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Entry version 150 (17 Jun 2020)
Sequence version 1 (01 Feb 1995)
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Protein

Aspartyl aminopeptidase 4

Gene

APE4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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

Aspartyl aminopeptidase that contributes to peptide degradation both in the cytosol and the vacuole. Cells may respond to environmental conditions by changing the distributions of the cytosolic enzyme to the vacuole when cells need more active vacuolar degradation.1 Publication

Miscellaneous

Present with 172 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

  • Release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate. EC:3.4.11.21

<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+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The metalloproteases inhibitors EDTA and 1.10-phenanthroline both inhibit the activity, whereas bestatin, an inhibitor of most aminopeptidases, does not affect enzyme activity.1 Publication

<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. KM=64 µM for angiotensin I1 Publication

    pH dependencei

    Optimum pH is 7.5-7.9.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi97Zinc 1By similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei173SubstrateBy similarity1
    Metal bindingi273Zinc 1By similarity1
    Metal bindingi273Zinc 2By similarity1
    Binding sitei308SubstrateBy similarity1
    Metal bindingi309Zinc 2By similarity1
    Metal bindingi362Zinc 1By similarity1
    Binding sitei362SubstrateBy similarity1
    Binding sitei365SubstrateBy similarity1
    Binding sitei390SubstrateBy similarity1
    Binding sitei397SubstrateBy similarity1
    Metal bindingi456Zinc 2By similarity1

    <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

    • aminopeptidase activity Source: SGD
    • metalloaminopeptidase activity Source: GO_Central
    • zinc ion binding Source: InterPro

    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 functionAminopeptidase, Hydrolase, Metalloprotease, Protease
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    YEAST:G3O-31155-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.4.11.21 984

    Protein family/group databases

    MEROPS protease database

    More...
    MEROPSi
    M18.002

    <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%5Fand%5Ftaxonomy%5Fsection">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:
    Aspartyl aminopeptidase 4 (EC:3.4.11.21)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:APE4
    Ordered Locus Names:YHR113W
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri559292 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
    • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 VIII

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    FungiDB:YHR113W

    Saccharomyces Genome Database

    More...
    SGDi
    S000001155 APE4

    <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 Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm, Vacuole

    <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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001734551 – 490Aspartyl aminopeptidase 4Add BLAST490

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P38821

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

    More...
    PaxDbi
    P38821

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P38821

    Consortium for Top Down Proteomics

    More...
    TopDownProteomicsi
    P38821

    <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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Tetrahedron-shaped homododecamer built from six homodimers.

    1 Publication

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    36546, 62 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-2097N

    Protein interaction database and analysis system

    More...
    IntActi
    P38821, 20 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    4932.YHR113W

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...
    RNActi
    P38821 protein

    <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

    3D structure databases

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

    More...
    SMRi
    P38821

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <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

    <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

    Belongs to the peptidase M18 family.Curated

    Phylogenomic databases

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_019532_2_0_1

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P38821

    KEGG Orthology (KO)

    More...
    KOi
    K01267

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    GHAVHPN

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.30.250.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR001948 Peptidase_M18
    IPR023358 Peptidase_M18_dom2

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR28570 PTHR28570, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02127 Peptidase_M18, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00932 AMINO1PTASE

    <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%5Flength">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>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    P38821-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MFRIQLRTMS SKTCKSDYPK EFVSFLNSSH SPYHTVHNIK KHLVSNGFKE
    60 70 80 90 100
    LSERDSWAGH VAQKGKYFVT RNGSSIIAFA VGGKWEPGNP IAITGAHTDS
    110 120 130 140 150
    PALRIKPISK RVSEKYLQVG VETYGGAIWH SWFDKDLGVA GRVFVKDAKT
    160 170 180 190 200
    GKSIARLVDL NRPLLKIPTL AIHLDRDVNQ KFEFNRETQL LPIGGLQEDK
    210 220 230 240 250
    TEAKTEKEIN NGEFTSIKTI VQRHHAELLG LIAKELAIDT IEDIEDFELI
    260 270 280 290 300
    LYDHNASTLG GFNDEFVFSG RLDNLTSCFT SMHGLTLAAD TEIDRESGIR
    310 320 330 340 350
    LMACFDHEEI GSSSAQGADS NFLPNILERL SILKGDGSDQ TKPLFHSAIL
    360 370 380 390 400
    ETSAKSFFLS SDVAHAVHPN YANKYESQHK PLLGGGPVIK INANQRYMTN
    410 420 430 440 450
    SPGLVLVKRL AEAAKVPLQL FVVANDSPCG STIGPILASK TGIRTLDLGN
    460 470 480 490
    PVLSMHSIRE TGGSADLEFQ IKLFKEFFER YTSIESEIVV
    Length:490
    Mass (Da):54,174
    Last modified:February 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:i511CD6EB85C4EA53
    GO

    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
    U00059 Genomic DNA Translation: AAB68851.1
    BK006934 Genomic DNA Translation: DAA06807.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S48955

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_011981.1, NM_001179243.1

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    YHR113W_mRNA; YHR113W; YHR113W

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    856513

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sce:YHR113W

    <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
    U00059 Genomic DNA Translation: AAB68851.1
    BK006934 Genomic DNA Translation: DAA06807.1
    PIRiS48955
    RefSeqiNP_011981.1, NM_001179243.1

    3D structure databases

    SMRiP38821
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGRIDi36546, 62 interactors
    DIPiDIP-2097N
    IntActiP38821, 20 interactors
    STRINGi4932.YHR113W

    Protein family/group databases

    MEROPSiM18.002

    Proteomic databases

    MaxQBiP38821
    PaxDbiP38821
    PRIDEiP38821
    TopDownProteomicsiP38821

    Genome annotation databases

    EnsemblFungiiYHR113W_mRNA; YHR113W; YHR113W
    GeneIDi856513
    KEGGisce:YHR113W

    Organism-specific databases

    EuPathDBiFungiDB:YHR113W
    SGDiS000001155 APE4

    Phylogenomic databases

    HOGENOMiCLU_019532_2_0_1
    InParanoidiP38821
    KOiK01267
    OMAiGHAVHPN

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31155-MONOMER
    BRENDAi3.4.11.21 984

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P38821
    RNActiP38821 protein

    Family and domain databases

    Gene3Di2.30.250.10, 1 hit
    InterProiView protein in InterPro
    IPR001948 Peptidase_M18
    IPR023358 Peptidase_M18_dom2
    PANTHERiPTHR28570 PTHR28570, 1 hit
    PfamiView protein in Pfam
    PF02127 Peptidase_M18, 1 hit
    PRINTSiPR00932 AMINO1PTASE

    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 nameiDNPEP_YEAST
    <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: P38821
    Secondary accession number(s): D3DL63
    <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: June 17, 2020
    This is version 150 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 programFungal Protein Annotation Program

    <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

    Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome VIII
      Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names
    4. Peptidase families
      Classification of peptidase families and list of entries
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