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UniProtKB - P39522 (ILV3_YEAST)

Entry version 161 (08 May 2019)
Sequence version 2 (01 Nov 1995)
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Protein

Dihydroxy-acid dehydratase, mitochondrial

Gene

ILV3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:4 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

Miscellaneous

Present with 171000 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

[4Fe-4S] clusterCuratedNote: Binds 1 [4Fe-4S] cluster.Curated

<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: L-isoleucine biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase small subunit, mitochondrial (ILV6), Acetolactate synthase catalytic subunit, mitochondrial (ILV2)
  2. Ketol-acid reductoisomerase, mitochondrial (ILV5)
  3. Dihydroxy-acid dehydratase, mitochondrial (ILV3)
  4. Branched-chain-amino-acid aminotransferase, cytosolic (BAT2), Branched-chain-amino-acid aminotransferase, mitochondrial (BAT1)
This subpathway is part of the pathway L-isoleucine biosynthesis, 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-isoleucine from 2-oxobutanoate, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-valine biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes L-valine from pyruvate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase small subunit, mitochondrial (ILV6), Acetolactate synthase catalytic subunit, mitochondrial (ILV2)
  2. Ketol-acid reductoisomerase, mitochondrial (ILV5)
  3. Dihydroxy-acid dehydratase, mitochondrial (ILV3)
  4. Branched-chain-amino-acid aminotransferase, cytosolic (BAT2), Branched-chain-amino-acid aminotransferase, mitochondrial (BAT1)
This subpathway is part of the pathway L-valine biosynthesis, 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-valine from pyruvate, the pathway L-valine biosynthesis and in Amino-acid biosynthesis.

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 bindingi143Iron-sulfur (4Fe-4S)Sequence analysis1
Metal bindingi221Iron-sulfur (4Fe-4S)Sequence analysis1

<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

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • dihydroxy-acid dehydratase activity Source: SGD
  • metal ion binding Source: UniProtKB-KW
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 functionLyase
Biological processAmino-acid biosynthesis, Branched-chain amino acid biosynthesis
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		YEAST:YJR016C-MONOMER

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

More...UniPathwayi		UPA00047;UER00057
UPA00049;UER00061

<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:
Dihydroxy-acid dehydratase, mitochondrial (EC:4.2.1.9)
Short name:
DAD
Alternative name(s):
2,3-dihydroxy acid hydrolyase
<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:ILV3
Ordered Locus Names:YJR016C
ORF Names:J1450
<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 X

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		FungiDB:YJR016C

Saccharomyces Genome Database

More...SGDi		S000003777 ILV3

<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

Mitochondrion

<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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – ?MitochondrionSequence analysis
<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_0000015636? – 585Dihydroxy-acid dehydratase, mitochondrial

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P39522

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

More...PaxDbi		P39522

PRoteomics IDEntifications database

More...PRIDEi		P39522

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P39522

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P39522

<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

Homodimer.

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		33772, 133 interactors

Database of interacting proteins

More...DIPi		DIP-6456N

Protein interaction database and analysis system

More...IntActi		P39522, 33 interactors

Molecular INTeraction database

More...MINTi		P39522

STRING: functional protein association networks

More...STRINGi		4932.YJR016C

<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		P39522

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

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

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

Belongs to the IlvD/Edd family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000173155

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P39522

KEGG Orthology (KO)

More...KOi		K01687

Identification of Orthologs from Complete Genome Data

More...OMAi		IPGHVHL

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.50.30.80, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00012 IlvD, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR042096 Dihydro-acid_dehy_C
IPR004404 DihydroxyA_deHydtase
IPR000581 DiOHA_6PGluconate_deHydtase
IPR020558 DiOHA_6PGluconate_deHydtase_CS
IPR037237 IlvD/EDD_N

