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P02309

- H4_YEAST

UniProt

P02309 - H4_YEAST

Protein

Histone H4

Gene

HHF1

more
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Component of the UAF (upstream activation factor) complex which interacts with the upstream element of the RNA polymerase I promoter and forms a stable preinitiation complex. Together with SPT15/TBP UAF seems to stimulate basal transcription to a fully activated level.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi17 – 215

    GO - Molecular functioni

    1. DNA binding Source: SGD
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. chromatin assembly or disassembly Source: SGD
    2. histone H3-K79 methylation Source: SGD
    3. nucleosome assembly Source: InterPro
    4. sexual sporulation resulting in formation of a cellular spore Source: SGD
    5. transfer RNA gene-mediated silencing Source: SGD

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-28996-MONOMER.
    YEAST:G3O-33067-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone H4
    Gene namesi
    Name:HHF1
    Ordered Locus Names:YBR009C
    ORF Names:YBR0122
    AND
    Name:HHF2
    Ordered Locus Names:YNL030W
    ORF Names:N2752
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II, UP000002311: Chromosome XIV

    Organism-specific databases

    SGDiS000000213. HHF1.
    S000004975. HHF2.

    Subcellular locationi

    GO - Cellular componenti

    1. nuclear nucleosome Source: SGD
    2. replication fork protection complex Source: SGD

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedCurated
    Chaini2 – 103102Histone H4PRO_0000158377Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei6 – 61N6-acetyllysine1 Publication
    Modified residuei13 – 131N6-acetyllysine1 Publication
    Modified residuei17 – 171N6-acetyllysine3 Publications
    Modified residuei61 – 611Phosphoserine2 Publications
    Modified residuei65 – 651Phosphoserine2 Publications
    Modified residuei80 – 801N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP02309.
    PaxDbiP02309.

    Expressioni

    Gene expression databases

    GenevestigatoriP02309.

    Interactioni

    Subunit structurei

    The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. Histone H4 is a component of the UAF (upstream activation factor) complex which consists of UAF30, RRN5, RRN9, RRN10, and histones H3 and H4.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ASF1P324475EBI-8113,EBI-3003
    ESA1Q086495EBI-8113,EBI-6648
    FPR4Q062055EBI-8113,EBI-6956
    HHT2P618307EBI-8113,EBI-8098
    HIF1Q123735EBI-8113,EBI-31911
    KAT8Q9H7Z62EBI-8113,EBI-896414From a different organism.
    SET3P361242EBI-8113,EBI-16993
    STH1P325974EBI-8113,EBI-18410

    Protein-protein interaction databases

    BioGridi32710. 586 interactions.
    35797. 424 interactions.
    DIPiDIP-418N.
    IntActiP02309. 289 interactions.
    MINTiMINT-613388.
    STRINGi4932.YBR009C.

    Structurei

    Secondary structure

    1
    103
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 74
    Beta strandi16 – 194
    Helixi26 – 294
    Helixi32 – 4110
    Turni46 – 494
    Helixi51 – 7626
    Beta strandi80 – 823
    Helixi84 – 9310
    Beta strandi97 – 1015

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E6IX-ray1.87P16-30[»]
    1ID3X-ray3.10B/F2-103[»]
    1Q1AX-ray1.50B13-22[»]
    1SZCX-ray1.75B13-22[»]
    1SZDX-ray1.50B13-22[»]
    2DVQX-ray2.04P/Q2-16[»]
    2DVRX-ray2.30P/Q2-16[»]
    2E3KX-ray2.30Q/R2-16[»]
    2FSBmodel-B/F1-103[»]
    2H2HX-ray2.20B76-86[»]
    2L5ANMR-A42-103[»]
    2QQFX-ray2.00B13-23[»]
    2QQGX-ray2.05B13-23[»]
    3TO6X-ray2.10B12-23[»]
    4JJNX-ray3.09B/F2-103[»]
    4KUDX-ray3.20B/F1-103[»]
    ProteinModelPortaliP02309.
    SMRiP02309. Positions 13-103.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02309.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone H4 family.Curated

    Phylogenomic databases

    eggNOGiCOG2036.
    GeneTreeiENSGT00750000117310.
    HOGENOMiHOG000234654.
    KOiK11254.
    OMAiYEEVRVV.
    OrthoDBiEOG7HQNNQ.

