Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P53204 (NMA2_YEAST)

Entry version 156 (11 Dec 2019)
Sequence version 1 (01 Oct 1996)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2

Gene

NMA2

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 formation of NAD+ from nicotinamide mononucleotide (NMN) and ATP (PubMed:12597897). Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate to form deamido-NAD+ (NaAD). Key enzyme in both de novo and salvage pathways for NAD+ biosynthesis (By similarity). Predominantly acts in the salvage pathways via NMN (PubMed:11884393).By similarity2 Publications

Miscellaneous

Present with 1430 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 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

Co2+1 PublicationNote: Divalent metal cation.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=1.4 mM for ATP1 Publication
  2. KM=0.13 mM for NMN1 Publication
  3. KM=0.023 mM for NAD+1 Publication
  4. KM=5 mM for diphosphate1 Publication

    pH dependencei

    Optimum pH is 6.5-8.0.1 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: NAD(+) biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes deamido-NAD(+) from nicotinate D-ribonucleotide.1 Publication
    Proteins known to be involved in this subpathway in this organism are:
    1. Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 (NMA1), Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 (NMA2)
    This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes deamido-NAD(+) from nicotinate D-ribonucleotide, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

    Pathwayi: NAD(+) biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes NAD(+) from nicotinamide D-ribonucleotide.1 Publication
    Proteins known to be involved in this subpathway in this organism are:
    1. Nicotinamide mononucleotide adenylyltransferase (POF1), Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 (NMA1), Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 (NMA2)
    This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes NAD(+) from nicotinamide D-ribonucleotide, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei175ATPBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi166 – 168ATPBy similarity3
    Nucleotide bindingi282 – 284ATPBy similarity3
    Nucleotide bindingi350 – 353ATPBy similarity4

    <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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <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 functionNucleotidyltransferase, Transferase
    Biological processPyridine nucleotide biosynthesis
    LigandATP-binding, NAD, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		MetaCyc:YGR010W-MONOMER
    YEAST:YGR010W-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		2.7.7.1 984
    2.7.7.18 984

    Reactome - a knowledgebase of biological pathways and processes

    More...    Reactomei    		R-SCE-196807 Nicotinate metabolism

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

    More...    UniPathwayi    		UPA00253;UER00332
    UPA00253;UER00600

    <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:
    Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2Curated (EC:2.7.7.11 Publication, EC:2.7.7.181 Publication)
    Short name:
    NMN/NaMN adenylyltransferase 2
    Alternative name(s):
    NAD(+) diphosphorylase 2
    NAD(+) pyrophosphorylase 2
    Nicotinamide-nucleotide adenylyltransferase 21 Publication
    Short name:
    NMN adenylyltransferase 2
    Short name:
    NMNAT 2
    Nicotinate-nucleotide adenylyltransferase 21 Publication
    Short name:
    NaMN adenylyltransferase 2
    Short name:
    NaMNAT 2
    <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:NMA21 Publication
    Ordered Locus Names:YGR010WImported
    <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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
    <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:YGR010W

    Saccharomyces Genome Database

    More...    SGDi    		S000003242 NMA2

    <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

    Nucleus

    <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_00001350191 – 395Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2Add BLAST395

    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 residuei85PhosphoserineCombined sources1
    Modified residuei89PhosphoserineCombined sources1
    Modified residuei90PhosphoserineCombined sources1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...    MaxQBi    		P53204

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

    More...    PaxDbi    		P53204

    PRoteomics IDEntifications database

    More...    PRIDEi    		P53204

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		P53204

    <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

    Expression is slightly induced in late log phase.1 Publication

    <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%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q061786EBI-23073,EBI-11803

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		33254, 49 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-1227N

    Protein interaction database and analysis system

    More...    IntActi    		P53204, 2 interactors

    Molecular INTeraction database

    More...    MINTi    		P53204

    STRING: functional protein association networks

    More...    STRINGi    		4932.YGR010W

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...    RNActi    		P53204 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    		P53204

    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

    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>Regioni206 – 208Substrate bindingBy similarity3
    Regioni244 – 247Substrate bindingBy similarity4
    Regioni294 – 295Substrate bindingBy similarity2

    <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 eukaryotic NMN adenylyltransferase family.Curated

    Phylogenomic databases

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000216047

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P53204

    KEGG Orthology (KO)

    More...    KOi    		K06210

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		PAHHRVI

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.40.50.620, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR004821 Cyt_trans-like
    IPR005248 NadD/NMNAT
    IPR014729 Rossmann-like_a/b/a_fold

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF01467 CTP_transf_like, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR00482 TIGR00482, 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>. 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_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.

