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 - P32626 (ENOPH_YEAST)

Entry version 160 (07 Apr 2021)
Sequence version 2 (16 Jun 2009)
Previous versions | rss
Add a publicationFeedback
Protein

Enolase-phosphatase E1

Gene

UTR4

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

Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).UniRule annotation

Miscellaneous

Present with 2850 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Mg2+Note: Binds 1 Mg2+ ion per subunit.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-methionine biosynthesis via salvage pathway

This protein is involved in step 3 and 4 of the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate.UniRule annotation
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Methylthioribose-1-phosphate isomerase (MRI1)
  2. Methylthioribulose-1-phosphate dehydratase (MDE1)
  3. Enolase-phosphatase E1 (UTR4)
  4. Enolase-phosphatase E1 (UTR4)
  5. 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase (ADI1)
  6. Aromatic amino acid aminotransferase 2 (ARO9), Branched-chain-amino-acid aminotransferase, cytosolic (BAT2), Aromatic/aminoadipate aminotransferase 1 (ARO8), Branched-chain-amino-acid aminotransferase, mitochondrial (BAT1)
This subpathway is part of the pathway L-methionine biosynthesis via salvage pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate, the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi11MagnesiumUniRule annotation1 Publication1
Metal bindingi13Magnesium; via carbonyl oxygenUniRule annotation1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei161SubstrateUniRule annotation1
Metal bindingi186MagnesiumUniRule annotation1 Publication1

<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 functionHydrolase
Biological processAmino-acid biosynthesis, Methionine biosynthesis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SCE-1237112, Methionine salvage pathway

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

More...UniPathwayi		UPA00904;UER00876
UPA00904;UER00877

<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%5Fand%5Ftaxonomy%5Fsection">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:
Enolase-phosphatase E1UniRule annotation (EC:3.1.3.77UniRule annotation)
Alternative name(s):
2,3-diketo-5-methylthio-1-phosphopentane phosphataseUniRule annotation
Unknown transcript 4 proteinUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:UTR4UniRule annotation
Ordered Locus Names:YEL038W
ORF Names:SYGP-ORF20
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 V

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000000764, UTR4

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YEL038W

<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 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_00000657461 – 227Enolase-phosphatase E1Add BLAST227

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P32626

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

More...PaxDbi		P32626

PRoteomics IDEntifications database

More...PRIDEi		P32626

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

UniRule annotation

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		36691, 32 interactors

Database of interacting proteins

More...DIPi		DIP-5487N

STRING: functional protein association networks

More...STRINGi		4932.YEL038W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P32626, 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

Secondary structure

1227
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P32626

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P32626

<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>Regioni118 – 119Substrate bindingUniRule annotation2

<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 HAD-like hydrolase superfamily. MasA/MtnC family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2630, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00440000039914

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_023273_1_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P32626

Identification of Orthologs from Complete Genome Data

More...OMAi		HFDTHVG

Family and domain databases

Conserved Domains Database

More...CDDi		cd01629, HAD_EP, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.1000, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_03117, Salvage_MtnC_euk, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR023943, Enolase-ppase_E1
IPR027511, ENOPH1_eukaryotes
IPR036412, HAD-like_sf
IPR023214, HAD_sf

