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Protein

Aspartoacylase

Gene

ASPA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.3 Publications

Cofactori

Zn2+2 PublicationsNote: Binds 1 zinc ion per subunit.2 Publications

Kineticsi

    1. Vmax=1.2 nmol/h/mg enzyme1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi21Zinc1
    Metal bindingi24Zinc1
    Binding sitei63Substrate1
    Metal bindingi116Zinc1
    Active sitei1781 Publication1
    Binding sitei178Substrate1
    Binding sitei288Substrate1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionHydrolase
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03094-MONOMER.
    BRENDAi3.5.1.15. 2681.
    ReactomeiR-HSA-70614. Amino acid synthesis and interconversion (transamination).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aspartoacylase (EC:3.5.1.152 Publications)
    Alternative name(s):
    Aminoacylase-2
    Short name:
    ACY-2
    Gene namesi
    Name:ASPA
    Synonyms:ACY2, ASP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:756. ASPA.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: HPA
    • extracellular exosome Source: UniProtKB
    • nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Canavan disease (CAND)14 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA 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.
    See also OMIM:271900
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_03907916I → T in CAND; <0.5% residual enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs769653717Ensembl.1
    Natural variantiVAR_01677821H → P in CAND. 1 Publication1
    Natural variantiVAR_01678224E → G in CAND. 1 PublicationCorresponds to variant dbSNP:rs104894551Ensembl.1
    Natural variantiVAR_07808624E → K in CAND; <1% residual enzyme activity. 1 Publication1
    Natural variantiVAR_03908027G → R in CAND; 3% residual enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs766328537Ensembl.1
    Natural variantiVAR_07808730L → P in CAND; <1% residual enzyme activity. 1 Publication1
    Natural variantiVAR_01677957A → T in CAND. 1 Publication1
    Natural variantiVAR_07808857A → V in CAND; <1% residual enzyme activity. 1 Publication1
    Natural variantiVAR_07808963R → T in CAND; <1% residual enzyme activity. 1 Publication1
    Natural variantiVAR_01678368D → A in CAND. 1 Publication1
    Natural variantiVAR_07809069L → R in CAND; <1% residual enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs776777887Ensembl.1
    Natural variantiVAR_078091101G → V in CAND; <1% residual enzyme activity. 1 Publication1
    Natural variantiVAR_039081114D → E in CAND; <0.5% residual enzyme activity. 1 Publication1
    Natural variantiVAR_016784114D → Y in CAND. 1 Publication1
    Natural variantiVAR_039082123G → E in CAND; about 25% residual enzyme activity. 1 Publication1
    Natural variantiVAR_078092129E → K in CAND; <1% residual enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs773049803Ensembl.1
    Natural variantiVAR_004995143I → T in CAND. 1 PublicationCorresponds to variant dbSNP:rs777936704Ensembl.1
    Natural variantiVAR_004996152C → R in CAND; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs104894548Ensembl.1
    Natural variantiVAR_016785152C → W in CAND. 1 Publication1
    Natural variantiVAR_039083152C → Y in CAND; <0.5% residual enzyme activity. 1 Publication1
    Natural variantiVAR_039084168R → C in CAND; undetectable enzyme activity. 1 Publication1
    Natural variantiVAR_016780168R → H in CAND. 1 PublicationCorresponds to variant dbSNP:rs770706390Ensembl.1
    Natural variantiVAR_078093170I → T in CAND; 5.5% residual enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs144321760Ensembl.1
    Natural variantiVAR_004997176 – 177Missing in CAND. 1 Publication2
    Natural variantiVAR_078094177I → T in CAND; Loss of catalytic activity. 1 Publication1
    Natural variantiVAR_078095180G → V in CAND; <1% residual enzyme activity. 1 Publication1
    Natural variantiVAR_016781181P → T in CAND. 1 PublicationCorresponds to variant dbSNP:rs786204572Ensembl.1
    Natural variantiVAR_039085183P → H in CAND. 1 Publication1
    Natural variantiVAR_039086186V → F in CAND. 1 Publication1
    Natural variantiVAR_039087195M → R in CAND. 1 Publication1
    Natural variantiVAR_078096204D → H in CAND; 12% residual enzyme activity. 1 Publication1
    Natural variantiVAR_016786231Y → C in CAND. 1 PublicationCorresponds to variant dbSNP:rs104894550Ensembl.1
    Natural variantiVAR_016787244H → R in CAND. 1 Publication1
    Natural variantiVAR_078097248Q → R in CAND; <1% residual enzyme activity. 1 Publication1
    Natural variantiVAR_016788249D → V in CAND. 2 PublicationsCorresponds to variant dbSNP:rs104894552Ensembl.1
    Natural variantiVAR_004998274G → R in CAND. 2 PublicationsCorresponds to variant dbSNP:rs761064915Ensembl.1
    Natural variantiVAR_039088280P → L in CAND. 1 Publication1
    Natural variantiVAR_039089280P → S in CAND. 1 PublicationCorresponds to variant dbSNP:rs750505963Ensembl.1
    Natural variantiVAR_004999285E → A in CAND; predominant mutation in Ashkenazi Jewish population; 99% loss of activity. 5 PublicationsCorresponds to variant dbSNP:rs28940279Ensembl.1
    Natural variantiVAR_078098286A → D in CAND; <1% residual enzyme activity. 1 Publication1
    Natural variantiVAR_039090287A → T in CAND. 1 PublicationCorresponds to variant dbSNP:rs774323189Ensembl.1
    Natural variantiVAR_005000295F → S in CAND. 2 Publications1
    Natural variantiVAR_005001305A → E in CAND; pan-European origin; most prevalent among non-Jewish CAND patients; probably the most ancient mutation; loss of activity. 4 PublicationsCorresponds to variant dbSNP:rs28940574Ensembl.1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi71R → K: Reduces activity by 99%. 1 Publication1
    Mutagenesisi164Y → F: Reduces activity by 99%. 1 Publication1
    Mutagenesisi168R → K: Reduces activity by 99%. 1 Publication1
    Mutagenesisi178E → A: Reduces activity by 99%. 2 Publications1
    Mutagenesisi178E → D: Abolishes enzymatic activity. 2 Publications1
    Mutagenesisi178E → Q: Abolishes enzymatic activity. 2 Publications1
    Mutagenesisi285E → D: 5-fold decrease in activity. 1 Publication1
    Mutagenesisi288Y → F: Reduces activity by 99%. 1 Publication1