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00920 ILVD_EDD, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF143975 SSF143975, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00110 ilvD, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00886 ILVD_EDD_1, 1 hit
PS00887 ILVD_EDD_2, 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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P39522-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGLLTKVATS RQFSTTRCVA KKLNKYSYII TEPKGQGASQ AMLYATGFKK 
        60         70         80         90        100
EDFKKPQVGV GSCWWSGNPC NMHLLDLNNR CSQSIEKAGL KAMQFNTIGV 
       110        120        130        140        150
SDGISMGTKG MRYSLQSREI IADSFETIMM AQHYDANIAI PSCDKNMPGV 
       160        170        180        190        200
MMAMGRHNRP SIMVYGGTIL PGHPTCGSSK ISKNIDIVSA FQSYGEYISK 
       210        220        230        240        250
QFTEEEREDV VEHACPGPGS CGGMYTANTM ASAAEVLGLT IPNSSSFPAV 
       260        270        280        290        300
SKEKLAECDN IGEYIKKTME LGILPRDILT KEAFENAITY VVATGGSTNA 
       310        320        330        340        350
VLHLVAVAHS AGVKLSPDDF QRISDTTPLI GDFKPSGKYV MADLINVGGT 
       360        370        380        390        400
QSVIKYLYEN NMLHGNTMTV TGDTLAERAK KAPSLPEGQE IIKPLSHPIK 
       410        420        430        440        450
ANGHLQILYG SLAPGGAVGK ITGKEGTYFK GRARVFEEEG AFIEALERGE 
       460        470        480        490        500
IKKGEKTVVV IRYEGPRGAP GMPEMLKPSS ALMGYGLGKD VALLTDGRFS 
       510        520        530        540        550
GGSHGFLIGH IVPEAAEGGP IGLVRDGDEI IIDADNNKID LLVSDKEMAQ 
       560        570        580 
RKQSWVAPPP RYTRGTLSKY AKLVSNASNG CVLDA
Length:585
Mass (Da):62,861
Last modified:November 1, 1995 - 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:i35AB3C679BA6E8D0
GO

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 conflicti82 – 89SQSIEKAG → MFSIIEKR in AAA34568 (PubMed:8299945).Curated8
Sequence conflicti238G → S in AAA34568 (PubMed:8299945).Curated1
Sequence conflicti242P → S in AAA34568 (PubMed:8299945).Curated1
Sequence conflicti492A → T in AAA34568 (PubMed:8299945).Curated1
Sequence conflicti520P → R in AAA34568 (PubMed:8299945).Curated1
Sequence conflicti551R → A in AAA34568 (PubMed:8299945).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
X87611 Genomic DNA Translation: CAA60939.1
Z49516 Genomic DNA Translation: CAA89540.1
L13975 Genomic DNA Translation: AAA34568.1 Different termination.
BK006943 Genomic DNA Translation: DAA08808.1

Protein sequence database of the Protein Information Resource

More...PIRi		S55205

NCBI Reference Sequences

More...RefSeqi		NP_012550.1, NM_001181674.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YJR016C_mRNA; YJR016C_mRNA; YJR016C

Database of genes from NCBI RefSeq genomes

More...GeneIDi		853473

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YJR016C

<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
X87611 Genomic DNA Translation: CAA60939.1
Z49516 Genomic DNA Translation: CAA89540.1
L13975 Genomic DNA Translation: AAA34568.1 Different termination.
BK006943 Genomic DNA Translation: DAA08808.1
PIRiS55205
RefSeqiNP_012550.1, NM_001181674.1

3D structure databases

SMRiP39522
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33772, 133 interactors
DIPiDIP-6456N
IntActiP39522, 33 interactors
MINTiP39522
STRINGi4932.YJR016C

PTM databases

iPTMnetiP39522

Proteomic databases

MaxQBiP39522
PaxDbiP39522
PRIDEiP39522
TopDownProteomicsiP39522

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJR016C_mRNA; YJR016C_mRNA; YJR016C
GeneIDi853473
KEGGisce:YJR016C

Organism-specific databases

EuPathDBiFungiDB:YJR016C
SGDiS000003777 ILV3

Phylogenomic databases

HOGENOMiHOG000173155
InParanoidiP39522
KOiK01687
OMAiIPGHVHL

Enzyme and pathway databases

UniPathwayiUPA00047;UER00057
UPA00049;UER00061
BioCyciYEAST:YJR016C-MONOMER

Miscellaneous databases

Protein Ontology

More...PROi		PR:P39522

Family and domain databases

Gene3Di3.50.30.80, 1 hit
HAMAPiMF_00012 IlvD, 1 hit
InterProiView protein in InterPro
IPR042096 Dihydro-acid_dehy_C
IPR004404 DihydroxyA_deHydtase
IPR000581 DiOHA_6PGluconate_deHydtase
IPR020558 DiOHA_6PGluconate_deHydtase_CS
IPR037237 IlvD/EDD_N
PfamiView protein in Pfam
PF00920 ILVD_EDD, 1 hit
SUPFAMiSSF143975 SSF143975, 1 hit
TIGRFAMsiTIGR00110 ilvD, 1 hit
PROSITEiView protein in PROSITE
PS00886 ILVD_EDD_1, 1 hit
PS00887 ILVD_EDD_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiILV3_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: P39522
Secondary accession number(s): D6VWJ2
<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: February 1, 1995
Last sequence update: November 1, 1995
Last modified: May 8, 2019
This is version 161 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

Complete proteome, Reference proteome

Documents

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