    Family and domain databases

    Gene3Di1.10.20.10. 1 hit.
    InterProiIPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR001951. Histone_H4.
    IPR019809. Histone_H4_CS.
    [Graphical view]
    PfamiPF00125. Histone. 1 hit.
    [Graphical view]
    PRINTSiPR00623. HISTONEH4.
    SMARTiSM00417. H4. 1 hit.
    [Graphical view]
    SUPFAMiSSF47113. SSF47113. 1 hit.
    PROSITEiPS00047. HISTONE_H4. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P02309-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGRGKGGKG LGKGGAKRHR KILRDNIQGI TKPAIRRLAR RGGVKRISGL    50
    IYEEVRAVLK SFLESVIRDS VTYTEHAKRK TVTSLDVVYA LKRQGRTLYG 100
    FGG 103
    Length:103
    Mass (Da):11,368
    Last modified:January 23, 2007 - v2
    Checksum:i69B7D1F89E62DE41
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti46 – 461R → K AA sequence (PubMed:7002547)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00724 Genomic DNA. Translation: CAA25311.1.
    X00725 Genomic DNA. Translation: CAA25313.1.
    K03154 Genomic DNA. Translation: AAA34660.1.
    Z35878 Genomic DNA. Translation: CAA84947.1.
    Z71306 Genomic DNA. Translation: CAA95892.1.
    AY692960 Genomic DNA. Translation: AAT92979.1.
    BK006936 Genomic DNA. Translation: DAA07130.1.
    BK006947 Genomic DNA. Translation: DAA10515.1.
    PIRiA02647. HSBY4.
    RefSeqiNP_009563.1. NM_001178357.1.
    NP_014368.1. NM_001182869.1.

    Genome annotation databases

    EnsemblFungiiYBR009C; YBR009C; YBR009C.
    YNL030W; YNL030W; YNL030W.
    GeneIDi852294.
    855701.
    KEGGisce:YBR009C.
    sce:YNL030W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00724 Genomic DNA. Translation: CAA25311.1 .
    X00725 Genomic DNA. Translation: CAA25313.1 .
    K03154 Genomic DNA. Translation: AAA34660.1 .
    Z35878 Genomic DNA. Translation: CAA84947.1 .
    Z71306 Genomic DNA. Translation: CAA95892.1 .
    AY692960 Genomic DNA. Translation: AAT92979.1 .
    BK006936 Genomic DNA. Translation: DAA07130.1 .
    BK006947 Genomic DNA. Translation: DAA10515.1 .
    PIRi A02647. HSBY4.
    RefSeqi NP_009563.1. NM_001178357.1.
    NP_014368.1. NM_001182869.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1E6I X-ray 1.87 P 16-30 [» ]
    1ID3 X-ray 3.10 B/F 2-103 [» ]
    1Q1A X-ray 1.50 B 13-22 [» ]
    1SZC X-ray 1.75 B 13-22 [» ]
    1SZD X-ray 1.50 B 13-22 [» ]
    2DVQ X-ray 2.04 P/Q 2-16 [» ]
    2DVR X-ray 2.30 P/Q 2-16 [» ]
    2E3K X-ray 2.30 Q/R 2-16 [» ]
    2FSB model - B/F 1-103 [» ]
    2H2H X-ray 2.20 B 76-86 [» ]
    2L5A NMR - A 42-103 [» ]
    2QQF X-ray 2.00 B 13-23 [» ]
    2QQG X-ray 2.05 B 13-23 [» ]
    3TO6 X-ray 2.10 B 12-23 [» ]
    4JJN X-ray 3.09 B/F 2-103 [» ]
    4KUD X-ray 3.20 B/F 1-103 [» ]
    ProteinModelPortali P02309.
    SMRi P02309. Positions 13-103.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32710. 586 interactions.
    35797. 424 interactions.
    DIPi DIP-418N.
    IntActi P02309. 289 interactions.
    MINTi MINT-613388.
    STRINGi 4932.YBR009C.

    Proteomic databases

    MaxQBi P02309.
    PaxDbi P02309.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBR009C ; YBR009C ; YBR009C .
    YNL030W ; YNL030W ; YNL030W .
    GeneIDi 852294.
    855701.
    KEGGi sce:YBR009C.
    sce:YNL030W.

    Organism-specific databases

    SGDi S000000213. HHF1.
    S000004975. HHF2.

