Peroxiredoxin TSA1

<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

<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

• [protein]-dithiol

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  + a hydroperoxide

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  = [protein]-disulfide

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  + an alcohol

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  + H₂O

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  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.7

    "Purification and characterization of a second type thioredoxin peroxidase (type II TPx) from Saccharomyces cerevisiae."
    Jeong J.S., Kwon S.J., Kang S.W., Rhee S.G., Kim K.
    Biochemistry 38:776-783(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  EC:1.11.1.15
  • Search proteins in UniProtKB for this EC number.
  • See the description of this EC number in ENZYME.
  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.7

    "Purification and characterization of a second type thioredoxin peroxidase (type II TPx) from Saccharomyces cerevisiae."
    Jeong J.S., Kwon S.J., Kang S.W., Rhee S.G., Kim K.
    Biochemistry 38:776-783(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  Source: Rhea

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  • See the description of this reaction in Rhea.

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  [protein]-dithiol

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  L-cysteine residue

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  Position: C1

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  L-cysteine residue

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  Position: C2

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  +

  a hydroperoxide

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  zoom

  =

  [protein]-disulfide

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  L-cystine residue

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  +

  an alcohol

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  zoom

  +

  H₂O

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<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsⁱ

Sites

<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

• identical protein binding Source: CAFA <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • Ref.11

    "Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function."
    Jang H.H., Lee K.O., Chi Y.H., Jung B.G., Park S.K., Park J.H., Lee J.R., Lee S.S., Moon J.C., Yun J.W., Choi Y.O., Kim W.Y., Kang J.S., Cheong G.W., Yun D.J., Rhee S.G., Cho M.J., Lee S.Y.
    Cell 117:625-635(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• kinase regulator activity Source: SGDInferred from mutant phenotypeⁱ
  • "Redox-dependent Regulation of Gluconeogenesis by a Novel Mechanism Mediated by a Peroxidatic Cysteine of Peroxiredoxin."
    Irokawa H., Tachibana T., Watanabe T., Matsuyama Y., Motohashi H., Ogasawara A., Iwai K., Naganuma A., Kuge S.
    Sci Rep 6:33536-33536(2016) [PubMed] [Europe PMC] [Abstract]
• peroxiredoxin activity Source: SGD <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Reactions of yeast thioredoxin peroxidases I and II with hydrogen peroxide and peroxynitrite: rate constants by competitive kinetics."
    Ogusucu R., Rettori D., Munhoz D.C., Netto L.E., Augusto O.
    Free Radic. Biol. Med. 42:326-334(2007) [PubMed] [Europe PMC] [Abstract]
• ribosome binding Source: SGDInferred from direct assayⁱ
  • Ref.14

    "The yeast Tsa1 peroxiredoxin is a ribosome-associated antioxidant."
    Trotter E.W., Rand J.D., Vickerstaff J., Grant C.M.
    Biochem. J. 412:73-80(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION.
• thioredoxin peroxidase activity Source: SGDInferred from direct assayⁱ
  • Ref.6

    "Thioredoxin-dependent peroxide reductase from yeast."
    Chae H.Z., Chung S.J., Rhee S.G.
    J. Biol. Chem. 269:27670-27678(1994) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, MUTAGENESIS OF CYS-48 AND CYS-171.
  • "Thermosensitive phenotype of yeast mutant lacking thioredoxin peroxidase."
    Lee S.M., Park J.W.
    Arch. Biochem. Biophys. 359:99-106(1998) [PubMed] [Europe PMC] [Abstract]
• unfolded protein binding Source: SGDInferred from direct assayⁱ
  • Ref.11

    "Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function."
    Jang H.H., Lee K.O., Chi Y.H., Jung B.G., Park S.K., Park J.H., Lee J.R., Lee S.S., Moon J.C., Yun J.W., Choi Y.O., Kim W.Y., Kang J.S., Cheong G.W., Yun D.J., Rhee S.G., Cho M.J., Lee S.Y.
    Cell 117:625-635(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.

GO - Biological processⁱ

• cell redox homeostasis Source: SGDInferred from direct assayⁱ
  • Ref.1

    "Cloning, sequencing, and mutation of thiol-specific antioxidant gene of Saccharomyces cerevisiae."
    Chae H.Z., Kim I.-H., Kim K., Rhee S.G.
    J. Biol. Chem. 268:16815-16821(1993) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE, PARTIAL PROTEIN SEQUENCE OF 2-13; 62-66; 79-87; 90-94; 137-143; 148-153; 155-161 AND 192-196, CLEAVAGE OF INITIATOR METHIONINE, SUBCELLULAR LOCATION.
• cellular response to heat Source: CAFAInferred from mutant phenotypeⁱ
  • Ref.11

