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P45381

- ACY2_HUMAN

UniProt

P45381 - ACY2_HUMAN

Protein

Aspartoacylase

Gene

ASPA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate. NAA occurs in high concentration in brain and its hydrolysis NAA plays a significant part in the maintenance of intact white matter. In other tissues it act as a scavenger of NAA from body fluids.

    Catalytic activityi

    N-acyl-L-aspartate + H2O = a carboxylate + L-aspartate.1 Publication

    Cofactori

    Binds 1 zinc ion per subunit.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi21 – 211Zinc
    Metal bindingi24 – 241Zinc
    Binding sitei63 – 631Substrate
    Metal bindingi116 – 1161Zinc
    Active sitei178 – 17811 Publication
    Binding sitei178 – 1781Substrate
    Binding sitei288 – 2881Substrate

    GO - Molecular functioni

    1. aminoacylase activity Source: ProtInc
    2. aspartoacylase activity Source: UniProtKB-EC
    3. hydrolase activity, acting on ester bonds Source: InterPro
    4. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. aspartate catabolic process Source: ProtInc
    2. central nervous system myelination Source: Ensembl
    3. positive regulation of oligodendrocyte differentiation Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03094-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aspartoacylase (EC:3.5.1.15)
    Alternative name(s):
    Aminoacylase-2
    Short name:
    ACY-2
    Gene namesi
    Name:ASPA
    Synonyms:ACY2, ASP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:756. ASPA.

    Subcellular locationi

    Cytoplasm. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. extracellular vesicular exosome Source: UniProt
    3. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Canavan disease (CAND) [MIM:271900]: A rare neurodegenerative condition of infancy or childhood characterized by white matter vacuolization and demyelination that gives rise to a spongy appearance. The clinical features are onset in early infancy, atonia of neck muscles, hypotonia, hyperextension of legs and flexion of arms, blindness, severe mental defect, megalocephaly, and death by 18 months on the average.11 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161I → T in CAND; <0.5% residual enzyme activity. 2 Publications
    VAR_039079
    Natural varianti21 – 211H → P in CAND. 1 Publication
    VAR_016778
    Natural varianti24 – 241E → G in CAND. 1 Publication
    VAR_016782
    Natural varianti27 – 271G → R in CAND; 3% residual enzyme activity. 2 Publications
    VAR_039080
    Natural varianti57 – 571A → T in CAND. 1 Publication
    VAR_016779
    Natural varianti68 – 681D → A in CAND. 1 Publication
    VAR_016783
    Natural varianti114 – 1141D → E in CAND; <0.5% residual enzyme activity. 1 Publication
    VAR_039081
    Natural varianti114 – 1141D → Y in CAND. 1 Publication
    VAR_016784
    Natural varianti123 – 1231G → E in CAND; about 25% residual enzyme activity. 1 Publication
    VAR_039082
    Natural varianti143 – 1431I → T in CAND; in a Japanese patient. 1 Publication
    VAR_004995
    Natural varianti152 – 1521C → R in CAND; loss of activity. 1 Publication
    VAR_004996
    Natural varianti152 – 1521C → W in CAND. 1 Publication
    VAR_016785
    Natural varianti152 – 1521C → Y in CAND; <0.5% residual enzyme activity. 1 Publication
    VAR_039083
    Natural varianti168 – 1681R → C in CAND; undetectable enzyme activity. 1 Publication
    VAR_039084
    Natural varianti168 – 1681R → H in CAND. 1 Publication
    VAR_016780
    Natural varianti176 – 1772Missing in CAND.
    VAR_004997
    Natural varianti181 – 1811P → T in CAND. 1 Publication
    VAR_016781
    Natural varianti183 – 1831P → H in CAND. 1 Publication
    VAR_039085
    Natural varianti186 – 1861V → F in CAND. 1 Publication
    VAR_039086
    Natural varianti195 – 1951M → R in CAND. 1 Publication
    VAR_039087
    Natural varianti231 – 2311Y → C in CAND. 1 Publication
    VAR_016786
    Natural varianti244 – 2441H → R in CAND. 1 Publication
    VAR_016787
    Natural varianti249 – 2491D → V in CAND. 2 Publications
    VAR_016788
    Natural varianti274 – 2741G → R in CAND. 2 Publications
    VAR_004998
    Natural varianti280 – 2801P → L in CAND. 1 Publication
    VAR_039088
    Natural varianti280 – 2801P → S in CAND. 1 Publication
    VAR_039089
    Natural varianti285 – 2851E → A in CAND; predominant mutation in Ashkenazi Jewish population; 99% loss of activity. 3 Publications
    Corresponds to variant rs28940279 [ dbSNP | Ensembl ].
    VAR_004999
    Natural varianti287 – 2871A → T in CAND. 1 Publication
    VAR_039090
    Natural varianti295 – 2951F → S in CAND. 2 Publications
    VAR_005000
    Natural varianti305 – 3051A → E in CAND; loss of activity; pan-European origin; most prevalent among non-Jewish CAND patients; probably the most ancient mutation. 4 Publications
    Corresponds to variant rs28940574 [ dbSNP | Ensembl ].
    VAR_005001

