Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 154 (13 Feb 2019)
Sequence version 1 (01 Nov 1988)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Phosphatidylethanolamine N-methyltransferase

Gene

CHO2

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

Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME). Preferentially converts di-C16:1 substrates.UniRule annotation8 Publications

Miscellaneous

Present with 1810 molecules/cell in log phase SD medium.1 Publication

<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 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=60 µM for S-adenosyl-L-methionine1 Publication
  2. KM=110 µM for S-adenosyl-L-methionine1 Publication
  3. KM=57 µM for phosphatidylethanolamine (PE)1 Publication

    pH dependencei

    Optimum pH is 9.9.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: phosphatidylcholine biosynthesis

    This protein is involved in the pathway phosphatidylcholine biosynthesis, which is part of Phospholipid metabolism.UniRule annotation2 Publications
    View all proteins of this organism that are known to be involved in the pathway phosphatidylcholine biosynthesis and in Phospholipid metabolism.

    <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

    • phosphatidylethanolamine N-methyltransferase activity Source: SGD

    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 functionMethyltransferase, Transferase
    Biological processLipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism
    LigandS-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:YGR157W-MONOMER
    YEAST:YGR157W-MONOMER

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00753

    Chemistry databases

    SwissLipids knowledge resource for lipid biology

    More...
    SwissLipidsi
    SLP:000000085

    <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:
    Phosphatidylethanolamine N-methyltransferase1 PublicationUniRule annotation (EC:2.1.1.17UniRule annotation4 Publications)
    Short name:
    PE methyltransferase1 PublicationUniRule annotation
    Short name:
    PEAMTUniRule annotation
    Short name:
    PEMT1 PublicationUniRule annotation
    Alternative name(s):
    Choline-requiring protein 21 Publication
    <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:CHO21 Publication
    Synonyms:PEM11 Publication
    Ordered Locus Names:YGR157WImported
    ORF Names:G6673
    <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 VII

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    FungiDB:YGR157W

    Saccharomyces Genome Database

    More...
    SGDi
    S000003389 CHO2

    <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

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini2 – 55LumenalUniRule annotation1 PublicationAdd BLAST54
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei56 – 76HelicalUniRule annotationAdd BLAST21
    Topological domaini77 – 86CytoplasmicUniRule annotation1 Publication10
    Transmembranei87 – 107HelicalUniRule annotationAdd BLAST21
    Topological domaini108 – 187LumenalUniRule annotation1 PublicationAdd BLAST80
    Transmembranei188 – 208HelicalUniRule annotationAdd BLAST21
    Topological domaini209 – 212CytoplasmicUniRule annotation1 Publication4
    Transmembranei213 – 233HelicalUniRule annotationAdd BLAST21
    Topological domaini234 – 258LumenalUniRule annotation1 PublicationAdd BLAST25
    Transmembranei259 – 279HelicalUniRule annotationAdd BLAST21
    Topological domaini280 – 291CytoplasmicUniRule annotation1 PublicationAdd BLAST12
    Transmembranei292 – 310HelicalUniRule annotationAdd BLAST19
    Topological domaini311 – 362LumenalUniRule annotation1 PublicationAdd BLAST52
    Transmembranei363 – 383HelicalUniRule annotationAdd BLAST21
    Topological domaini384 – 389CytoplasmicUniRule annotation1 Publication6
    Transmembranei390 – 410HelicalUniRule annotationAdd BLAST21
    Topological domaini411 – 439LumenalUniRule annotation1 PublicationAdd BLAST29
    Transmembranei440 – 460HelicalUniRule annotationAdd BLAST21
    Topological domaini461 – 463CytoplasmicUniRule annotation1 Publication3
    Transmembranei464 – 484HelicalUniRule annotationAdd BLAST21
    Topological domaini485 – 534LumenalUniRule annotation1 PublicationAdd BLAST50
    Transmembranei535 – 555HelicalUniRule annotationAdd BLAST21
    Topological domaini556 – 869CytoplasmicUniRule annotation1 PublicationAdd BLAST314

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    <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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
    <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_00000583042 – 869Phosphatidylethanolamine N-methyltransferaseAdd BLAST868

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineCombined sources1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P05374

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

    More...
    PaxDbi
    P05374

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P05374

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P05374

    <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 reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Repressed by myo-inositol and choline.4 Publications

    <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

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    33405, 704 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-8037N

    Protein interaction database and analysis system

    More...
    IntActi
    P05374, 2 interactors

    Molecular INTeraction database

    More...
    MINTi
    P05374

    STRING: functional protein association networks

    More...
    STRINGi
    4932.YGR157W

    <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

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P05374

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

    More...
    SMRi
    P05374

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    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 class VI-like SAM-binding methyltransferase superfamily. CHO2 family.UniRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P05374

    KEGG Orthology (KO)

    More...
    KOi
    K16369

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    WFFCAQF

    Family and domain databases

    HAMAP database of protein families

    More...
    HAMAPi
    MF_03217 PEMT, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR007318 Phopholipid_MeTrfase
    IPR016219 Phosphatid-EA_MeTrfase_fun

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF04191 PEMT, 2 hits

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000383 PEAMT, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51598 SAM_CHO2, 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.

