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Entry version 179 (16 Oct 2019)
Sequence version 1 (01 Nov 1995)
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Protein

Aspartoacylase

Gene

ASPA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

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

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi21Zinc1
    Metal bindingi24Zinc1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei63Substrate1
    Metal bindingi116Zinc1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1781 Publication1
    Binding sitei178Substrate1
    Binding sitei288Substrate1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionHydrolase
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:HS03094-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.5.1.15 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-8963693 Aspartate and asparagine metabolism

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Aspartoacylase (EC:3.5.1.152 Publications)
    Alternative name(s):
    Aminoacylase-2
    Short name:
    ACY-2
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:ASPA
    Synonyms:ACY2, ASP
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 17

    Organism-specific databases

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:756 ASPA

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    608034 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P45381

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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.
    Related information in OMIM
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_03907916I → T in CAND; <0.5% residual enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs769653717EnsemblClinVar.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:rs766328537EnsemblClinVar.1
    Natural variantiVAR_07808730L → P in CAND; <1% residual enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs1555538144EnsemblClinVar.1
    Natural variantiVAR_01677957A → T in CAND. 1 Publication1
    Natural variantiVAR_07808857A → V in CAND; <1% residual enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs1555538148EnsemblClinVar.1
    Natural variantiVAR_07808963R → T in CAND; <1% residual enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs1555538151EnsemblClinVar.1
    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 PublicationCorresponds to variant dbSNP:rs1446467099EnsemblClinVar.1
    Natural variantiVAR_039082123G → E in CAND; about 25% residual enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs1057521115EnsemblClinVar.1
    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:rs777936704EnsemblClinVar.1
    Natural variantiVAR_004996152C → R in CAND; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs104894548EnsemblClinVar.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 PublicationCorresponds to variant dbSNP:rs937670540Ensembl.1
    Natural variantiVAR_016780168R → H in CAND. 1 PublicationCorresponds to variant dbSNP:rs770706390EnsemblClinVar.1
    Natural variantiVAR_078093170I → T in CAND; 5.5% residual enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs144321760EnsemblClinVar.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 PublicationCorresponds to variant dbSNP:rs1014551540EnsemblClinVar.1
    Natural variantiVAR_016781181P → T in CAND. 1 PublicationCorresponds to variant dbSNP:rs786204572EnsemblClinVar.1
    Natural variantiVAR_039085183P → H in CAND. 1 PublicationCorresponds to variant dbSNP:rs1555539857EnsemblClinVar.1
    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 PublicationCorresponds to variant dbSNP:rs1057516995EnsemblClinVar.1
    Natural variantiVAR_078097248Q → R in CAND; <1% residual enzyme activity. 1 Publication1
    Natural variantiVAR_016788249D → V in CAND. 2 PublicationsCorresponds to variant dbSNP:rs104894552EnsemblClinVar.1
    Natural variantiVAR_004998274G → R in CAND. 2 PublicationsCorresponds to variant dbSNP:rs761064915EnsemblClinVar.1
    Natural variantiVAR_039088280P → L in CAND. 1 PublicationCorresponds to variant dbSNP:rs1555541310EnsemblClinVar.1
    Natural variantiVAR_039089280P → S in CAND. 1 PublicationCorresponds to variant dbSNP:rs750505963EnsemblClinVar.1
    Natural variantiVAR_004999285E → A in CAND; predominant mutation in Ashkenazi Jewish population; 99% loss of activity. 5 PublicationsCorresponds to variant dbSNP:rs28940279EnsemblClinVar.1
    Natural variantiVAR_078098286A → D in CAND; <1% residual enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs1414684396Ensembl.1
    Natural variantiVAR_039090287A → T in CAND. 1 PublicationCorresponds to variant dbSNP:rs774323189EnsemblClinVar.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:rs28940574EnsemblClinVar.1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

