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Protein

Glycylpeptide N-tetradecanoyltransferase

Gene

NMT1

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

Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. Substrate specificity requires an N-terminal glycine in the nascent polypeptide substrates. Uncharged amino acids are preferred at position 2 while neutral residues are favored at positions 3 and 4. Ser is present at position 5 in almost all known N-myristoyl proteins and Lys is commonly encountered at postion 6.

Miscellaneous

Has an ordered Bi-Bi kinetic mechanism, with myristoyl-CoA binding taking place prior to peptide binding and CoA release occurring before acylated peptide release. Cooperative interactions between the acyl-CoA and peptide binding sites of NMT contribute to its extraordinary chain-length specificity.

<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 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

Inhibited by diethylpyrocarbonate. Competitively inhibited by S-(2-oxo)pentadecyl-CoA, a non hydrolysable myristoyl-CoA analog, and by SC-58272, a peptidomimetic derived from the N-terminal sequence of a natural substrate.

<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=1.4 µM for myristoyl-CoA2 Publications

    pH dependencei

    Optimum pH is 7.5-8.0.2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 sitei455Proton acceptor; via carboxylate1

    <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

    • glycylpeptide N-tetradecanoyltransferase activity Source: SGD

    GO - Biological processi

    • N-terminal peptidyl-glycine N-myristoylation Source: GO_Central
    • replicative cell aging Source: SGD

    <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 functionAcyltransferase, Transferase

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    YEAST:YLR195C-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.3.1.97 984

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-SCE-2514859 Inactivation, recovery and regulation of the phototransduction cascade

    <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:
    Glycylpeptide N-tetradecanoyltransferase (EC:2.3.1.97)
    Alternative name(s):
    Cell division control protein 72
    Myristoyl-CoA:protein N-myristoyltransferase
    Short name:
    NMT
    Peptide N-myristoyltransferase
    <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:NMT1
    Synonyms:CDC72
    Ordered Locus Names:YLR195C
    ORF Names:L8167.14
    <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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    <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 identifieri559292 [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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    <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
    • UP000002311 <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 XII

    Organism-specific databases

    Saccharomyces Genome Database

    More...
    SGDi
    S000004185 NMT1

    <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; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm

    <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

    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>Mutagenesisi99L → P in NMT1-72; temperature-sensitive mutant with myristic acid auxotrophy. 1 Publication1
    Mutagenesisi169N → L: Reduces the chemical transformation rate; when associated with A-205. 1 Publication1
    Mutagenesisi170F → A: Reduces the chemical transformation rate; when associated with A-171. 1 Publication1
    Mutagenesisi171L → A: Reduces the chemical transformation rate; when associated with A-170. 1 Publication1
    Mutagenesisi202A → T: Reduces affinity for both substrate and myristoyl-CoA. 1 Publication1
    Mutagenesisi205T → A: Reduces the chemical transformation rate; when associated with L-169. 1 Publication1
    Mutagenesisi217C → R: Reduces affinity for substrate, but not for myristoyl-CoA. 1 Publication1
    Mutagenesisi328S → P: Moderately reduces affinity for myristoyl-CoA, but not for substrate. 1 Publication1
    Mutagenesisi404N → Y: Moderately reduces affinity for substrate, but not for myristoyl-CoA. 1 Publication1
    Mutagenesisi426N → I: Reduces affinity for myristoyl-CoA, but not for substrate. 1 Publication1
    Mutagenesisi451G → D in NMT1-181; temperature-sensitive with myristic acid auxotrophy. Reduces affinity for myristoyl-CoA. 1 Publication1
    Mutagenesisi454 – 455Missing : Reduces chemical transformation rate 400-fold. 1 Publication2

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL5484

    <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_00000642481 – 455Glycylpeptide N-tetradecanoyltransferaseAdd BLAST455

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    The N-terminus is blocked.

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P14743

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

    More...
    PaxDbi
    P14743

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P14743

    <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

    Monomer.2 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    31465, 302 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    4932.YLR195C

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P14743

    <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

    1455
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P14743

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

    More...
    SMRi
    P14743

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P14743

    <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>Regioni38 – 41Myristoyl CoA-binding4
    Regioni168 – 204Myristoyl CoA-bindingAdd BLAST37

    <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 NMT family.Curated

    Phylogenomic databases

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00390000017837

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000189123

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P14743

    KEGG Orthology (KO)

    More...
    KOi
    K00671

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    YNWRCPS

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG092C3LZ4

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR016181 Acyl_CoA_acyltransferase
    IPR000903 MyristoylCoA_TrFase
    IPR022677 MyristoylCoA_TrFase_C
    IPR022678 MyristoylCoA_TrFase_CS
    IPR022676 MyristoylCoA_TrFase_N

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR11377 PTHR11377, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01233 NMT, 1 hit
    PF02799 NMT_C, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF015892 N-myristl_transf, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF55729 SSF55729, 2 hits

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00975 NMT_1, 1 hit
    PS00976 NMT_2, 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>.<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_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.

