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P32494

- NGG1_YEAST

UniProt

P32494 - NGG1_YEAST

Protein

Chromatin-remodeling complexes subunit NGG1

Gene

NGG1

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 126 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    Transcription regulator. Could inhibit GAL4 DNA-binding or its ability to activate transcription. Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA, SLIK and ADA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. ADA preferentially acetylates nucleosomal histones H3 (at 'Lys-14' and 'Lys-18') and H2B.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. chromatin modification Source: SGD
    2. histone acetylation Source: SGD
    3. regulation of transcription, DNA-templated Source: UniProtKB-KW
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29765-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chromatin-remodeling complexes subunit NGG1
    Alternative name(s):
    Transcriptional adapter 3
    Gene namesi
    Name:NGG1
    Synonyms:ADA3, SWI7
    Ordered Locus Names:YDR176W
    ORF Names:YD9395.09
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR176w.
    SGDiS000002583. NGG1.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. Ada2/Gcn5/Ada3 transcription activator complex Source: SGD
    2. SAGA complex Source: SGD
    3. SLIK (SAGA-like) complex Source: SGD

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 702702Chromatin-remodeling complexes subunit NGG1PRO_0000064448Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei134 – 1341Phosphoserine3 Publications
    Modified residuei407 – 4071Phosphoserine1 Publication
    Modified residuei464 – 4641Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP32494.
    PaxDbiP32494.
    PeptideAtlasiP32494.

    Expressioni

    Gene expression databases

    GenevestigatoriP32494.

    Interactioni

    Subunit structurei

    Component of the 1.8 MDa SAGA complex, which consists of at least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. Component of the SALSA complex, which consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3. Component of the SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9. Component of the ADA/GCN5 complex that consists of HFI1/ADA1, ADA2, ADA3, SPT20/ADA5 and GCN5 and is probably a subcomplex of SAGA. Component of the 0.8 MDa ADA complex, which at least consists of ADA2, ADA3, AHC1 and GCN5.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADA2Q0233625EBI-2192,EBI-2186
    HFI1Q120605EBI-2192,EBI-8287
    SGF29P255545EBI-2192,EBI-21678
    SPT8P389157EBI-2192,EBI-17964
    TRA1P388113EBI-2192,EBI-24638

    Protein-protein interaction databases

    BioGridi32229. 125 interactions.
    DIPiDIP-774N.
    IntActiP32494. 33 interactions.
    MINTiMINT-490762.
    STRINGi4932.YDR176W.

    Structurei

    3D structure databases

    ProteinModelPortaliP32494.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi606 – 61813Nuclear localization signalSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the NGG1 family.Curated

    Phylogenomic databases

    eggNOGiNOG304305.
    HOGENOMiHOG000248582.
    KOiK11315.
    OMAiKRELKYI.
    OrthoDBiEOG7N63WV.

    Family and domain databases

    InterProiIPR019340. Histone_AcTrfase_su3.
    [Graphical view]
    PfamiPF10198. Ada3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32494-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPRHGRRGKL PKGEKLPKKE GGDNTPSKLL SSMLKTLDLT FERDIGMLNG    50
    KSVRSIPNKK TLLELQSQLD SLNEILGTIA RGDQETIEAL RKIRDSKNEK 100
    QANDEKQETS NADGQHESST ATEETNIIDK GVQSPPKPPP SNEISGTIEN 150
    DVESIKQAAD NMAKEEINED KDLQVHRDQP REKRPFDSET ENRATENENT 200
    QRPDNKKQKI DVDKMENDPT VKNPKSEFVV SQTLPRAAAA LGLFNEEGLE 250
    STGEDFLKKK YNVASYPTND LKDLLPGELP DMDFSHPKPT NQIQFNTFLA 300
    FVENFFKDLS DDNLKFLKMK YIIPDSLQFD KTYDPEVNPF IIPKLGPLYT 350
    DVWFKDENDK NSAYKKPSPY SNDASTILPK KSANELDDNA LESGSISCGP 400
    LLSRLLSAVL KDDNDKSELQ SSKIIRDGGL PRTGGEDDIQ SFRNNNNDTV 450
    DMTLSQENGP SVQTPDNDID EEASFQAKLA ENKGSNGGTT STLPQQIGWI 500
    TNGINLDYPT FEERLKRELK YVGIYMNLPK DENNPNSDDP DWVTGREDDE 550
    ISAELRELQG TLKQVTKKNQ KRKAQLIPLV ERQLAWQEYS SILEDLDKQI 600
    DQAYVKRIRV PKKRKKHHTA ASNNVNTGTT SQIAQQKAAN SSLKSLLDKR 650
    QRWINKIGPL FDKPEIMKRI PNESVFKDMD QEEDEDEADV FAQNTNKDVE 700
    LN 702
    Length:702
    Mass (Da):79,282
    Last modified:October 1, 1993 - v1
    Checksum:i489016BFD1C095D4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti520 – 5201K → M in AAA03542. (PubMed:8413201)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L12137 Genomic DNA. Translation: AAA21684.1.
    L21189 Unassigned DNA. Translation: AAA03542.1. Sequence problems.
    Z46727 Genomic DNA. Translation: CAA86681.1.
    BK006938 Genomic DNA. Translation: DAA12018.1.
    PIRiS41685.
    RefSeqiNP_010461.3. NM_001180483.3.

