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P38806

- YNG2_YEAST

UniProt

P38806 - YNG2_YEAST

Protein

Chromatin modification-related protein YNG2

Gene

YNG2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Involved in cell cycle progression and meiosis.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei224 – 2241Histone H3K4me3By similarity
    Binding sitei235 – 2351Histone H3K4me3By similarity
    Binding sitei239 – 2391Histone H3K4me3By similarity
    Binding sitei247 – 2471Histone H3K4me3By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri222 – 27150PHD-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. methylated histone binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. chromatin modification Source: SGD
    2. DNA repair Source: SGD
    3. histone acetylation Source: SGD
    4. meiotic nuclear division Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Biological processi

    Cell cycle, DNA damage, DNA repair, Meiosis

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31137-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chromatin modification-related protein YNG2
    Alternative name(s):
    ESA1-associated factor 4
    ING1 homolog 2
    Gene namesi
    Name:YNG2
    Synonyms:EAF4, NBN1
    Ordered Locus Names:YHR090C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VIII

    Organism-specific databases

    CYGDiYHR090c.
    SGDiS000001132. YNG2.

    Subcellular locationi

    Nucleus 3 Publications

    GO - Cellular componenti

    1. cytosol Source: SGD
    2. NuA4 histone acetyltransferase complex Source: SGD
    3. nucleus Source: SGD
    4. Piccolo NuA4 histone acetyltransferase complex Source: SGD

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 282282Chromatin modification-related protein YNG2PRO_0000212679Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei183 – 1831Phosphoserine1 Publication
    Modified residuei185 – 1851Phosphothreonine1 Publication
    Modified residuei188 – 1881Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP38806.
    PaxDbiP38806.
    PeptideAtlasiP38806.

    Expressioni

    Gene expression databases

    GenevestigatoriP38806.

    Interactioni

    Subunit structurei

    Interacts with H3K4me3 and to a lesser extent with H3K4me2. Component of the NuA4 histone acetyltransferase complex composed of at least ACT1, ARP4, YAF9, VID21, SWC4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1, TRA1 and YNG2.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EPL1P435724EBI-24622,EBI-22792

    Protein-protein interaction databases

    BioGridi36525. 284 interactions.
    DIPiDIP-2095N.
    IntActiP38806. 18 interactions.
    MINTiMINT-561028.
    STRINGi4932.YHR090C.

    Structurei

    3D structure databases

    ProteinModelPortaliP38806.
    SMRiP38806. Positions 223-269.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili35 – 8652Sequence AnalysisAdd
    BLAST

    Domaini

    The PHD-type zinc finger mediates the binding to H3K4me3.1 Publication

    Sequence similaritiesi

    Belongs to the ING family.Curated
    Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri222 – 27150PHD-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5034.
    GeneTreeiENSGT00550000074538.
    HOGENOMiHOG000000883.
    KOiK11396.
    OMAiTLTKHPK.
    OrthoDBiEOG7G1VHM.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR028651. ING_fam.
    IPR024610. ING_N.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PANTHERiPTHR10333. PTHR10333. 1 hit.
    PfamiPF12998. ING. 1 hit.
    PF00628. PHD. 1 hit.
    [Graphical view]
    SMARTiSM00249. PHD. 1 hit.
    [Graphical view]
    SUPFAMiSSF57903. SSF57903. 1 hit.
    PROSITEiPS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P38806-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDPSLVLEQT IQDVSNLPSE FRYLLEEIGS NDLKLIEEKK KYEQKESQIH    50
    KFIRQQGSIP KHPQEDGLDK EIKESLLKCQ SLQREKCVLA NTALFLIARH 100
    LNKLEKNIAL LEEDGVLAPV EEDGDMDSAA EASRESSVVS NSSVKKRRAA 150
    SSSGSVPPTL KKKKTSRTSK LQNEIDVSSR EKSVTPVSPS IEKKIARTKE 200
    FKNSRNGKGQ NGSPENEEED KTLYCFCQRV SFGEMVACDG PNCKYEWFHY 250
    DCVNLKEPPK GTWYCPECKI EMEKNKLKRK RN 282
    Length:282
    Mass (Da):32,086
    Last modified:February 1, 1995 - v1
    Checksum:i110E0A2536547D03
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00060 Genomic DNA. Translation: AAB68930.1.
    BK006934 Genomic DNA. Translation: DAA06786.1.
    PIRiS46722.
    RefSeqiNP_011958.1. NM_001179220.1.