    Keywords - Diseasei

    Disease mutation, Leukodystrophy

    Organism-specific databases

    DisGeNETi443.
    MalaCardsiASPA.
    MIMi271900. phenotype.
    OpenTargetsiENSG00000108381.
    Orphaneti314918. Mild Canavan disease.
    314911. Severe Canavan disease.
    PharmGKBiPA25055.

    Chemistry databases

    DrugBankiDB00128. L-Aspartic Acid.

    Polymorphism and mutation databases

    BioMutaiASPA.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002168711 – 313AspartoacylaseAdd BLAST313

    Proteomic databases

    PaxDbiP45381.
    PeptideAtlasiP45381.
    PRIDEiP45381.

    PTM databases

    iPTMnetiP45381.
    PhosphoSitePlusiP45381.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    BgeeiENSG00000108381.
    CleanExiHS_ASPA.
    ExpressionAtlasiP45381. baseline and differential.
    GenevisibleiP45381. HS.

    Organism-specific databases

    HPAiHPA022142.
    HPA022145.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Binary interactionsi

    Show more details

    Protein-protein interaction databases

    BioGridi106935. 5 interactors.
    DIPiDIP-60793N.
    IntActiP45381. 3 interactors.
    MINTiMINT-1440951.
    STRINGi9606.ENSP00000263080.

