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Entry version 186 (11 Dec 2019)
Sequence version 1 (01 Nov 1991)
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Protein

Serine/threonine-protein phosphatase PP2A-1 catalytic subunit

Gene

PPH21

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

Exact function not known, phosphatase 2A performs an essential cellular function.

Miscellaneous

Present with 5620 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

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi117Manganese 1By similarity1
Metal bindingi119Manganese 1By similarity1
Metal bindingi145Manganese 1By similarity1
Metal bindingi145Manganese 2By similarity1
Metal bindingi177Manganese 2By similarity1
<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 sitei178Proton donorBy similarity1
Metal bindingi227Manganese 2By similarity1
Metal bindingi301Manganese 2By similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • protein serine/threonine phosphatase 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 functionHydrolase, Protein phosphatase
LigandManganese, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-29532-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-198753 ERK/MAPK targets
R-SCE-202670 ERKs are inactivated
R-SCE-389513 CTLA4 inhibitory signaling
R-SCE-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-SCE-69273 Cyclin A/B1/B2 associated events during G2/M transition
R-SCE-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

<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:
Serine/threonine-protein phosphatase PP2A-1 catalytic subunit (EC:3.1.3.16)
<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:PPH21
Ordered Locus Names:YDL134C
ORF Names:D2180
<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 IV

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YDL134C

Saccharomyces Genome Database

More...
SGDi
S000002292 PPH21

<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

<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 → A: Reduced interaction with TAP42. 1 Publication1
Mutagenesisi102E → A: Reduced interaction with TAP42. 1 Publication1
Mutagenesisi103E → A: Reduced interaction with TAP42. 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000588731 – 369Serine/threonine-protein phosphatase PP2A-1 catalytic subunitAdd BLAST369

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 residuei369Leucine methyl ester1 Publication1

<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

Reversibly methyl esterified on Leu-369 by leucine carboxyl methyltransferase 1 (PPM1) and protein phosphatase methylesterase 1 (PPE1). Carboxyl methylation influences the affinity of the catalytic subunit for the different regulatory subunits, thereby modulating the PP2A holoenzyme's substrate specificity, enzyme activity and cellular localization.2 Publications

Keywords - PTMi

Methylation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P23594

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

More...
PaxDbi
P23594

PRoteomics IDEntifications database

More...
PRIDEi
P23594

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P23594

<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

Inactivated in a complex with phosphatase methylesterase PPE1 (PP2Ai).

Interacts with phosphatase 2A activator RRD2, which can reactivate PP2Ai by dissociating the catalytic subunit from the complex.

Forms a ternary complex with RRD2-TAP42.

3 Publications

<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

Show more details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
31927, 229 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1380 TAP42-RRD2-PPH21 phosphatase complex
CPX-1856 Serine/threonine-protein phosphatase PP2A variant 1
CPX-1857 Serine/threonine-protein phosphatase PP2A variant 2

Database of interacting proteins

More...
DIPi
DIP-2282N

Protein interaction database and analysis system

More...
IntActi
P23594, 27 interactors

Molecular INTeraction database

More...
MINTi
P23594

STRING: functional protein association networks

More...
STRINGi
4932.YDL134C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P23594 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
P23594

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-2A subfamily.Curated

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000172696

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P23594

KEGG Orthology (KO)

More...
KOi
K04382

Identification of Orthologs from Complete Genome Data

More...
OMAi
DHINYAF

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.60.21.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004843 Calcineurin-like_PHP_ApaH
IPR029052 Metallo-depent_PP-like
IPR006186 Ser/Thr-sp_prot-phosphatase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00149 Metallophos, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00114 STPHPHTASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00156 PP2Ac, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00125 SER_THR_PHOSPHATASE, 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.