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF56784, SSF56784, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01691, enolase-ppase, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P32626-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGDNYSTYLL DIEGTVCPIS FVKETLFPYF TNKVPQLVQQ DTRDSPVSNI 
        60         70         80         90        100
LSQFHIDNKE QLQAHILELV AKDVKDPILK QLQGYVWAHG YESGQIKAPV 
       110        120        130        140        150
YADAIDFIKR KKRVFIYSSG SVKAQKLLFG YVQDPNAPAH DSLDLNSYID 
       160        170        180        190        200
GYFDINTSGK KTETQSYANI LRDIGAKASE VLFLSDNPLE LDAAAGVGIA 
       210        220 
TGLASRPGNA PVPDGQKYQV YKNFETL
Length:227
Mass (Da):25,187
Last modified:June 16, 2009 - v2
<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:i147305E847F765DB
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA34939 differs from that shown. Reason: Frameshift.Curated
The sequence AAA34939 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence AAB28443 differs from that shown. Reason: Frameshift.Curated
The sequence AAB28443 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence AAB65004 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence AAD13973 differs from that shown. Reason: Frameshift.Curated
The sequence AAD13973 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti56 – 57ID → MH in AAA34939 (PubMed:8411151).Curated2
Sequence conflicti56 – 57ID → MH in AAD13973 (PubMed:8411151).Curated2
Sequence conflicti56 – 57ID → MH in AAB28443 (PubMed:8411151).Curated2
Sequence conflicti179S → T in AAA34939 (PubMed:8411151).Curated1
Sequence conflicti179S → T in AAD13973 (PubMed:8411151).Curated1
Sequence conflicti179S → T in AAB28443 (PubMed:8411151).Curated1

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
L22173 Genomic DNA Translation: AAA34939.1 Sequence problems.
S65964 Genomic DNA Translation: AAD13973.1 Sequence problems.
S66121 mRNA Translation: AAB28443.1 Sequence problems.
U18779 Genomic DNA Translation: AAB65004.1 Different initiation.
BK006939 Genomic DNA Translation: DAA07615.1

Protein sequence database of the Protein Information Resource

More...PIRi		S30843

NCBI Reference Sequences

More...RefSeqi		NP_010876.2, NM_001178853.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YEL038W_mRNA; YEL038W; YEL038W

Database of genes from NCBI RefSeq genomes

More...GeneIDi		856673

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YEL038W

<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
L22173 Genomic DNA Translation: AAA34939.1 Sequence problems.
S65964 Genomic DNA Translation: AAD13973.1 Sequence problems.
S66121 mRNA Translation: AAB28443.1 Sequence problems.
U18779 Genomic DNA Translation: AAB65004.1 Different initiation.
BK006939 Genomic DNA Translation: DAA07615.1
PIRiS30843
RefSeqiNP_010876.2, NM_001178853.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2G80X-ray2.28A/B/C/D1-227[»]
SMRiP32626
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi36691, 32 interactors
DIPiDIP-5487N
STRINGi4932.YEL038W

Proteomic databases

MaxQBiP32626
PaxDbiP32626
PRIDEiP32626

Genome annotation databases

EnsemblFungiiYEL038W_mRNA; YEL038W; YEL038W
GeneIDi856673
KEGGisce:YEL038W

Organism-specific databases

SGDiS000000764, UTR4
VEuPathDBiFungiDB:YEL038W

Phylogenomic databases

eggNOGiKOG2630, Eukaryota
GeneTreeiENSGT00440000039914
HOGENOMiCLU_023273_1_1_1
InParanoidiP32626
OMAiHFDTHVG

Enzyme and pathway databases

UniPathwayiUPA00904;UER00876
UPA00904;UER00877
ReactomeiR-SCE-1237112, Methionine salvage pathway

Miscellaneous databases

EvolutionaryTraceiP32626

Protein Ontology

More...PROi		PR:P32626
RNActiP32626, protein

Family and domain databases

CDDicd01629, HAD_EP, 1 hit
Gene3Di3.40.50.1000, 1 hit
HAMAPiMF_03117, Salvage_MtnC_euk, 1 hit
InterProiView protein in InterPro
IPR023943, Enolase-ppase_E1
IPR027511, ENOPH1_eukaryotes
IPR036412, HAD-like_sf
IPR023214, HAD_sf
SUPFAMiSSF56784, SSF56784, 1 hit
TIGRFAMsiTIGR01691, enolase-ppase, 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 nameiENOPH_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: P32626
Secondary accession number(s): D3DLL1
<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%5Fand%5Fisoforms">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: June 16, 2009
Last modified: April 7, 2021
This is version 160 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

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

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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