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi71 – 711R → K: Reduces activity by 99%. 1 Publication
    Mutagenesisi164 – 1641Y → F: Reduces activity by 99%. 1 Publication
    Mutagenesisi168 – 1681R → K: Reduces activity by 99%. 1 Publication
    Mutagenesisi178 – 1781E → A: Reduces activity by 99%. 2 Publications
    Mutagenesisi178 – 1781E → D: Abolishes enzymatic activity. 2 Publications
    Mutagenesisi178 – 1781E → Q: Abolishes enzymatic activity. 2 Publications
    Mutagenesisi285 – 2851E → D: 5-fold decrease in activity. 1 Publication
    Mutagenesisi288 – 2881Y → F: Reduces activity by 99%. 1 Publication

    Keywords - Diseasei

    Disease mutation, Leukodystrophy

    Organism-specific databases

    MIMi271900. phenotype.
    Orphaneti314918. Mild Canavan disease.
    314911. Severe Canavan disease.
    PharmGKBiPA25055.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 313313AspartoacylasePRO_0000216871Add
    BLAST

    Proteomic databases

    PaxDbiP45381.
    PRIDEiP45381.

    PTM databases

    PhosphoSiteiP45381.

    Expressioni

    Tissue specificityi

    Brain white matter, skeletal muscle, kidney, adrenal glands, lung and liver.

    Gene expression databases

    ArrayExpressiP45381.
    BgeeiP45381.
    CleanExiHS_ASPA.
    GenevestigatoriP45381.

    Organism-specific databases

    HPAiHPA022142.
    HPA022145.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi106935. 1 interaction.
    DIPiDIP-60793N.
    MINTiMINT-1440951.
    STRINGi9606.ENSP00000263080.

    Structurei

    Secondary structure

    1
    313
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 186
    Helixi25 – 3410
    Helixi39 – 413
    Beta strandi46 – 538
    Helixi55 – 606
    Beta strandi65 – 673
    Helixi69 – 713
    Helixi75 – 784
    Helixi88 – 10013
    Beta strandi105 – 1084
    Beta strandi110 – 1178
    Beta strandi119 – 1213
    Beta strandi123 – 1297
    Helixi134 – 14714
    Beta strandi152 – 1565
    Beta strandi160 – 1623
    Helixi167 – 1704
    Beta strandi171 – 18010
    Helixi189 – 21022
    Beta strandi218 – 22912
    Beta strandi235 – 2373
    Beta strandi241 – 2433
    Turni245 – 2495
    Beta strandi259 – 2635
    Beta strandi269 – 2713
    Beta strandi274 – 2763
    Beta strandi278 – 2825
    Helixi286 – 2883
    Turni289 – 2924
    Beta strandi294 – 30512

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2I3CX-ray2.80A/B2-313[»]
    2O4HX-ray2.70A/B1-313[»]
    2O53X-ray2.70A/B1-313[»]
    2Q51X-ray2.80A/B2-313[»]
    ProteinModelPortaliP45381.
    SMRiP45381. Positions 9-310.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP45381.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni70 – 712Substrate binding
    Regioni164 – 1685Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2988.
    HOGENOMiHOG000232489.
    HOVERGENiHBG004172.
    InParanoidiP45381.
    KOiK01437.
    OMAiTTRSVAK.
    PhylomeDBiP45381.
    TreeFamiTF328708.