P23594-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDTDLDVPMQ DAVTEQLTPT VSEDMDLNNN SSDNNAEEFS VDDLKPGSSG
60 70 80 90 100
IADHKSSKPL ELNNTNINQL DQWIEHLSKC EPLSEDDVAR LCKMAVDVLQ
110 120 130 140 150
FEENVKPINV PVTICGDVHG QFHDLLELFK IGGPCPDTNY LFMGDYVDRG
160 170 180 190 200
YYSVETVSYL VAMKVRYPHR ITILRGNHES RQITQVYGFY DECLRKYGSA
210 220 230 240 250
NVWKMFTDLF DYFPITALVD NKIFCLHGGL SPMIETIDQV RELNRIQEVP
260 270 280 290 300
HEGPMCDLLW SDPDDRGGWG ISPRGAGFTF GQDVSEQFNH TNDLSLIARA
310 320 330 340 350
HQLVMEGYAW SHQQNVVTIF SAPNYCYRCG NQAAIMEVDE NHNRQFLQYD
360
PSVRPGEPSV SRKTPDYFL
Length:369
Mass (Da):41,938
Last modified:November 1, 1991 - 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:iD8D5757283C9BBD6
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
X56261 Genomic DNA Translation: CAA39702.1
X58856 Genomic DNA Translation: CAA41656.1
X96876 Genomic DNA Translation: CAA65625.1
Z74182 Genomic DNA Translation: CAA98707.1
BK006938 Genomic DNA Translation: DAA11724.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A41525 PABY21

NCBI Reference Sequences

More...
RefSeqi
NP_010147.1, NM_001180193.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YDL134C_mRNA; YDL134C; YDL134C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
851421

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YDL134C

<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
X56261 Genomic DNA Translation: CAA39702.1
X58856 Genomic DNA Translation: CAA41656.1
X96876 Genomic DNA Translation: CAA65625.1
Z74182 Genomic DNA Translation: CAA98707.1
BK006938 Genomic DNA Translation: DAA11724.1
PIRiA41525 PABY21
RefSeqiNP_010147.1, NM_001180193.1

3D structure databases

SMRiP23594
ModBaseiSearch...

Protein-protein interaction databases

BioGridi31927, 229 interactors
ComplexPortaliCPX-1380 TAP42-RRD2-PPH21 phosphatase complex
CPX-1856 Serine/threonine-protein phosphatase PP2A variant 1
CPX-1857 Serine/threonine-protein phosphatase PP2A variant 2
DIPiDIP-2282N
IntActiP23594, 27 interactors
MINTiP23594
STRINGi4932.YDL134C

PTM databases

iPTMnetiP23594

Proteomic databases

MaxQBiP23594
PaxDbiP23594
PRIDEiP23594

Genome annotation databases

EnsemblFungiiYDL134C_mRNA; YDL134C; YDL134C
GeneIDi851421
KEGGisce:YDL134C

Organism-specific databases

EuPathDBiFungiDB:YDL134C
SGDiS000002292 PPH21

Phylogenomic databases

HOGENOMiHOG000172696
InParanoidiP23594
KOiK04382
OMAiDHINYAF

Enzyme and pathway databases

BioCyciYEAST:G3O-29532-MONOMER
ReactomeiR-SCE-198753 ERK/MAPK targets
R-SCE-202670 ERKs are inactivated
R-SCE-389513 CTLA4 inhibitory signaling
R-SCE-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-SCE-69273 Cyclin A/B1/B2 associated events during G2/M transition
R-SCE-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P23594
RNActiP23594 protein

Family and domain databases

Gene3Di3.60.21.10, 1 hit
InterProiView protein in InterPro
IPR004843 Calcineurin-like_PHP_ApaH
IPR029052 Metallo-depent_PP-like
IPR006186 Ser/Thr-sp_prot-phosphatase
PfamiView protein in Pfam
PF00149 Metallophos, 1 hit
PRINTSiPR00114 STPHPHTASE
SMARTiView protein in SMART
SM00156 PP2Ac, 1 hit
PROSITEiView protein in PROSITE
PS00125 SER_THR_PHOSPHATASE, 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 nameiPP2A1_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: P23594
Secondary accession number(s): D6VRL4
<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, 1991
Last sequence update: November 1, 1991
Last modified: December 11, 2019
This is version 186 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

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