    DisGeNET

    More...
    DisGeNETi
    443

    GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

    More...
    GeneReviewsi
    ASPA

    MalaCards human disease database

    More...
    MalaCardsi
    ASPA
    MIMi271900 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000108381

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...
    Orphaneti
    314918 Mild Canavan disease
    314911 Severe Canavan disease

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA25055

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...
    Pharosi
    P45381

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB00128 Aspartic acid
    DB01593 Zinc
    DB14487 Zinc acetate
    DB14533 Zinc chloride

    DrugCentral

    More...
    DrugCentrali
    P45381

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    ASPA

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002168711 – 313AspartoacylaseAdd BLAST313

    Proteomic databases

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    P45381

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P45381

    PeptideAtlas

    More...
    PeptideAtlasi
    P45381

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P45381

    ProteomicsDB: a multi-organism proteome resource

    More...
    ProteomicsDBi
    55676

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P45381

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    P45381

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000108381 Expressed in 185 organ(s), highest expression level in corpus callosum

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P45381 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P45381 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    HPA022142
    HPA022145

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.

    2 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    106935, 5 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-60793N

    Protein interaction database and analysis system

    More...
    IntActi
    P45381, 7 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000263080

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1313
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P45381

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P45381

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni70 – 71Substrate binding2
    Regioni164 – 168Substrate binding5

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG410IERR Eukaryota
    COG2988 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00390000001189

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000232489

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P45381

    KEGG Orthology (KO)

    More...
    KOi
    K01437

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    THGNEIN

    Database of Orthologous Groups

    More...
    OrthoDBi
    1074294at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P45381

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF328708

    Family and domain databases

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00704 Aspartoacylase, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR016708 Aspartoacylase
    IPR007036 Aste_AspA

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF04952 AstE_AspA, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF018001 Aspartoacylase, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

    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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i33C0B9B07839E7F5
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    I3L0T3I3L0T3_HUMAN
    Aspartoacylase
    ASPA
    78Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    I3L4M0I3L4M0_HUMAN
    Aspartoacylase
    ASPA
    56Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_03907916I → T in CAND; <0.5% residual enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs769653717EnsemblClinVar.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:rs766328537EnsemblClinVar.1
    Natural variantiVAR_07808730L → P in CAND; <1% residual enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs1555538144EnsemblClinVar.1
    Natural variantiVAR_01677957A → T in CAND. 1 Publication1
    Natural variantiVAR_07808857A → V in CAND; <1% residual enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs1555538148EnsemblClinVar.1
    Natural variantiVAR_07808963R → T in CAND; <1% residual enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs1555538151EnsemblClinVar.1
    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 PublicationCorresponds to variant dbSNP:rs1446467099EnsemblClinVar.1
    Natural variantiVAR_039082123G → E in CAND; about 25% residual enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs1057521115EnsemblClinVar.1
    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:rs777936704EnsemblClinVar.1
    Natural variantiVAR_004996152C → R in CAND; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs104894548EnsemblClinVar.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 PublicationCorresponds to variant dbSNP:rs937670540Ensembl.1
    Natural variantiVAR_016780168R → H in CAND. 1 PublicationCorresponds to variant dbSNP:rs770706390EnsemblClinVar.1
    Natural variantiVAR_078093170I → T in CAND; 5.5% residual enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs144321760EnsemblClinVar.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 PublicationCorresponds to variant dbSNP:rs1014551540EnsemblClinVar.1
    Natural variantiVAR_016781181P → T in CAND. 1 PublicationCorresponds to variant dbSNP:rs786204572EnsemblClinVar.1
    Natural variantiVAR_039085183P → H in CAND. 1 PublicationCorresponds to variant dbSNP:rs1555539857EnsemblClinVar.1
    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 PublicationCorresponds to variant dbSNP:rs1057516995EnsemblClinVar.1
    Natural variantiVAR_078097248Q → R in CAND; <1% residual enzyme activity. 1 Publication1
    Natural variantiVAR_016788249D → V in CAND. 2 PublicationsCorresponds to variant dbSNP:rs104894552EnsemblClinVar.1
    Natural variantiVAR_004998274G → R in CAND. 2 PublicationsCorresponds to variant dbSNP:rs761064915EnsemblClinVar.1
    Natural variantiVAR_039088280P → L in CAND. 1 PublicationCorresponds to variant dbSNP:rs1555541310EnsemblClinVar.1
    Natural variantiVAR_039089280P → S in CAND. 1 PublicationCorresponds to variant dbSNP:rs750505963EnsemblClinVar.1
    Natural variantiVAR_004999285E → A in CAND; predominant mutation in Ashkenazi Jewish population; 99% loss of activity. 5 PublicationsCorresponds to variant dbSNP:rs28940279EnsemblClinVar.1
    Natural variantiVAR_078098286A → D in CAND; <1% residual enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs1414684396Ensembl.1
    Natural variantiVAR_039090287A → T in CAND. 1 PublicationCorresponds to variant dbSNP:rs774323189EnsemblClinVar.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:rs28940574EnsemblClinVar.1
    Natural variantiVAR_039091310C → G1 PublicationCorresponds to variant dbSNP:rs376854191Ensembl.1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    S67156 mRNA Translation: AAB29190.1
    BC029128 mRNA Translation: AAH29128.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS11028.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S38538