    Family and domain databases

    HAMAPiMF_00704. Aspartoacylase.
    InterProiIPR016708. Aspartoacylase.
    IPR007036. Aste_AspA.
    [Graphical view]
    PfamiPF04952. AstE_AspA. 1 hit.
    [Graphical view]
    PIRSFiPIRSF018001. Aspartoacylase. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P45381-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSCHIAEEH IQKVAIFGGT HGNELTGVFL VKHWLENGAE IQRTGLEVKP    50
    FITNPRAVKK CTRYIDCDLN RIFDLENLGK KMSEDLPYEV RRAQEINHLF 100
    GPKDSEDSYD IIFDLHNTTS NMGCTLILED SRNNFLIQMF HYIKTSLAPL 150
    PCYVYLIEHP SLKYATTRSI AKYPVGIEVG PQPQGVLRAD ILDQMRKMIK 200
    HALDFIHHFN EGKEFPPCAI EVYKIIEKVD YPRDENGEIA AIIHPNLQDQ 250
    DWKPLHPGDP MFLTLDGKTI PLGGDCTVYP VFVNEAAYYE KKEAFAKTTK 300
    LTLNAKSIRC CLH 313
    Length:313
    Mass (Da):35,735
    Last modified:November 1, 1995 - v1
    Checksum:i33C0B9B07839E7F5
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161I → T in CAND; <0.5% residual enzyme activity. 2 Publications
    VAR_039079
    Natural varianti21 – 211H → P in CAND. 1 Publication
    VAR_016778
    Natural varianti24 – 241E → G in CAND. 1 Publication
    VAR_016782
    Natural varianti27 – 271G → R in CAND; 3% residual enzyme activity. 2 Publications
    VAR_039080
    Natural varianti57 – 571A → T in CAND. 1 Publication
    VAR_016779
    Natural varianti68 – 681D → A in CAND. 1 Publication
    VAR_016783
    Natural varianti114 – 1141D → E in CAND; <0.5% residual enzyme activity. 1 Publication
    VAR_039081
    Natural varianti114 – 1141D → Y in CAND. 1 Publication
    VAR_016784
    Natural varianti123 – 1231G → E in CAND; about 25% residual enzyme activity. 1 Publication
    VAR_039082
    Natural varianti143 – 1431I → T in CAND; in a Japanese patient. 1 Publication
    VAR_004995
    Natural varianti152 – 1521C → R in CAND; loss of activity. 1 Publication
    VAR_004996
    Natural varianti152 – 1521C → W in CAND. 1 Publication
    VAR_016785
    Natural varianti152 – 1521C → Y in CAND; <0.5% residual enzyme activity. 1 Publication
    VAR_039083
    Natural varianti168 – 1681R → C in CAND; undetectable enzyme activity. 1 Publication
    VAR_039084
    Natural varianti168 – 1681R → H in CAND. 1 Publication
    VAR_016780
    Natural varianti176 – 1772Missing in CAND.
    VAR_004997
    Natural varianti181 – 1811P → T in CAND. 1 Publication
    VAR_016781
    Natural varianti183 – 1831P → H in CAND. 1 Publication
    VAR_039085
    Natural varianti186 – 1861V → F in CAND. 1 Publication
    VAR_039086
    Natural varianti195 – 1951M → R in CAND. 1 Publication
    VAR_039087
    Natural varianti231 – 2311Y → C in CAND. 1 Publication
    VAR_016786
    Natural varianti244 – 2441H → R in CAND. 1 Publication
    VAR_016787
    Natural varianti249 – 2491D → V in CAND. 2 Publications
    VAR_016788
    Natural varianti274 – 2741G → R in CAND. 2 Publications
    VAR_004998
    Natural varianti280 – 2801P → L in CAND. 1 Publication
    VAR_039088
    Natural varianti280 – 2801P → S in CAND. 1 Publication
    VAR_039089
    Natural varianti285 – 2851E → A in CAND; predominant mutation in Ashkenazi Jewish population; 99% loss of activity. 3 Publications
    Corresponds to variant rs28940279 [ dbSNP | Ensembl ].
    VAR_004999
    Natural varianti287 – 2871A → T in CAND. 1 Publication
    VAR_039090
    Natural varianti295 – 2951F → S in CAND. 2 Publications
    VAR_005000
    Natural varianti305 – 3051A → E in CAND; loss of activity; pan-European origin; most prevalent among non-Jewish CAND patients; probably the most ancient mutation. 4 Publications
    Corresponds to variant rs28940574 [ dbSNP | Ensembl ].
    VAR_005001
    Natural varianti310 – 3101C → G.1 Publication
    VAR_039091

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S67156 mRNA. Translation: AAB29190.1.
    BC029128 mRNA. Translation: AAH29128.1.
    CCDSiCCDS11028.1.
    PIRiS38538.
    RefSeqiNP_000040.1. NM_000049.2.
    NP_001121557.1. NM_001128085.1.
    XP_006721590.1. XM_006721527.1.
    UniGeneiHs.171142.