    Structurei

    Secondary structure

    1313
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi14 – 18Combined sources5
    Helixi25 – 34Combined sources10
    Helixi39 – 41Combined sources3
    Beta strandi48 – 53Combined sources6
    Helixi55 – 59Combined sources5
    Beta strandi65 – 67Combined sources3
    Helixi69 – 71Combined sources3
    Helixi75 – 78Combined sources4
    Beta strandi84 – 86Combined sources3
    Helixi88 – 100Combined sources13
    Beta strandi105 – 108Combined sources4
    Beta strandi110 – 117Combined sources8
    Beta strandi119 – 121Combined sources3
    Beta strandi123 – 129Combined sources7
    Helixi134 – 147Combined sources14
    Beta strandi152 – 156Combined sources5
    Beta strandi160 – 162Combined sources3
    Helixi167 – 170Combined sources4
    Beta strandi171 – 181Combined sources11
    Helixi189 – 210Combined sources22
    Beta strandi218 – 229Combined sources12
    Beta strandi237 – 239Combined sources3
    Beta strandi241 – 243Combined sources3
    Turni245 – 249Combined sources5
    Beta strandi259 – 263Combined sources5
    Beta strandi269 – 271Combined sources3
    Beta strandi274 – 276Combined sources3
    Beta strandi278 – 282Combined sources5
    Helixi286 – 288Combined sources3
    Turni289 – 292Combined sources4
    Beta strandi294 – 305Combined sources12

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2I3CX-ray2.80A/B2-313[»]
    2O4HX-ray2.70A/B1-313[»]
    2O53X-ray2.70A/B1-313[»]
    2Q51X-ray2.80A/B2-313[»]
    4MRIX-ray2.80A/B1-313[»]
    4MXUX-ray2.60A/B1-313[»]
    4NFRX-ray3.00A/B1-313[»]
    4TNUX-ray2.90A/B1-313[»]
    ProteinModelPortaliP45381.
    SMRiP45381.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP45381.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni70 – 71Substrate binding2
    Regioni164 – 168Substrate binding5

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG410IERR. Eukaryota.
    COG2988. LUCA.
    GeneTreeiENSGT00390000001189.
    HOGENOMiHOG000232489.
    HOVERGENiHBG004172.
    InParanoidiP45381.
    KOiK01437.
    OMAiVYKIMEK.
    OrthoDBiEOG091G0BL6.
    PhylomeDBiP45381.
    TreeFamiTF328708.

    Family and domain databases

    CDDicd06909. M14_ASPA. 1 hit.
    HAMAPiMF_00704. Aspartoacylase. 1 hit.
    InterProiView protein in InterPro
    IPR016708. Aspartoacylase.
    IPR007036. Aste_AspA.
    PfamiView protein in Pfam
    PF04952. AstE_AspA. 1 hit.
    PIRSFiPIRSF018001. Aspartoacylase. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P45381-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTSCHIAEEH IQKVAIFGGT HGNELTGVFL VKHWLENGAE IQRTGLEVKP
    60 70 80 90 100
    FITNPRAVKK CTRYIDCDLN RIFDLENLGK KMSEDLPYEV RRAQEINHLF
    110 120 130 140 150
    GPKDSEDSYD IIFDLHNTTS NMGCTLILED SRNNFLIQMF HYIKTSLAPL
    160 170 180 190 200
    PCYVYLIEHP SLKYATTRSI AKYPVGIEVG PQPQGVLRAD ILDQMRKMIK
    210 220 230 240 250
    HALDFIHHFN EGKEFPPCAI EVYKIIEKVD YPRDENGEIA AIIHPNLQDQ
    260 270 280 290 300
    DWKPLHPGDP MFLTLDGKTI PLGGDCTVYP VFVNEAAYYE KKEAFAKTTK
    310
    LTLNAKSIRC CLH
    Length:313
    Mass (Da):35,735
    Last modified:November 1, 1995 - v1
    Checksum:i33C0B9B07839E7F5
    GO

