805). Ubiquitously expressed with higher levels in kidney, skeletal muscle and heart (PubMed:10781606). According to PubMed:17334805, ubiquitous expression attributed to ASAH2 may be actually that of the paralog ASAH2B.2 Publications

    Gene expression databases

    BgeeiQ9NR71.
    CleanExiHS_ASAH2.
    GenevestigatoriQ9NR71.

    Interactioni

    Protein-protein interaction databases

    BioGridi121160. 1 interaction.
    575684. 1 interaction.
    STRINGi9606.ENSP00000378897.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NR71.
    SMRiQ9NR71. Positions 102-778.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini34 – 780747LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei13 – 3321Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni770 – 78011Required for correct folding and localizationBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the neutral ceramidase family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG75118.
    HOVERGENiHBG080870.
    InParanoidiQ9NR71.
    KOiK12349.
    OMAiGAFCESP.
    OrthoDBiEOG7WQ7RQ.
    PhylomeDBiQ9NR71.
    TreeFamiTF300786.

    Family and domain databases

    InterProiIPR006823. Ceramidase_alk.
    [Graphical view]
    PANTHERiPTHR12670. PTHR12670. 1 hit.
    PfamiPF04734. Ceramidase_alk. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NR71-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAKRTFSNLE TFLIFLLVMM SAITVALLSL LFITSGTIEN HKDLGGHFFS    50
    TTQSPPATQG STAAQRSTAT QHSTATQSST ATQTSPVPLT PESPLFQNFS 100
    GYHIGVGRAD CTGQVADINL MGYGKSGQNA QGILTRLYSR AFIMAEPDGS 150
    NRTVFVSIDI GMVSQRLRLE VLNRLQSKYG SLYRRDNVIL SGTHTHSGPA 200
    GYFQYTVFVI ASEGFSNQTF QHMVTGILKS IDIAHTNMKP GKIFINKGNV 250
    DGVQINRSPY SYLQNPQSER ARYSSNTDKE MIVLKMVDLN GDDLGLISWF 300
    AIHPVSMNNS NHLVNSDNVG YASYLLEQEK NKGYLPGQGP FVAAFASSNL 350
    GDVSPNILGP RCINTGESCD NANSTCPIGG PSMCIAKGPG QDMFDSTQII 400
    GRAMYQRAKE LYASASQEVT GPLASAHQWV DMTDVTVWLN STHASKTCKP 450
    ALGYSFAAGT IDGVGGLNFT QGKTEGDPFW DTIRDQILGK PSEEIKECHK 500
    PKPILLHTGE LSKPHPWHPD IVDVQIITLG SLAITAIPGE FTTMSGRRLR 550
    EAVQAEFASH GMQNMTVVIS GLCNVYTHYI TTYEEYQAQR YEAASTIYGP 600
    HTLSAYIQLF RNLAKAIATD TVANLSRGPE PPFFKQLIVP LIPSIVDRAP 650
    KGRTFGDVLQ PAKPEYRVGE VAEVIFVGAN PKNSVQNQTH QTFLTVEKYE 700
    ATSTSWQIVC NDASWETRFY WHKGLLGLSN ATVEWHIPDT AQPGIYRIRY 750
    FGHNRKQDIL KPAVILSFEG TSPAFEVVTI 780
    Length:780
    Mass (Da):85,516
    Last modified:July 25, 2006 - v2
    Checksum:iD2BD7947B022A619
    GO
    Isoform 2 (identifier: Q9NR71-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         410-444: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:745
    Mass (Da):81,718
    Checksum:iB4577FFD1C6397EA
    GO

    Sequence cautioni

    The sequence AAL06061.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAI15870.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti274 – 2741S → P in AAL06061. (PubMed:14557071)Curated
    Sequence conflicti274 – 2741S → P in AAF86240. (PubMed:10781606)Curated
    Sequence conflicti602 – 6021T → A in AAL06061. (PubMed:14557071)Curated
    Sequence conflicti602 – 6021T → A in AAF86240. (PubMed:10781606)Curated
    Sequence conflicti689 – 6891T → N in CAI17190. (PubMed:15164054)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti51 – 511T → A.
    Corresponds to variant rs7067625 [ dbSNP | Ensembl ].
    VAR_027064
    Natural varianti346 – 3461A → S.
    Corresponds to variant rs993869 [ dbSNP | Ensembl ].
    VAR_027065

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei410 – 44435Missing in isoform 2. 1 PublicationVSP_019928Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY049008 Genomic DNA. Translation: AAL06061.1. Different initiation.
    AF449759 mRNA. Translation: AAQ04667.2.
    AL450382 Genomic DNA. Translation: CAI15870.1. Different initiation.
    AL589794 Genomic DNA. Translation: CAI15766.1. Sequence problems.
    AL589794 Genomic DNA. Translation: CAI15767.1. Sequence problems.
    AL954360 Genomic DNA. Translation: CAI17190.1.
    AF250847 mRNA. Translation: AAF86240.1.
    BC107105 mRNA. Translation: AAI07106.1.
    CCDSiCCDS44398.1. [Q9NR71-2]
    CCDS7239.2. [Q9NR71-1]
    RefSeqiNP_001137446.1. NM_001143974.1. [Q9NR71-2]
    NP_063946.2. NM_019893.2. [Q9NR71-1]
    UniGeneiHs.512645.