    Genome annotation databases

    EnsembliENST00000263080; ENSP00000263080; ENSG00000108381.
    ENST00000456349; ENSP00000409976; ENSG00000108381.
    GeneIDi443.
    KEGGihsa:443.
    UCSCiuc002fvq.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S67156 mRNA. Translation: AAB29190.1 .
    BC029128 mRNA. Translation: AAH29128.1 .
    CCDSi CCDS11028.1.
    PIRi S38538.
    RefSeqi NP_000040.1. NM_000049.2.
    NP_001121557.1. NM_001128085.1.
    XP_006721590.1. XM_006721527.1.
    UniGenei Hs.171142.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2I3C X-ray 2.80 A/B 2-313 [» ]
    2O4H X-ray 2.70 A/B 1-313 [» ]
    2O53 X-ray 2.70 A/B 1-313 [» ]
    2Q51 X-ray 2.80 A/B 2-313 [» ]
    ProteinModelPortali P45381.
    SMRi P45381. Positions 9-310.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106935. 1 interaction.
    DIPi DIP-60793N.
    MINTi MINT-1440951.
    STRINGi 9606.ENSP00000263080.

    Chemistry

    DrugBanki DB00128. L-Aspartic Acid.

    PTM databases

    PhosphoSitei P45381.

    Proteomic databases

    PaxDbi P45381.
    PRIDEi P45381.

    Protocols and materials databases

    DNASUi 443.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263080 ; ENSP00000263080 ; ENSG00000108381 .
    ENST00000456349 ; ENSP00000409976 ; ENSG00000108381 .
    GeneIDi 443.
    KEGGi hsa:443.
    UCSCi uc002fvq.3. human.

    Organism-specific databases

    CTDi 443.
    GeneCardsi GC17P003326.
    GeneReviewsi ASPA.
    HGNCi HGNC:756. ASPA.
    HPAi HPA022142.
    HPA022145.
    MIMi 271900. phenotype.
    608034. gene.
    neXtProti NX_P45381.
    Orphaneti 314918. Mild Canavan disease.
    314911. Severe Canavan disease.
    PharmGKBi PA25055.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2988.
    HOGENOMi HOG000232489.
    HOVERGENi HBG004172.
    InParanoidi P45381.
    KOi K01437.
    OMAi TTRSVAK.
    PhylomeDBi P45381.
    TreeFami TF328708.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS03094-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P45381.
    GenomeRNAii 443.
    NextBioi 1855.
    PROi P45381.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P45381.
    Bgeei P45381.
    CleanExi HS_ASPA.
    Genevestigatori P45381.

