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APE2 metallo-aminopeptidase [ Saccharomyces cerevisiae S288C ]

Gene ID: 853699, updated on 18-Sep-2024

Summary

Official Symbol
APE2
Official Full Name
metallo-aminopeptidase
Primary source
SGD:S000001640
Locus tag
YKL157W
See related
AllianceGenome:SGD:S000001640; FungiDB:YKL157W; VEuPathDB:YKL157W
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as
LAP1; YKL158W
Summary
Enables metalloaminopeptidase activity. Involved in peptide catabolic process. Located in cell wall-bounded periplasmic space and extracellular region. Human ortholog(s) of this gene implicated in cervix carcinoma. Orthologous to several human genes including NPEPPS (aminopeptidase puromycin sensitive). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

See APE2 in Genome Data Viewer
Location:
chromosome: XI
Exon count:
2
Sequence:
Chromosome: XI; NC_001143.9 (154991..158232)

Chromosome XI - NC_001143.9Genomic Context describing neighboring genes Neighboring gene Elf1p Neighboring gene Rcn1p Neighboring gene ribosomal 40S subunit protein S27A Neighboring gene tRNA methyltransferase RSM22

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Gene Ontology Provided by SGD

Function Evidence Code Pubs
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 metalloaminopeptidase activity IDA
Inferred from Direct Assay
more info
PubMed 
enables metallopeptidase activity IEA
Inferred from Electronic Annotation
more info
 
enables peptide binding IBA
Inferred from Biological aspect of Ancestor
more info
 
enables zinc ion binding IBA
Inferred from Biological aspect of Ancestor
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 peptide catabolic process IBA
Inferred from Biological aspect of Ancestor
more info
 
involved_in peptide catabolic process IDA
Inferred from Direct Assay
more info
PubMed 
involved_in peptide catabolic process IMP
Inferred from Mutant Phenotype
more info
PubMed 
involved_in proteolysis IBA
Inferred from Biological aspect of Ancestor
more info
 
involved_in proteolysis IEA
Inferred from Electronic Annotation
more info
 
Component Evidence Code Pubs
located_in cell wall-bounded periplasmic space IDA
Inferred from Direct Assay
more info
PubMed 
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
 
located_in extracellular region IDA
Inferred from Direct Assay
more info
PubMed 
is_active_in extracellular space IBA
Inferred from Biological aspect of Ancestor
more info
 
is_active_in membrane IBA
Inferred from Biological aspect of Ancestor
more info
 
located_in mitochondrion HDA PubMed 
located_in mitochondrion IEA
Inferred from Electronic Annotation
more info
 
located_in nucleus HDA PubMed 
located_in periplasmic space IEA
Inferred from Electronic Annotation
more info
 

General protein information

Preferred Names
metallo-aminopeptidase
NP_012765.3
  • Aminopeptidase yscII; may have role in obtaining leucine from dipeptide substrates; targeted to vacuole via Vps10p-dependent endosomal vacuolar protein sorting pathway; APE2 has a paralog, AAP1, that arose from the whole genome duplication

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_001143.9 Reference assembly

    Range
    154991..158232
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001179723.2NP_012765.3  TPA: metallo-aminopeptidase [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_012765.3

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6VX41, P32454, P36055
    UniProtKB/TrEMBL
    C8ZC17, N1P147
    Conserved Domains (1) summary
    COG0308
    Location:90941
    PepN; Aminopeptidase N [Amino acid transport and metabolism]