    Genome annotation databases

    EnsemblFungiiYHR090C; YHR090C; YHR090C.
    GeneIDi856490.
    KEGGisce:YHR090C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00060 Genomic DNA. Translation: AAB68930.1 .
    BK006934 Genomic DNA. Translation: DAA06786.1 .
    PIRi S46722.
    RefSeqi NP_011958.1. NM_001179220.1.

    3D structure databases

    ProteinModelPortali P38806.
    SMRi P38806. Positions 223-269.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36525. 284 interactions.
    DIPi DIP-2095N.
    IntActi P38806. 18 interactions.
    MINTi MINT-561028.
    STRINGi 4932.YHR090C.

    Proteomic databases

    MaxQBi P38806.
    PaxDbi P38806.
    PeptideAtlasi P38806.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YHR090C ; YHR090C ; YHR090C .
    GeneIDi 856490.
    KEGGi sce:YHR090C.

    Organism-specific databases

    CYGDi YHR090c.
    SGDi S000001132. YNG2.

    Phylogenomic databases

    eggNOGi COG5034.
    GeneTreei ENSGT00550000074538.
    HOGENOMi HOG000000883.
    KOi K11396.
    OMAi TLTKHPK.
    OrthoDBi EOG7G1VHM.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31137-MONOMER.

    Miscellaneous databases

    NextBioi 982194.
    PROi P38806.

    Gene expression databases

    Genevestigatori P38806.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR028651. ING_fam.
    IPR024610. ING_N.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    PANTHERi PTHR10333. PTHR10333. 1 hit.
    Pfami PF12998. ING. 1 hit.
    PF00628. PHD. 1 hit.
    [Graphical view ]
    SMARTi SM00249. PHD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57903. SSF57903. 1 hit.
    PROSITEi PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "Three yeast proteins related to the human candidate tumor suppressor p33(ING1) are associated with histone acetyltransferase activities."
      Loewith R., Meijer M., Lees-Miller S.P., Riabowol K., Young D.
      Mol. Cell. Biol. 20:3807-3816(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE NUA4 COMPLEX.
    4. "Yng2p-dependent NuA4 histone H4 acetylation activity is required for mitotic and meiotic progression."
      Choy J.S., Tobe B.T.D., Huh J.H., Kron S.J.
      J. Biol. Chem. 276:43653-43662(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    5. "Role of an ING1 growth regulator in transcriptional activation and targeted histone acetylation by the NuA4 complex."
      Nourani A., Doyon Y., Utley R.T., Allard S., Lane W.S., Cote J.
      Mol. Cell. Biol. 21:7629-7640(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-34; 62-70; 107-161; 171-180 AND 184-193, IDENTIFICATION IN THE NUA4 COMPLEX, FUNCTION.
    6. "NuA4 subunit Yng2 function in intra-S-phase DNA damage response."
      Choy J.S., Kron S.J.
      Mol. Cell. Biol. 22:8215-8225(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    8. "The Yaf9 component of the SWR1 and NuA4 complexes is required for proper gene expression, histone H4 acetylation, and Htz1 replacement near telomeres."
      Zhang H., Richardson D.O., Roberts D.N., Utley R.T., Erdjument-Bromage H., Tempst P., Cote J., Cairns B.R.
      Mol. Cell. Biol. 24:9424-9436(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    9. "A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin."
      Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W., Jennings J.L., Link A.J., Madhani H.D., Rine J.
      PLoS Biol. 2:587-599(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "Regulation of chromosome stability by the histone H2A variant Htz1, the Swr1 chromatin remodeling complex, and the histone acetyltransferase NuA4."
      Krogan N.J., Baetz K., Keogh M.-C., Datta N., Sawa C., Kwok T.C.Y., Thompson N.J., Davey M.G., Pootoolal J., Hughes T.R., Emili A., Buratowski S., Hieter P., Greenblatt J.F.
      Proc. Natl. Acad. Sci. U.S.A. 101:13513-13518(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    11. Cited for: DOMAIN PHD-TYPE ZINC-FINGER, INTERACTION WITH HISTONES H3K4ME3 AND H3K4ME2.
    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: 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-183; THR-185 AND SER-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiYNG2_YEAST
    AccessioniPrimary (citable) accession number: P38806
    Secondary accession number(s): D3DL42
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 120 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3