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    APE4 aspartyl aminopeptidase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 856513, updated on 2-Nov-2024

    Summary

    Official Symbol
    APE4
    Official Full Name
    aspartyl aminopeptidase
    Primary source
    SGD:S000001155
    Locus tag
    YHR113W
    See related
    AllianceGenome:SGD:S000001155; FungiDB:YHR113W; VEuPathDB:YHR113W
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Summary
    Enables aminopeptidase activity. Involved in proteolysis. Located in fungal-type vacuole lumen. Orthologous to human DNPEP (aspartyl aminopeptidase). [provided by Alliance of Genome Resources, Nov 2024]
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    Genomic context

    See APE4 in Genome Data Viewer
    Location:
    chromosome: VIII
    Exon count:
    1
    Sequence:
    Chromosome: VIII; NC_001140.6 (336337..337809)

    Chromosome VIII - NC_001140.6Genomic Context describing neighboring genes Neighboring gene Uba4p Neighboring gene putative cystathionine beta-lyase Neighboring gene Bzz1p Neighboring gene ubiquitin-conjugating protein DMA1

    Interactions

    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables aminopeptidase activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    enables aminopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
     
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
     
    enables metalloaminopeptidase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    enables metallopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
     
    enables zinc ion binding IEA
    Inferred from Electronic Annotation
    more info
     
    enables zinc ion binding RCA
    inferred from Reviewed Computational Analysis
    more info
    PubMed 
    Process Evidence Code Pubs
    involved_in proteolysis IDA
    Inferred from Direct Assay
    more info
    PubMed 
    involved_in proteolysis IEA
    Inferred from Electronic Annotation
    more info
     
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
     
    is_active_in fungal-type vacuole IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    located_in fungal-type vacuole lumen IDA
    Inferred from Direct Assay
    more info
    PubMed 
    located_in vacuolar lumen IEA
    Inferred from Electronic Annotation
    more info
     
    located_in vacuole IEA
    Inferred from Electronic Annotation
    more info
     

    General protein information

    Preferred Names
    aspartyl aminopeptidase
    NP_011981.1
    • Cytoplasmic aspartyl aminopeptidase with possible vacuole function; targeted to vacuole via Vps10p-dependent endosomal vacuolar protein sorting pathway and via CVT pathway; cleaves unblocked N-terminal acidic amino acids from peptide substrates; forms 12-subunit homo-oligomer; M18 metalloprotease family

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_001140.6 Reference assembly

      Range
      336337..337809
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001179243.1NP_011981.1  TPA: aspartyl aminopeptidase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_011981.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D3DL63, P38821
      UniProtKB/TrEMBL
      A6ZT21, B3LSM8, C7GLZ9, C8Z9Q6, G2WFI7, N1P151
      Conserved Domains (1) summary
      cd05658
      Location:20479
      M18_DAP; M18 peptidase aspartyl aminopeptidase