    "Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function."
    Jang H.H., Lee K.O., Chi Y.H., Jung B.G., Park S.K., Park J.H., Lee J.R., Lee S.S., Moon J.C., Yun J.W., Choi Y.O., Kim W.Y., Kang J.S., Cheong G.W., Yun D.J., Rhee S.G., Cho M.J., Lee S.Y.
    Cell 117:625-635(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• cellular response to hydroperoxide Source: CAFAInferred from mutant phenotypeⁱ
  • Ref.11

    "Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function."
    Jang H.H., Lee K.O., Chi Y.H., Jung B.G., Park S.K., Park J.H., Lee J.R., Lee S.S., Moon J.C., Yun J.W., Choi Y.O., Kim W.Y., Kang J.S., Cheong G.W., Yun D.J., Rhee S.G., Cho M.J., Lee S.Y.
    Cell 117:625-635(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• cellular response to osmotic stress Source: SGDInferred from direct assayⁱ
  • "Analysis of novel hyperosmotic shock response suggests 'beads in liquid' cytosol structure."
    Alexandrov A.I., Grosfeld E.V., Dergalev A.A., Kushnirov V.V., Chuprov-Netochin R.N., Tyurin-Kuzmin P.A., Kireev I.I., Ter-Avanesyan M.D., Leonov S.V., Agaphonov M.O.
    Biol Open 8:0-0(2019) [PubMed] [Europe PMC] [Abstract]
• cellular response to oxidative stress Source: SGDInferred from direct assayⁱ
  • Ref.1

    "Cloning, sequencing, and mutation of thiol-specific antioxidant gene of Saccharomyces cerevisiae."
    Chae H.Z., Kim I.-H., Kim K., Rhee S.G.
    J. Biol. Chem. 268:16815-16821(1993) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE, PARTIAL PROTEIN SEQUENCE OF 2-13; 62-66; 79-87; 90-94; 137-143; 148-153; 155-161 AND 192-196, CLEAVAGE OF INITIATOR METHIONINE, SUBCELLULAR LOCATION.
• chaperone-mediated protein folding Source: CAFAInferred from mutant phenotypeⁱ
  • Ref.11

    "Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function."
    Jang H.H., Lee K.O., Chi Y.H., Jung B.G., Park S.K., Park J.H., Lee J.R., Lee S.S., Moon J.C., Yun J.W., Choi Y.O., Kim W.Y., Kang J.S., Cheong G.W., Yun D.J., Rhee S.G., Cho M.J., Lee S.Y.
    Cell 117:625-635(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• DNA damage checkpoint Source: SGD <p>Inferred from Genetic Interaction</p> <p>Used to describe "traditional" genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "Loss of yeast peroxiredoxin Tsa1p induces genome instability through activation of the DNA damage checkpoint and elevation of dNTP levels."
    Tang H.M., Siu K.L., Wong C.M., Jin D.Y.
    PLoS Genet. 5:e1000697-e1000697(2009) [PubMed] [Europe PMC] [Abstract]
• DNA protection Source: SGDInferred from mutant phenotypeⁱ
  • "Peroxiredoxin Tsa1 is the key peroxidase suppressing genome instability and protecting against cell death in Saccharomyces cerevisiae."
    Iraqui I., Kienda G., Soeur J., Faye G., Baldacci G., Kolodner R.D., Huang M.E.
    PLoS Genet. 5:e1000524-e1000524(2009) [PubMed] [Europe PMC] [Abstract]
• negative regulation of cell aging Source: SGDInferred from mutant phenotypeⁱ
  • "Lifespan Control by Redox-Dependent Recruitment of Chaperones to Misfolded Proteins."
    Hanzen S., Vielfort K., Yang J., Roger F., Andersson V., Zamarbide-Fores S., Andersson R., Malm L., Palais G., Biteau B., Liu B., Toledano M.B., Molin M., Nystrom T.
    Cell 166:140-151(2016) [PubMed] [Europe PMC] [Abstract]
• negative regulation of cell death Source: CAFAInferred from mutant phenotypeⁱ
  • Ref.11

    "Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function."
    Jang H.H., Lee K.O., Chi Y.H., Jung B.G., Park S.K., Park J.H., Lee J.R., Lee S.S., Moon J.C., Yun J.W., Choi Y.O., Kim W.Y., Kang J.S., Cheong G.W., Yun D.J., Rhee S.G., Cho M.J., Lee S.Y.
    Cell 117:625-635(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• negative regulation of hydrogen peroxide-induced cell death Source: CAFAInferred from mutant phenotypeⁱ
  • Ref.11

    "Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function."
    Jang H.H., Lee K.O., Chi Y.H., Jung B.G., Park S.K., Park J.H., Lee J.R., Lee S.S., Moon J.C., Yun J.W., Choi Y.O., Kim W.Y., Kang J.S., Cheong G.W., Yun D.J., Rhee S.G., Cho M.J., Lee S.Y.
    Cell 117:625-635(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• protein folding Source: SGDInferred from direct assayⁱ
  • Ref.11