    Genome annotation databases

    EnsembliENST00000329428; ENSP00000329886; ENSG00000188611.
    ENST00000395526; ENSP00000378897; ENSG00000188611. [Q9NR71-1]
    ENST00000447815; ENSP00000388206; ENSG00000188611. [Q9NR71-2]
    GeneIDi56624.
    KEGGihsa:56624.
    UCSCiuc001jjd.3. human. [Q9NR71-1]
    uc009xos.3. human. [Q9NR71-2]

    Polymorphism databases

    DMDMi110832757.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY049008 Genomic DNA. Translation: AAL06061.1 . Different initiation.
    AF449759 mRNA. Translation: AAQ04667.2 .
    AL450382 Genomic DNA. Translation: CAI15870.1 . Different initiation.
    AL589794 Genomic DNA. Translation: CAI15766.1 . Sequence problems.
    AL589794 Genomic DNA. Translation: CAI15767.1 . Sequence problems.
    AL954360 Genomic DNA. Translation: CAI17190.1 .
    AF250847 mRNA. Translation: AAF86240.1 .
    BC107105 mRNA. Translation: AAI07106.1 .
    CCDSi CCDS44398.1. [Q9NR71-2 ]
    CCDS7239.2. [Q9NR71-1 ]
    RefSeqi NP_001137446.1. NM_001143974.1. [Q9NR71-2 ]
    NP_063946.2. NM_019893.2. [Q9NR71-1 ]
    UniGenei Hs.512645.

    3D structure databases

    ProteinModelPortali Q9NR71.
    SMRi Q9NR71. Positions 102-778.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121160. 1 interaction.
    575684. 1 interaction.
    STRINGi 9606.ENSP00000378897.

    Chemistry

    ChEMBLi CHEMBL2021754.

    Polymorphism databases

    DMDMi 110832757.

    Proteomic databases

    MaxQBi Q9NR71.
    PaxDbi Q9NR71.
    PRIDEi Q9NR71.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000329428 ; ENSP00000329886 ; ENSG00000188611 .
    ENST00000395526 ; ENSP00000378897 ; ENSG00000188611 . [Q9NR71-1 ]
    ENST00000447815 ; ENSP00000388206 ; ENSG00000188611 . [Q9NR71-2 ]
    GeneIDi 56624.
    KEGGi hsa:56624.
    UCSCi uc001jjd.3. human. [Q9NR71-1 ]
    uc009xos.3. human. [Q9NR71-2 ]

    Organism-specific databases

    CTDi 56624.
    GeneCardsi GC10M051944.
    H-InvDB HIX0058802.
    HGNCi HGNC:18860. ASAH2.
    MIMi 611202. gene.
    neXtProti NX_Q9NR71.
    PharmGKBi PA134977109.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG75118.
    HOVERGENi HBG080870.
    InParanoidi Q9NR71.
    KOi K12349.
    OMAi GAFCESP.
    OrthoDBi EOG7WQ7RQ.
    PhylomeDBi Q9NR71.
    TreeFami TF300786.

    Enzyme and pathway databases

    BRENDAi 3.5.1.23. 2681.
    Reactomei REACT_116105. Glycosphingolipid metabolism.
    SABIO-RK Q9NR71.

    Miscellaneous databases

    GeneWikii ASAH2.
    GenomeRNAii 56624.
    NextBioi 62071.
    PROi Q9NR71.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9NR71.
    CleanExi HS_ASAH2.
    Genevestigatori Q9NR71.

    Family and domain databases

    InterProi IPR006823. Ceramidase_alk.
    [Graphical view ]
    PANTHERi PTHR12670. PTHR12670. 1 hit.
    Pfami PF04734. Ceramidase_alk. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Neutral ceramidase gene: role in regulating ceramide-induced apoptosis."
      Choi M.S., Anderson M.A., Zhang Z., Zimonjic D.B., Popescu N., Mukherjee A.B.
      Gene 315:113-122(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Roles for C16-ceramide and sphingosine 1-phosphate in regulating hepatocyte apoptosis in response to tumor necrosis factor-alpha."
      Osawa Y., Uchinami H., Bielawski J., Schwabe R.F., Hannun Y.A., Brenner D.A.
      J. Biol. Chem. 280:27879-27887(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    3. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Molecular cloning and characterization of a human mitochondrial ceramidase."
      El Bawab S., Roddy P., Qian T., Bielawska A., Lemasters J.J., Hannun Y.A.
      J. Biol. Chem. 275:21508-21513(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-780 (ISOFORM 1), ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, POSSIBLE SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-780 (ISOFORM 2).
    6. "Subcellular localization of human neutral ceramidase expressed in HEK293 cells."
      Hwang Y.H., Tani M., Nakagawa T., Okino N., Ito M.
      Biochem. Biophys. Res. Commun. 331:37-42(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION.
    7. "Mechanisms of sphingosine and sphingosine 1-phosphate generation in human platelets."
      Tani M., Sano T., Ito M., Igarashi Y.
      J. Lipid Res. 46:2458-2467(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Identification of a novel amidase motif in neutral ceramidase."
      Galadari S., Wu B.X., Mao C., Roddy P., El Bawab S., Hannun Y.A.
      Biochem. J. 393:687-695(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, MUTAGENESIS OF SER-258; ASP-352; SER-354; CYS-362; SER-374; SER-396; SER-595 AND SER-729.
    9. "A novel gene derived from a segmental duplication shows perturbed expression in Alzheimer's disease."
      Avramopoulos D., Wang R., Valle D., Fallin M.D., Bassett S.S.
      Neurogenetics 8:111-120(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiASAH2_HUMAN
    AccessioniPrimary (citable) accession number: Q9NR71
    Secondary accession number(s): Q3KNU1
    , Q5SNT7, Q5SZP6, Q5SZP7, Q5T1D5, Q71ME6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: July 25, 2006
    Last modified: October 1, 2014
    This is version 101 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3