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_000040.1, NM_000049.2
    NP_001121557.1, NM_001128085.1
    XP_016880150.1, XM_017024661.1

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000263080; ENSP00000263080; ENSG00000108381
    ENST00000456349; ENSP00000409976; ENSG00000108381

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    443

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:443

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    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[»]
    SMRiP45381
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi106935, 5 interactors
    DIPiDIP-60793N
    IntActiP45381, 7 interactors
    STRINGi9606.ENSP00000263080

    Chemistry databases

    DrugBankiDB00128 Aspartic acid
    DB01593 Zinc
    DB14487 Zinc acetate
    DB14533 Zinc chloride
    DrugCentraliP45381

    PTM databases

    iPTMnetiP45381
    PhosphoSitePlusiP45381

    Polymorphism and mutation databases

    BioMutaiASPA

    Proteomic databases

    MassIVEiP45381
    PaxDbiP45381
    PeptideAtlasiP45381
    PRIDEiP45381
    ProteomicsDBi55676

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    443

    Genome annotation databases

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

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    443
    DisGeNETi443

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    ASPA
    GeneReviewsiASPA
    HGNCiHGNC:756 ASPA
    HPAiHPA022142
    HPA022145
    MalaCardsiASPA
    MIMi271900 phenotype
    608034 gene
    neXtProtiNX_P45381
    OpenTargetsiENSG00000108381
    Orphaneti314918 Mild Canavan disease
    314911 Severe Canavan disease
    PharmGKBiPA25055

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiENOG410IERR Eukaryota
    COG2988 LUCA
    GeneTreeiENSGT00390000001189
    HOGENOMiHOG000232489
    InParanoidiP45381
    KOiK01437
    OMAiTHGNEIN
    OrthoDBi1074294at2759
    PhylomeDBiP45381
    TreeFamiTF328708

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03094-MONOMER
    BRENDAi3.5.1.15 2681
    ReactomeiR-HSA-8963693 Aspartate and asparagine metabolism

    Miscellaneous databases

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...
    ChiTaRSi
    ASPA human
    EvolutionaryTraceiP45381

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...
    GenomeRNAii
    443
    PharosiP45381

    Protein Ontology

    More...
    PROi
    PR:P45381

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000108381 Expressed in 185 organ(s), highest expression level in corpus callosum
    ExpressionAtlasiP45381 baseline and differential
    GenevisibleiP45381 HS

    Family and domain databases

    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

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiACY2_HUMAN
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P45381
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 16, 2019
    This is version 179 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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. SIMILARITY comments
      Index of protein domains and families
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    UniProt is an ELIXIR core data resource
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