    Phylogenomic databases

    eggNOGi COG2036.
    GeneTreei ENSGT00750000117310.
    HOGENOMi HOG000234654.
    KOi K11254.
    OMAi YEEVRVV.
    OrthoDBi EOG7HQNNQ.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-28996-MONOMER.
    YEAST:G3O-33067-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P02309.
    NextBioi 970946.
    PROi P02309.

    Gene expression databases

    Genevestigatori P02309.

    Family and domain databases

    Gene3Di 1.10.20.10. 1 hit.
    InterProi IPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR001951. Histone_H4.
    IPR019809. Histone_H4_CS.
    [Graphical view ]
    Pfami PF00125. Histone. 1 hit.
    [Graphical view ]
    PRINTSi PR00623. HISTONEH4.
    SMARTi SM00417. H4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47113. SSF47113. 1 hit.
    PROSITEi PS00047. HISTONE_H4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "DNA sequences of yeast H3 and H4 histone genes from two non-allelic gene sets encode identical H3 and H4 proteins."
      Smith M.M., Andresson O.S.
      J. Mol. Biol. 169:663-690(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Lohan A.J.E., Wolfe K.H.
      Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "The genes coding for histone H3 and H4 in Neurospora crassa are unique and contain intervening sequences."
      Woudt L.P., Pastink A., Kempers-Veenstra A.E., Jansen A.E.M., Mager W.H., Planta R.J.
      Nucleic Acids Res. 11:5347-5360(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Carlsbergensis.
    4. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HHF1).
      Strain: ATCC 204508 / S288c.
    5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
      Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
      , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
      Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HHF2).
      Strain: ATCC 204508 / S288c.
    6. Cited for: GENOME REANNOTATION (HHF1 AND HHF2).
      Strain: ATCC 204508 / S288c.
    7. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    8. "The histones of yeast. The isolation and partial structure of the core histones."
      Brandt W.F., Patterson K., von Holt C.
      Eur. J. Biochem. 110:67-76(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-48; 69-83 AND 86-100, PROBABLE CLEAVAGE OF INITIATOR METHIONINE.
    9. "Histones H3 and H4 are components of upstream activation factor required for the high-level transcription of yeast rDNA by RNA polymerase I."
      Keener J., Dodd J.A., Lalo D., Nomura M.
      Proc. Natl. Acad. Sci. U.S.A. 94:13458-13462(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE UAF COMPLEX.
    10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    11. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 AND SER-65, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase gcn5p."
      Owen D.J., Ornaghi P., Yang J.C., Lowe N., Evans P.R., Ballario P., Neuhaus D., Filetici P., Travers A.A.
      EMBO J. 19:6141-6149(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 16-30, ACETYLATION AT LYS-17.
    15. "Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions."
      White C.L., Suto R.K., Luger K.
      EMBO J. 20:5207-5218(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF H4 IN NUCLEOSOME COMPLEX.
    16. "Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone/protein deacetylases."
      Zhao K., Harshaw R., Chai X., Marmorstein R.
      Proc. Natl. Acad. Sci. U.S.A. 101:8563-8568(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 13-22, ACETYLATION AT LYS-17.
    17. Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 76-86, ACETYLATION AT LYS-80.
    18. Cited for: 3D-STRUCTURE MODELING.
    19. "Structural basis for diacetylated histone H4 tail recognition by the second bromodomain of human BRD2."
      Padmanabhan B., Umehara T., Nakano K., Jang M.K., Ozato K., Yokohama S.
      Submitted (NOV-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-16, ACETYLATION AT LYS-6 AND LYS-13.
    20. "Structural basis for nicotinamide inhibition and base exchange in Sir2 enzymes."
      Sanders B.D., Zhao K., Slama J.T., Marmorstein R.
      Mol. Cell 25:463-472(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 13-23, ACETYLATION AT LYS-17.
    21. "Structural basis for recognition of centromere histone variant CenH3 by the chaperone Scm3."
      Zhou Z., Feng H., Zhou B.R., Ghirlando R., Hu K., Zwolak A., Miller Jenkins L.M., Xiao H., Tjandra N., Wu C., Bai Y.
      Nature 472:234-237(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 42-103.
    22. Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 12-23.

    Entry informationi

    Entry nameiH4_YEAST
    AccessioniPrimary (citable) accession number: P02309
    Secondary accession number(s): D6VQ10
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 160 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 524000 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3