    "Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function."
    Jang H.H., Lee K.O., Chi Y.H., Jung B.G., Park S.K., Park J.H., Lee J.R., Lee S.S., Moon J.C., Yun J.W., Choi Y.O., Kim W.Y., Kang J.S., Cheong G.W., Yun D.J., Rhee S.G., Cho M.J., Lee S.Y.
    Cell 117:625-635(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• protein polymerization Source: CAFAInferred from mutant phenotypeⁱ
  • Ref.11

    "Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function."
    Jang H.H., Lee K.O., Chi Y.H., Jung B.G., Park S.K., Park J.H., Lee J.R., Lee S.S., Moon J.C., Yun J.W., Choi Y.O., Kim W.Y., Kang J.S., Cheong G.W., Yun D.J., Rhee S.G., Cho M.J., Lee S.Y.
    Cell 117:625-635(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• protein stabilization Source: CAFAInferred from mutant phenotypeⁱ
  • Ref.11

    "Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function."
    Jang H.H., Lee K.O., Chi Y.H., Jung B.G., Park S.K., Park J.H., Lee J.R., Lee S.S., Moon J.C., Yun J.W., Choi Y.O., Kim W.Y., Kang J.S., Cheong G.W., Yun D.J., Rhee S.G., Cho M.J., Lee S.Y.
    Cell 117:625-635(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• regulation of gluconeogenesis Source: SGDInferred from mutant phenotypeⁱ
  • "Redox-dependent Regulation of Gluconeogenesis by a Novel Mechanism Mediated by a Peroxidatic Cysteine of Peroxiredoxin."
    Irokawa H., Tachibana T., Watanabe T., Matsuyama Y., Motohashi H., Ogasawara A., Iwai K., Naganuma A., Kuge S.
    Sci Rep 6:33536-33536(2016) [PubMed] [Europe PMC] [Abstract]
• replicative cell aging Source: SGDInferred from mutant phenotypeⁱ
  • "A new dominant peroxiredoxin allele identified by whole-genome re-sequencing of random mutagenized yeast causes oxidant-resistance and premature aging."
    Timmermann B., Jarolim S., Russmayer H., Kerick M., Michel S., Kruger A., Bluemlein K., Laun P., Grillari J., Lehrach H., Breitenbach M., Ralser M.
    Aging (Albany NY) 2:475-486(2010) [PubMed] [Europe PMC] [Abstract]
• response to hydroperoxide Source: SGDInferred from mutant phenotypeⁱ
  • Ref.12

    "Cytosolic thioredoxin peroxidase I and II are important defenses of yeast against organic hydroperoxide insult: catalases and peroxiredoxins cooperate in the decomposition of H2O2 by yeast."
    Munhoz D.C., Netto L.E.
    J. Biol. Chem. 279:35219-35227(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
• response to oxidative stress Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]

<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

Enzyme and pathway databases

Protein family/group databases

<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

Organism-specific databases

<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

<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

<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

Amino acid modifications

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

Keywords - PTMⁱ

Proteomic databases

2D gel databases

PTM databases

<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

GO - Molecular functionⁱ

• identical protein binding Source: CAFAInferred from mutant phenotypeⁱ
  • Ref.11

    "Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function."
    Jang H.H., Lee K.O., Chi Y.H., Jung B.G., Park S.K., Park J.H., Lee J.R., Lee S.S., Moon J.C., Yun J.W., Choi Y.O., Kim W.Y., Kang J.S., Cheong G.W., Yun D.J., Rhee S.G., Cho M.J., Lee S.Y.
    Cell 117:625-635(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• unfolded protein binding Source: SGDInferred from direct assayⁱ
  • Ref.11

    "Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function."
    Jang H.H., Lee K.O., Chi Y.H., Jung B.G., Park S.K., Park J.H., Lee J.R., Lee S.S., Moon J.C., Yun J.W., Choi Y.O., Kim W.Y., Kang J.S., Cheong G.W., Yun D.J., Rhee S.G., Cho M.J., Lee S.Y.
    Cell 117:625-635(2004) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.

Protein-protein interaction databases

Miscellaneous databases

<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

3D structure databases

<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

Domains and Repeats

Region

<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

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<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.

<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 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.

        10         20         30         40         50
MVAQVQKQAP TFKKTAVVDG VFDEVSLDKY KGKYVVLAFI PLAFTFVCPT 
        60         70         80         90        100
EIIAFSEAAK KFEEQGAQVL FASTDSEYSL LAWTNIPRKE GGLGPINIPL 
       110        120        130        140        150
LADTNHSLSR DYGVLIEEEG VALRGLFIID PKGVIRHITI NDLPVGRNVD 
       160        170        180        190 
EALRLVEAFQ WTDKNGTVLP CNWTPGAATI KPTVEDSKEY FEAANK     

Sequence databases

Genome annotation databases

<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

• 100% Identity
• 90% Identity
• 50% Identity

<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

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

2D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<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 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

Documents

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