    <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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P05374-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSSCKTTLSE MVGSVTKDRG TINVEARTRS SNVTFKPPVT HDMVRSLFDP
    60 70 80 90 100
    TLKKSLLEKC IALAIISNFF ICYWVFQRFG LQFTKYFFLV QYLFWRIAYN
    110 120 130 140 150
    LGIGLVLHYQ SHYETLTNCA KTHAIFSKIP QNKDANSNFS TNSNSFSEKF
    160 170 180 190 200
    WNFIRKFCQY EIRSKMPKEY DLFAYPEEIN VWLIFRQFVD LILMQDFVTY
    210 220 230 240 250
    IIYVYLSIPY SWVQIFNWRS LLGVILILFN IWVKLDAHRV VKDYAWYWGD
    260 270 280 290 300
    FFFLEESELI FDGVFNISPH PMYSIGYLGY YGLSLICNDY KVLLVSVFGH
    310 320 330 340 350
    YSQFLFLKYV ENPHIERTYG DGTDSDSQMN SRIDDLISKE NYDYSRPLIN
    360 370 380 390 400
    MGLSFNNFNK LRFTDYFTIG TVAALMLGTI MNARFINLNY LFITVFVTKL
    410 420 430 440 450
    VSWLFISTIL YKQSQSKWFT RLFLENGYTQ VYSYEQWQFI YNYYLVLTYT
    460 470 480 490 500
    LMIIHTGLQI WSNFSNINNS QLIFGLILVA LQTWCDKETR LAISDFGWFY
    510 520 530 540 550
    GDFFLSNYIS TRKLTSQGIY RYLNHPEAVL GVVGVWGTVL MTNFAVTNII
    560 570 580 590 600
    LAVLWTLTNF ILVKFIETPH VNKIYGKTKR VSGVGKTLLG LKPLRQVSDI
    610 620 630 640 650
    VNRIENIIIK SLVDESKNSN GGAELLPKNY QDNKEWNILI QEAMDSVATR
    660 670 680 690 700
    LSPYCELKIE NEQVETNFVL PTPVTLNWKM PIELYNGDDW IGLYKVIDTR
    710 720 730 740 750
    ADREKTRVGS GGHWSATSKD SYMNHGLRHK ESVTEIKATE KYVQGKVTFD
    760 770 780 790 800
    TSLLYFENGI YEFRYHSGNS HKVLLISTPF EISLPVLNTT TPELFEKDLT
    810 820 830 840 850
    EFLTKVNVLK DGKFRPLGNK FFGMDSLKQL IKNSIGVELS SEYMRRVNGD
    860
    AHVISHRAWD IKQTLDSLA
    Length:869
    Mass (Da):101,204
    Last modified:November 1, 1988 - 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:iA273F179B4E46A20
    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
    M16987 Genomic DNA Translation: AAA34850.1
    X85807 Genomic DNA Translation: CAA59814.1
    Z72942 Genomic DNA Translation: CAA97171.1
    BK006941 Genomic DNA Translation: DAA08248.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A28443

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_011673.1, NM_001181286.1

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    YGR157W_mRNA; YGR157W_mRNA; YGR157W

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    853061

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sce:YGR157W

    <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
    M16987 Genomic DNA Translation: AAA34850.1
    X85807 Genomic DNA Translation: CAA59814.1
    Z72942 Genomic DNA Translation: CAA97171.1
    BK006941 Genomic DNA Translation: DAA08248.1
    PIRiA28443
    RefSeqiNP_011673.1, NM_001181286.1

    3D structure databases

    ProteinModelPortaliP05374
    SMRiP05374
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi33405, 704 interactors
    DIPiDIP-8037N
    IntActiP05374, 2 interactors
    MINTiP05374
    STRINGi4932.YGR157W

    Chemistry databases

    SwissLipidsiSLP:000000085

    PTM databases

    iPTMnetiP05374

    Proteomic databases

    MaxQBiP05374
    PaxDbiP05374
    PRIDEiP05374

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYGR157W_mRNA; YGR157W_mRNA; YGR157W
    GeneIDi853061
    KEGGisce:YGR157W

    Organism-specific databases

    EuPathDBiFungiDB:YGR157W
    SGDiS000003389 CHO2

    Phylogenomic databases

    InParanoidiP05374
    KOiK16369
    OMAiWFFCAQF

    Enzyme and pathway databases

    UniPathwayi
    UPA00753

    BioCyciMetaCyc:YGR157W-MONOMER
    YEAST:YGR157W-MONOMER

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P05374

    Family and domain databases

    HAMAPiMF_03217 PEMT, 1 hit
    InterProiView protein in InterPro
    IPR007318 Phopholipid_MeTrfase
    IPR016219 Phosphatid-EA_MeTrfase_fun
    PfamiView protein in Pfam
    PF04191 PEMT, 2 hits
    PIRSFiPIRSF000383 PEAMT, 1 hit
    PROSITEiView protein in PROSITE
    PS51598 SAM_CHO2, 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 nameiCHO2_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: P05374
    Secondary accession number(s): D6VUT7
    <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, 1988
    Last sequence update: November 1, 1988
    Last modified: February 13, 2019
    This is version 154 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

    Complete proteome, Reference proteome

    Documents

    1. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    2. Yeast chromosome VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families
    4. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again