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 205 (29 Sep 2021)
Sequence version 1 (01 Oct 1993)
Previous versions | rss
Add a publicationFeedback
Protein

Histone deacetylase RPD3

Gene

RPD3

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

Catalytic component of the RPD3 histone deacetylase (HDAC) complexes RPD3C(L) and RPD3C(S) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation plays an important role in transcriptional regulation, cell cycle progression, DNA damage response, osmotic stress response and developmental events. Is involved in rDNA and telomere silencing and in double strand breaks repair. Required for both full transcription repression and activation of many genes including cell type-specific genes (STE6, TY2 and HO), cell differentiation-specific genes (SPO13), genes that respond to external signals (PHO5) and TRK2. The RPD3 complexes regulate also chromosomal replication timing.

19 Publications

Miscellaneous

Present with 3850 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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei151Curated1

<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

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 functionChromatin regulator, Hydrolase, Repressor
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.5.1.98, 984

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-3214815, HDACs deacetylate histones
R-SCE-4551638, SUMOylation of chromatin organization proteins
R-SCE-9018519, Estrogen-dependent gene expression

<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:
Histone deacetylase RPD3 (EC:3.5.1.98)
Alternative name(s):
Transcriptional regulatory protein RPD3
<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:RPD3
Synonyms:MOF6, REC3, SDI2, SDS6
Ordered Locus Names:YNL330C
ORF Names:N0305
<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 XIV

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000005274, RPD3

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YNL330C

<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

Keywords - Cellular componenti

Cytoplasm, Nucleus

<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>Mutagenesisi150H → A: Impairs histone deacetylase activity and transcription repression. 1 Publication1
Mutagenesisi151H → A: Impairs histone deacetylase activity and transcription repression. 1 Publication1
Mutagenesisi188H → A: Impairs histone deacetylase activity and transcription repression. 1 Publication1
Mutagenesisi322W → A: Reduces strongly HDAC activity. 1 Publication1
Mutagenesisi325E → A: Reduces strongly HDAC activity. 1 Publication1
Mutagenesisi327G → A: Reduces strongly HDAC activity. 1 Publication1
Mutagenesisi328L → A: Reduces strongly HDAC activity. 1 Publication1
Mutagenesisi329L → A: Reduces strongly HDAC activity. 1 Publication1
Mutagenesisi332V → A: Reduces strongly HDAC activity. 1 Publication1
Mutagenesisi334L → A: Reduces strongly HDAC activity. 1 Publication1
Mutagenesisi335D → A: Reduces strongly HDAC activity. 1 Publication1
Mutagenesisi338L → A: Reduces strongly HDAC activity. 1 Publication1
Mutagenesisi339P → A: Reduces strongly HDAC activity. 1 Publication1

<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_00001147241 – 433Histone deacetylase RPD3Add BLAST433

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 residuei394PhosphothreonineCombined sources1
Modified residuei408PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P32561

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

More...
PaxDbi
P32561

PRoteomics IDEntifications database

More...
PRIDEi
P32561

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P32561

<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

Component of the RPD3C(L) complex composed of at least ASH1, CTI6, DEP1, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, UME1 and UME6.

Component of the RPD3C(S) complex composed of at least EAF3, RCO1, RPD3, SIN3, and UME1.

Interacts with cyclophilins CPR1, CPR6 and CPR7, with the kinase HOG1, and with ESS1, CYC8 and HAC1.

10 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
35511, 1038 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1372, SNT2C histone deacetylase complex
CPX-1851, RPD3S histone deacetylase complex
CPX-1852, RPD3L histone deacetylase complex

Database of interacting proteins

More...
DIPi
DIP-681N

Protein interaction database and analysis system

More...
IntActi
P32561, 78 interactors

Molecular INTeraction database

More...
MINTi
P32561

STRING: functional protein association networks

More...
STRINGi
4932.YNL330C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P32561, 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
P32561

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>Regioni19 – 331Histone deacetylaseAdd BLAST313
Regioni388 – 433DisorderedSequence analysisAdd BLAST46

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi320 – 340ESA1-RPD3 motifAdd BLAST21

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi408 – 433Basic and acidic residuesSequence analysisAdd BLAST26

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The ESA1-RPD3 (ER) motif is common to ESA1 and RPD3 and is required for ESA1 histone acetyl-transferase (HAT) activity and RPD3 histone deacetylase (HDAC) activity.1 Publication

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1342, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000165542

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_007727_7_4_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P32561

Identification of Orthologs from Complete Genome Data

More...
OMAi
MVYEAKP

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.800.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000286, His_deacetylse
IPR003084, His_deacetylse_1
IPR023801, His_deacetylse_dom
IPR037138, His_deacetylse_dom_sf
IPR023696, Ureohydrolase_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00850, Hist_deacetyl, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF037913, His_deacetylse_1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01270, HDASUPER
PR01271, HISDACETLASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52768, SSF52768, 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.