    Genome annotation databases

    EnsemblFungiiYDR176W; YDR176W; YDR176W.
    GeneIDi851756.
    KEGGisce:YDR176W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L12137 Genomic DNA. Translation: AAA21684.1 .
    L21189 Unassigned DNA. Translation: AAA03542.1 . Sequence problems.
    Z46727 Genomic DNA. Translation: CAA86681.1 .
    BK006938 Genomic DNA. Translation: DAA12018.1 .
    PIRi S41685.
    RefSeqi NP_010461.3. NM_001180483.3.

    3D structure databases

    ProteinModelPortali P32494.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32229. 125 interactions.
    DIPi DIP-774N.
    IntActi P32494. 33 interactions.
    MINTi MINT-490762.
    STRINGi 4932.YDR176W.

    Proteomic databases

    MaxQBi P32494.
    PaxDbi P32494.
    PeptideAtlasi P32494.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR176W ; YDR176W ; YDR176W .
    GeneIDi 851756.
    KEGGi sce:YDR176W.

    Organism-specific databases

    CYGDi YDR176w.
    SGDi S000002583. NGG1.

    Phylogenomic databases

    eggNOGi NOG304305.
    HOGENOMi HOG000248582.
    KOi K11315.
    OMAi KRELKYI.
    OrthoDBi EOG7N63WV.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29765-MONOMER.

    Miscellaneous databases

    NextBioi 969522.

    Gene expression databases

    Genevestigatori P32494.

    Family and domain databases

    InterProi IPR019340. Histone_AcTrfase_su3.
    [Graphical view ]
    Pfami PF10198. Ada3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of NGG1, a novel yeast gene required for glucose repression of GAL4p-regulated transcription."
      Brandl C.J., Furlanetto A.M., Martens J.A., Hamilton K.S.
      EMBO J. 12:5255-5265(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "ADA3: a gene, identified by resistance to GAL4-VP16, with properties similar to and different from those of ADA2."
      Pina B., Berger S.L., Marcus G.A., Silverman N., Agapite J., Guarente L.
      Mol. Cell. Biol. 13:5981-5989(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "ADA1, a novel component of the ADA/GCN5 complex, has broader effects than GCN5, ADA2, or ADA3."
      Horiuchi J., Silverman N., Pina B., Marcus G.A., Guarente L.
      Mol. Cell. Biol. 17:3220-3228(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE ADA/GCN5 COMPLEX.
      Strain: ATCC MYA-3516 / BWG1-7A.
    6. "A subset of TAF(II)s are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulation."
      Grant P.A., Schieltz D., Pray-Grant M.G., Steger D.J., Reese J.C., Yates J.R. III, Workman J.L.
      Cell 94:45-53(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SAGA COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    7. "The ATM-related cofactor Tra1 is a component of the purified SAGA complex."
      Grant P.A., Schieltz D., Pray-Grant M.G., Yates J.R. III, Workman J.L.
      Mol. Cell 2:863-867(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A SAGA COMPLEX WITH SPT7; HFI1; SPT8; GCN5; SPT20; SPT2; ADA2 AND TRA1.
    8. "Expanded lysine acetylation specificity of Gcn5 in native complexes."
      Grant P.A., Eberharter A., John S., Cook R.G., Turner B.M., Workman J.L.
      J. Biol. Chem. 274:5895-5900(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEX, FUNCTION IN HISTONE ACETYLATION AT THE ADA COMPLEX.
    9. "The ADA complex is a distinct histone acetyltransferase complex in Saccharomyces cerevisiae."
      Eberharter A., Sterner D.E., Schieltz D., Hassan A., Yates J.R. III, Berger S.L., Workman J.L.
      Mol. Cell. Biol. 19:6621-6631(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE ADA COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "The novel SLIK histone acetyltransferase complex functions in the yeast retrograde response pathway."
      Pray-Grant M.G., Schieltz D., McMahon S.J., Wood J.M., Kennedy E.L., Cook R.G., Workman J.L., Yates J.R. III, Grant P.A.
      Mol. Cell. Biol. 22:8774-8786(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SLIK COMPLEX.
    11. "SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates with activated transcription."
      Sterner D.E., Belotserkovskaya R., Berger S.L.
      Proc. Natl. Acad. Sci. U.S.A. 99:11622-11627(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SALSA COMPLEX.
    12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    13. "Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation."
      Pray-Grant M.G., Daniel J.A., Schieltz D., Yates J.R. III, Grant P.A.
      Nature 433:434-438(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SLIK COMPLEX.
    14. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    15. "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-134 AND SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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-134 AND THR-464, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Molecular architecture of the S. cerevisiae SAGA complex."
      Wu P.Y., Ruhlmann C., Winston F., Schultz P.
      Mol. Cell 15:199-208(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF THE SAGA COMPLEX.

    Entry informationi

    Entry nameiNGG1_YEAST
    AccessioniPrimary (citable) accession number: P32494
    Secondary accession number(s): D6VSF8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 126 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 2470 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, 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 IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3