    P14743-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSEEDKAKKL ENLLKLLQLN NDDTSKFTQE QKKAMKDHKF WRTQPVKDFD
    60 70 80 90 100
    EKVVEEGPID KPKTPEDISD KPLPLLSSFE WCSIDVDNKK QLEDVFVLLN
    110 120 130 140 150
    ENYVEDRDAG FRFNYTKEFF NWALKSPGWK KDWHIGVRVK ETQKLVAFIS
    160 170 180 190 200
    AIPVTLGVRG KQVPSVEINF LCVHKQLRSK RLTPVLIKEI TRRVNKCDIW
    210 220 230 240 250
    HALYTAGIVL PAPVSTCRYT HRPLNWKKLY EVDFTGLPDG HTEEDMIAEN
    260 270 280 290 300
    ALPAKTKTAG LRKLKKEDID QVFELFKRYQ SRFELIQIFT KEEFEHNFIG
    310 320 330 340 350
    EESLPLDKQV IFSYVVEQPD GKITDFFSFY SLPFTILNNT KYKDLGIGYL
    360 370 380 390 400
    YYYATDADFQ FKDRFDPKAT KALKTRLCEL IYDACILAKN ANMDVFNALT
    410 420 430 440 450
    SQDNTLFLDD LKFGPGDGFL NFYLFNYRAK PITGGLNPDN SNDIKRRSNV

    GVVML
    Length:455
    Mass (Da):52,838
    Last modified:April 1, 1990 - 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:i0424CA3978F76AE6
    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
    M23726 Genomic DNA Translation: AAA34815.1
    U14913 Genomic DNA Translation: AAB67436.1
    BK006945 Genomic DNA Translation: DAA09514.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A40163

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_013296.1, NM_001182082.1

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    YLR195C_mRNA; YLR195C_mRNA; YLR195C

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    850892

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sce:YLR195C

    <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
    M23726 Genomic DNA Translation: AAA34815.1
    U14913 Genomic DNA Translation: AAB67436.1
    BK006945 Genomic DNA Translation: DAA09514.1
    PIRiA40163
    RefSeqiNP_013296.1, NM_001182082.1

    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
    1IICX-ray2.20A/B34-455[»]
    1IIDX-ray2.50A34-455[»]
    2NMTX-ray2.90A34-455[»]
    2P6EX-ray2.90A/B/C/D/E/F1-455[»]
    2P6FX-ray3.10A/B/C/D/E/F1-455[»]
    2P6GX-ray3.00A/B/C/D/E/F1-455[»]
    ProteinModelPortaliP14743
    SMRiP14743
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi31465, 302 interactors
    STRINGi4932.YLR195C

    Chemistry databases

    BindingDBiP14743
    ChEMBLiCHEMBL5484

    Proteomic databases

    MaxQBiP14743
    PaxDbiP14743
    PRIDEiP14743

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYLR195C_mRNA; YLR195C_mRNA; YLR195C
    GeneIDi850892
    KEGGisce:YLR195C

    Organism-specific databases

    SGDiS000004185 NMT1

    Phylogenomic databases

    GeneTreeiENSGT00390000017837
    HOGENOMiHOG000189123
    InParanoidiP14743
    KOiK00671
    OMAiYNWRCPS
    OrthoDBiEOG092C3LZ4

    Enzyme and pathway databases

    BioCyciYEAST:YLR195C-MONOMER
    BRENDAi2.3.1.97 984
    ReactomeiR-SCE-2514859 Inactivation, recovery and regulation of the phototransduction cascade

    Miscellaneous databases

    EvolutionaryTraceiP14743

    Protein Ontology

    More...
    PROi
    PR:P14743

    Family and domain databases

    InterProiView protein in InterPro
    IPR016181 Acyl_CoA_acyltransferase
    IPR000903 MyristoylCoA_TrFase
    IPR022677 MyristoylCoA_TrFase_C
    IPR022678 MyristoylCoA_TrFase_CS
    IPR022676 MyristoylCoA_TrFase_N
    PANTHERiPTHR11377 PTHR11377, 1 hit
    PfamiView protein in Pfam
    PF01233 NMT, 1 hit
    PF02799 NMT_C, 1 hit
    PIRSFiPIRSF015892 N-myristl_transf, 1 hit
    SUPFAMiSSF55729 SSF55729, 2 hits
    PROSITEiView protein in PROSITE
    PS00975 NMT_1, 1 hit
    PS00976 NMT_2, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    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 nameiNMT_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: P14743
    Secondary accession number(s): D6VYJ8
    <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: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: December 5, 2018
    This is version 177 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names
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