    P53204-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MDPTKAPDFK PPQPNEELQP PPDPTHTIPK SGPIVPYVLA DYNSSIDAPF 
            60         70         80         90        100
    NLDIYKTLSS RKKNANSSNR MDHIPLNTSD FQPLSRDVSS EEESEGQSNG 
           110        120        130        140        150
    IDATLQDVTM TGNLGVLKSQ IADLEEVPHT IVRQARTIED YEFPVHRLTK 
           160        170        180        190        200
    KLQDPEKLPL IIVACGSFSP ITYLHLRMFE MALDDINEQT RFEVVGGYFS 
           210        220        230        240        250
    PVSDNYQKRG LAPAYHRVRM CELACERTSS WLMVDAWESL QSSYTRTAKV 
           260        270        280        290        300
    LDHFNHEINI KRGGIMTVDG EKMGVKIMLL AGGDLIESMG EPHVWADSDL 
           310        320        330        340        350
    HHILGNYGCL IVERTGSDVR SFLLSHDIMY EHRRNILIIK QLIYNDISST 
           360        370        380        390 
    KVRLFIRRGM SVQYLLPNSV IRYIQEYNLY INQSEPVKQV LDSKE
    Length:395
    Mass (Da):44,909
    Last modified:October 1, 1996 - 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:i4A358AF7885B6568
    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
    		Z72795 Genomic DNA Translation: CAA96993.1
    BK006941 Genomic DNA Translation: DAA08108.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		S64299

    NCBI Reference Sequences

    More...    RefSeqi    		NP_011524.1, NM_001181139.1

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...    EnsemblFungii    		YGR010W_mRNA; YGR010W; YGR010W

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		852893

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		sce:YGR010W

    <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
    		Z72795 Genomic DNA Translation: CAA96993.1
    BK006941 Genomic DNA Translation: DAA08108.1
    PIRiS64299
    RefSeqiNP_011524.1, NM_001181139.1

    3D structure databases

    SMRiP53204
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi33254, 49 interactors
    DIPiDIP-1227N
    IntActiP53204, 2 interactors
    MINTiP53204
    STRINGi4932.YGR010W

    PTM databases

    iPTMnetiP53204

    Proteomic databases

    MaxQBiP53204
    PaxDbiP53204
    PRIDEiP53204

    Genome annotation databases

    EnsemblFungiiYGR010W_mRNA; YGR010W; YGR010W
    GeneIDi852893
    KEGGisce:YGR010W

    Organism-specific databases

    EuPathDBiFungiDB:YGR010W
    SGDiS000003242 NMA2

    Phylogenomic databases

    HOGENOMiHOG000216047
    InParanoidiP53204
    KOiK06210
    OMAiPAHHRVI

    Enzyme and pathway databases

    UniPathwayiUPA00253;UER00332
    UPA00253;UER00600
    BioCyciMetaCyc:YGR010W-MONOMER
    YEAST:YGR010W-MONOMER
    BRENDAi2.7.7.1 984
    2.7.7.18 984
    ReactomeiR-SCE-196807 Nicotinate metabolism

    Miscellaneous databases

    Protein Ontology

    More...    PROi    		PR:P53204
    RNActiP53204 protein

    Family and domain databases

    Gene3Di3.40.50.620, 1 hit
    InterProiView protein in InterPro
    IPR004821 Cyt_trans-like
    IPR005248 NadD/NMNAT
    IPR014729 Rossmann-like_a/b/a_fold
    PfamiView protein in Pfam
    PF01467 CTP_transf_like, 1 hit
    TIGRFAMsiTIGR00482 TIGR00482, 1 hit

    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 nameiNMA2_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: P53204
    Secondary accession number(s): D6VUE7
    <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: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: December 11, 2019
    This is version 156 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

    Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names
    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