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_03907916I → T in CAND; <0.5% residual enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs769653717Ensembl.1
    Natural variantiVAR_01677821H → P in CAND. 1 Publication1
    Natural variantiVAR_01678224E → G in CAND. 1 PublicationCorresponds to variant dbSNP:rs104894551Ensembl.1
    Natural variantiVAR_07808624E → K in CAND; <1% residual enzyme activity. 1 Publication1
    Natural variantiVAR_03908027G → R in CAND; 3% residual enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs766328537Ensembl.1
    Natural variantiVAR_07808730L → P in CAND; <1% residual enzyme activity. 1 Publication1
    Natural variantiVAR_01677957A → T in CAND. 1 Publication1
    Natural variantiVAR_07808857A → V in CAND; <1% residual enzyme activity. 1 Publication1
    Natural variantiVAR_07808963R → T in CAND; <1% residual enzyme activity. 1 Publication1
    Natural variantiVAR_01678368D → A in CAND. 1 Publication1
    Natural variantiVAR_07809069L → R in CAND; <1% residual enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs776777887Ensembl.1
    Natural variantiVAR_078091101G → V in CAND; <1% residual enzyme activity. 1 Publication1
    Natural variantiVAR_039081114D → E in CAND; <0.5% residual enzyme activity. 1 Publication1
    Natural variantiVAR_016784114D → Y in CAND. 1 Publication1
    Natural variantiVAR_039082123G → E in CAND; about 25% residual enzyme activity. 1 Publication1
    Natural variantiVAR_078092129E → K in CAND; <1% residual enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs773049803Ensembl.1
    Natural variantiVAR_004995143I → T in CAND. 1 PublicationCorresponds to variant dbSNP:rs777936704Ensembl.1
    Natural variantiVAR_004996152C → R in CAND; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs104894548Ensembl.1
    Natural variantiVAR_016785152C → W in CAND. 1 Publication1
    Natural variantiVAR_039083152C → Y in CAND; <0.5% residual enzyme activity. 1 Publication1
    Natural variantiVAR_039084168R → C in CAND; undetectable enzyme activity. 1 Publication1
    Natural variantiVAR_016780168R → H in CAND. 1 PublicationCorresponds to variant dbSNP:rs770706390Ensembl.1
    Natural variantiVAR_078093170I → T in CAND; 5.5% residual enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs144321760Ensembl.1
    Natural variantiVAR_004997176 – 177Missing in CAND. 1 Publication2
    Natural variantiVAR_078094177I → T in CAND; Loss of catalytic activity. 1 Publication1
    Natural variantiVAR_078095180G → V in CAND; <1% residual enzyme activity. 1 Publication1
    Natural variantiVAR_016781181P → T in CAND. 1 PublicationCorresponds to variant dbSNP:rs786204572Ensembl.1
    Natural variantiVAR_039085183P → H in CAND. 1 Publication1
    Natural variantiVAR_039086186V → F in CAND. 1 Publication1
    Natural variantiVAR_039087195M → R in CAND. 1 Publication1
    Natural variantiVAR_078096204D → H in CAND; 12% residual enzyme activity. 1 Publication1
    Natural variantiVAR_016786231Y → C in CAND. 1 PublicationCorresponds to variant dbSNP:rs104894550Ensembl.1
    Natural variantiVAR_016787244H → R in CAND. 1 Publication1
    Natural variantiVAR_078097248Q → R in CAND; <1% residual enzyme activity. 1 Publication1
    Natural variantiVAR_016788249D → V in CAND. 2 PublicationsCorresponds to variant dbSNP:rs104894552Ensembl.1
    Natural variantiVAR_004998274G → R in CAND. 2 PublicationsCorresponds to variant dbSNP:rs761064915Ensembl.1
    Natural variantiVAR_039088280P → L in CAND. 1 Publication1
    Natural variantiVAR_039089280P → S in CAND. 1 PublicationCorresponds to variant dbSNP:rs750505963Ensembl.1
    Natural variantiVAR_004999285E → A in CAND; predominant mutation in Ashkenazi Jewish population; 99% loss of activity. 5 PublicationsCorresponds to variant dbSNP:rs28940279Ensembl.1
    Natural variantiVAR_078098286A → D in CAND; <1% residual enzyme activity. 1 Publication1
    Natural variantiVAR_039090287A → T in CAND. 1 PublicationCorresponds to variant dbSNP:rs774323189Ensembl.1
    Natural variantiVAR_005000295F → S in CAND. 2 Publications1
    Natural variantiVAR_005001305A → E in CAND; pan-European origin; most prevalent among non-Jewish CAND patients; probably the most ancient mutation; loss of activity. 4 PublicationsCorresponds to variant dbSNP:rs28940574Ensembl.1
    Natural variantiVAR_039091310C → G1 PublicationCorresponds to variant dbSNP:rs376854191Ensembl.1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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_016880150.1. XM_017024661.1.
    UniGeneiHs.171142.