P32561-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVYEATPFDP ITVKPSDKRR VAYFYDADVG NYAYGAGHPM KPHRIRMAHS
60 70 80 90 100
LIMNYGLYKK MEIYRAKPAT KQEMCQFHTD EYIDFLSRVT PDNLEMFKRE
110 120 130 140 150
SVKFNVGDDC PVFDGLYEYC SISGGGSMEG AARLNRGKCD VAVNYAGGLH
160 170 180 190 200
HAKKSEASGF CYLNDIVLGI IELLRYHPRV LYIDIDVHHG DGVEEAFYTT
210 220 230 240 250
DRVMTCSFHK YGEFFPGTGE LRDIGVGAGK NYAVNVPLRD GIDDATYRSV
260 270 280 290 300
FEPVIKKIME WYQPSAVVLQ CGGDSLSGDR LGCFNLSMEG HANCVNYVKS
310 320 330 340 350
FGIPMMVVGG GGYTMRNVAR TWCFETGLLN NVVLDKDLPY NEYYEYYGPD
360 370 380 390 400
YKLSVRPSNM FNVNTPEYLD KVMTNIFANL ENTKYAPSVQ LNHTPRDAED
410 420 430
LGDVEEDSAE AKDTKGGSQY ARDLHVEHDN EFY
Length:433
Mass (Da):48,904
Last modified:October 1, 1993 - 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:i34FFD72A7E7425DB
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
S66438 Genomic DNA Translation: AAB20328.1
X83226 Genomic DNA Translation: CAA58228.1
Z46259 Genomic DNA Translation: CAA86368.1
Z71605 Genomic DNA Translation: CAA96262.1
Z71606 Genomic DNA Translation: CAA96263.1
AY692813 Genomic DNA Translation: AAT92832.1
BK006947 Genomic DNA Translation: DAA10233.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S22284

NCBI Reference Sequences

More...
RefSeqi
NP_014069.1, NM_001183168.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YNL330C_mRNA; YNL330C; YNL330C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
855386

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YNL330C

<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
S66438 Genomic DNA Translation: AAB20328.1
X83226 Genomic DNA Translation: CAA58228.1
Z46259 Genomic DNA Translation: CAA86368.1
Z71605 Genomic DNA Translation: CAA96262.1
Z71606 Genomic DNA Translation: CAA96263.1
AY692813 Genomic DNA Translation: AAT92832.1
BK006947 Genomic DNA Translation: DAA10233.1
PIRiS22284
RefSeqiNP_014069.1, NM_001183168.1

3D structure databases

SMRiP32561
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi35511, 1038 interactors
ComplexPortaliCPX-1372, SNT2C histone deacetylase complex
CPX-1851, RPD3S histone deacetylase complex
CPX-1852, RPD3L histone deacetylase complex
DIPiDIP-681N
IntActiP32561, 78 interactors
MINTiP32561
STRINGi4932.YNL330C

PTM databases

iPTMnetiP32561

Proteomic databases

MaxQBiP32561
PaxDbiP32561
PRIDEiP32561

Genome annotation databases

EnsemblFungiiYNL330C_mRNA; YNL330C; YNL330C
GeneIDi855386
KEGGisce:YNL330C

Organism-specific databases

SGDiS000005274, RPD3
VEuPathDBiFungiDB:YNL330C

Phylogenomic databases

eggNOGiKOG1342, Eukaryota
GeneTreeiENSGT00940000165542
HOGENOMiCLU_007727_7_4_1
InParanoidiP32561
OMAiMVYEAKP

Enzyme and pathway databases

BRENDAi3.5.1.98, 984
ReactomeiR-SCE-3214815, HDACs deacetylate histones
R-SCE-4551638, SUMOylation of chromatin organization proteins
R-SCE-9018519, Estrogen-dependent gene expression

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P32561
RNActiP32561, protein

Family and domain databases

Gene3Di3.40.800.20, 1 hit
InterProiView protein in InterPro
IPR000286, His_deacetylse
IPR003084, His_deacetylse_1
IPR023801, His_deacetylse_dom
IPR037138, His_deacetylse_dom_sf
IPR023696, Ureohydrolase_dom_sf
PfamiView protein in Pfam
PF00850, Hist_deacetyl, 1 hit
PIRSFiPIRSF037913, His_deacetylse_1, 1 hit
PRINTSiPR01270, HDASUPER
PR01271, HISDACETLASE
SUPFAMiSSF52768, SSF52768, 1 hit

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 nameiRPD3_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: P32561
Secondary accession number(s): D6W0L7
<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, 1993
Last sequence update: October 1, 1993
Last modified: September 29, 2021
This is version 205 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. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families
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