    Family and domain databases

    HAMAPi MF_00704. Aspartoacylase.
    InterProi IPR016708. Aspartoacylase.
    IPR007036. Aste_AspA.
    [Graphical view ]
    Pfami PF04952. AstE_AspA. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF018001. Aspartoacylase. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of the human aspartoacylase cDNA and a common missense mutation in Canavan disease."
      Kaul R., Gao G.P., Balamurugan K., Matalon R.
      Nat. Genet. 5:118-123(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CAND ALA-285.
      Tissue: Kidney.
    2. "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].
      Tissue: Brain.
    3. "Purification and preliminary characterization of brain aspartoacylase."
      Moore R.A., Le Coq J., Faehnle C.R., Viola R.E.
      Arch. Biochem. Biophys. 413:1-8(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, CHARACTERIZATION OF VARIANT CAND ALA-285, MUTAGENESIS OF GLU-285.
      Tissue: Brain.
    4. "Identification of the zinc binding ligands and the catalytic residue in human aspartoacylase, an enzyme involved in Canavan disease."
      Herga S., Berrin J.G., Perrier J., Puigserver A., Giardina T.
      FEBS Lett. 580:5899-5904(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, ZINC-BINDING SITES, ACTIVE SITE, MUTAGENESIS OF GLU-178.
    5. "Examination of the mechanism of human brain aspartoacylase through the binding of an intermediate analogue."
      Le Coq J., Pavlovsky A., Malik R., Sanishvili R., Xu C., Viola R.E.
      Biochemistry 47:3484-3492(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEXES WITH ZINC IONS; PHOSPHATE AND N-PHOSPHONOMETHYL-L-ASPARTATE, COFACTOR, SUBUNIT, MUTAGENESIS OF ARG-71; TYR-164; ARG-168; GLU-178 AND TYR-288.
    6. "Structure of aspartoacylase, the brain enzyme impaired in Canavan disease."
      Bitto E., Bingman C.A., Wesenberg G.E., McCoy J.G., Phillips G.N. Jr.
      Proc. Natl. Acad. Sci. U.S.A. 104:456-461(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH ZINC IONS, SUBUNIT, COFACTOR.
    7. "Canavan disease: mutations among Jewish and non-Jewish patients."
      Kaul R., Gao G.P., Aloya M., Balamurugan K., Petrosky A., Michals K., Matalon R.
      Am. J. Hum. Genet. 55:34-41(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CAND ALA-285 AND GLU-305.
    8. "The molecular basis of canavan (aspartoacylase deficiency) disease in European non-Jewish patients."
      Shaag A., Anikster Y., Christensen E., Glustein J.Z., Fois A., Michelakakis H., Nigro F., Pronicka E., Ribes A., Zabot M.-T., Elpeleg O.N.
      Am. J. Hum. Genet. 57:572-580(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CAND 176-GLY-ILE-177 DEL; ARG-274; SER-295 AND GLU-305.
    9. "Novel (Cys152 > Arg) missense mutation in an Arab patient with Canavan disease."
      Kaul R., Gao G.P., Michals K., Whelan D.T., Levin S., Matalon R.
      Hum. Mutat. 5:269-271(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CAND ARG-152.
    10. "Identification and expression of eight novel mutations among non-Jewish patients with Canavan disease."
      Kaul R., Gao G.P., Matalon R., Aloya M., Su Q., Jin M., Johnson A.B., Schutgens R.B.H., Clarke J.T.R.
      Am. J. Hum. Genet. 59:95-102(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CAND THR-16; ARG-27; GLU-114; GLU-123; TYR-152; CYS-168; ALA-285 AND GLU-305, VARIANT GLY-310, CHARACTERIZATION OF VARIANTS CAND THR-16; ARG-27; GLU-114; GLU-123; TYR-152 AND CYS-168.
    11. "Missense mutation (I143T) in a Japanese patient with Canavan disease."
      Kobayashi K., Tsujino S., Ezoe T., Hamaguchi H., Nihei K., Sakuragawa N.
      Hum. Mutat. Suppl. 1:S308-S309(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CAND THR-143.
    12. "Novel missense mutation (Y231C) in a Turkish patient with Canavan disease."
      Rady P.L., Vargas T., Tyring S.K., Matalon R., Langenbeck U.
      Am. J. Med. Genet. 87:273-275(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CAND CYS-231.
    13. "The spectrum of mutations of the aspartoacylase gene in Canavan disease in non-Jewish patients."
      Elpeleg O.N., Shaag A.
      J. Inherit. Metab. Dis. 22:531-534(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CAND THR-16; ARG-27; HIS-183; PHE-186; ARG-195; ARG-274; SER-280; LEU-280; THR-287; SER-295 AND GLU-305.
    14. "Mutation detection in the aspartoacylase gene in 17 patients with Canavan disease: four new mutations in the non-Jewish population."
      Sistermans E.A., de Coo R.F., van Beerendonk H.M., Poll-The B.T., Kleijer W.J., van Oost B.A.
      Eur. J. Hum. Genet. 8:557-560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CAND PRO-21; THR-57; HIS-168 AND THR-181.
    15. "Identification and characterization of novel mutations of the aspartoacylase gene in non-Jewish patients with Canavan disease."
      Zeng B.J., Wang Z.H., Ribeiro L.A., Leone P., De Gasperi R., Kim S.J., Raghavan S., Ong E., Pastores G.M., Kolodny E.H.
      J. Inherit. Metab. Dis. 25:557-570(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CAND GLY-24; ALA-68; TRP-152; ARG-244 AND VAL-249.
    16. "Two novel aspartoacylase gene (ASPA) missense mutations specific to Norwegian and Swedish patients with Canavan disease."
      Olsen T.R., Tranebjaerg L., Kvittingen E.A., Hagenfeldt L., Moller C., Nilssen O.
      J. Med. Genet. 39:E55-E55(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CAND TYR-114 AND VAL-249.

    Entry informationi

    Entry nameiACY2_HUMAN
    AccessioniPrimary (citable) accession number: P45381
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 136 of the entry and version 1 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3