    Genome annotation databases

    EnsembliENST00000263080; ENSP00000263080; ENSG00000108381.
    ENST00000456349; ENSP00000409976; ENSG00000108381.
    GeneIDi443.
    KEGGihsa:443.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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_016880150.1. XM_017024661.1.
    UniGeneiHs.171142.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2I3CX-ray2.80A/B2-313[»]
    2O4HX-ray2.70A/B1-313[»]
    2O53X-ray2.70A/B1-313[»]
    2Q51X-ray2.80A/B2-313[»]
    4MRIX-ray2.80A/B1-313[»]
    4MXUX-ray2.60A/B1-313[»]
    4NFRX-ray3.00A/B1-313[»]
    4TNUX-ray2.90A/B1-313[»]
    ProteinModelPortaliP45381.
    SMRiP45381.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi106935. 5 interactors.
    DIPiDIP-60793N.
    IntActiP45381. 3 interactors.
    MINTiMINT-1440951.
    STRINGi9606.ENSP00000263080.

    Chemistry databases

    DrugBankiDB00128. L-Aspartic Acid.

    PTM databases

    iPTMnetiP45381.
    PhosphoSitePlusiP45381.

    Polymorphism and mutation databases

    BioMutaiASPA.

    Proteomic databases

    PaxDbiP45381.
    PeptideAtlasiP45381.
    PRIDEiP45381.

    Protocols and materials databases

    DNASUi443.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000263080; ENSP00000263080; ENSG00000108381.
    ENST00000456349; ENSP00000409976; ENSG00000108381.
    GeneIDi443.
    KEGGihsa:443.

    Organism-specific databases

    CTDi443.
    DisGeNETi443.
    GeneCardsiASPA.
    GeneReviewsiASPA.
    HGNCiHGNC:756. ASPA.
    HPAiHPA022142.
    HPA022145.
    MalaCardsiASPA.
    MIMi271900. phenotype.
    608034. gene.
    neXtProtiNX_P45381.
    OpenTargetsiENSG00000108381.
    Orphaneti314918. Mild Canavan disease.
    314911. Severe Canavan disease.
    PharmGKBiPA25055.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiENOG410IERR. Eukaryota.
    COG2988. LUCA.
    GeneTreeiENSGT00390000001189.
    HOGENOMiHOG000232489.
    HOVERGENiHBG004172.
    InParanoidiP45381.
    KOiK01437.
    OMAiVYKIMEK.
    OrthoDBiEOG091G0BL6.
    PhylomeDBiP45381.
    TreeFamiTF328708.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03094-MONOMER.
    BRENDAi3.5.1.15. 2681.
    ReactomeiR-HSA-70614. Amino acid synthesis and interconversion (transamination).

    Miscellaneous databases

    EvolutionaryTraceiP45381.
    GenomeRNAii443.
    PROiPR:P45381.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000108381.
    CleanExiHS_ASPA.
    ExpressionAtlasiP45381. baseline and differential.
    GenevisibleiP45381. HS.

    Family and domain databases

    CDDicd06909. M14_ASPA. 1 hit.
    HAMAPiMF_00704. Aspartoacylase. 1 hit.
    InterProiView protein in InterPro
    IPR016708. Aspartoacylase.
    IPR007036. Aste_AspA.
    PfamiView protein in Pfam
    PF04952. AstE_AspA. 1 hit.
    PIRSFiPIRSF018001. Aspartoacylase. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiACY2_HUMAN
    AccessioniPrimary (citable) accession number: P45381
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: June 7, 2017
    This is version 162 of the entry and version 1 of the sequence. See 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.