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Q02336

- ADA2_YEAST

UniProt

Q02336 - ADA2_YEAST

Protein

Transcriptional adapter 2

Gene

ADA2

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 147 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    Functioni

    Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA 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 (to form H3K14ac and H3K18ac) and H2B.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1 – 4848ZZ-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: SGD
    2. DNA binding Source: InterPro
    3. phosphatidylserine binding Source: SGD
    4. protein binding Source: IntAct
    5. transcription coactivator activity Source: SGD
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. chromatin modification Source: SGD
    2. chromatin silencing at rDNA Source: SGD
    3. chromatin silencing at telomere Source: SGD
    4. histone acetylation Source: GOC
    5. positive regulation of histone acetylation Source: SGD
    6. regulation of transcription from RNA polymerase II promoter Source: SGD
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29979-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcriptional adapter 2
    Gene namesi
    Name:ADA2
    Ordered Locus Names:YDR448W
    ORF Names:D9461.33
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR448w.
    SGDiS000002856. ADA2.

    Subcellular locationi

    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 – 434434Transcriptional adapter 2PRO_0000197082Add
    BLAST

    Proteomic databases

    MaxQBiQ02336.
    PaxDbiQ02336.
    PeptideAtlasiQ02336.

    Expressioni

    Gene expression databases

    GenevestigatoriQ02336.

    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. ADA2 interacts with GCN5.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GCN5Q0333035EBI-2186,EBI-7458
    HFI1Q1206022EBI-2186,EBI-8287
    NGG1P3249425EBI-2186,EBI-2192
    SLT2Q007722EBI-2186,EBI-17372
    TRA1P3881123EBI-2186,EBI-24638

    Protein-protein interaction databases

    BioGridi32503. 265 interactions.
    DIPiDIP-183N.
    IntActiQ02336. 162 interactions.
    MINTiMINT-403023.
    STRINGi4932.YDR448W.

    Structurei

    Secondary structure

    1
    434
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi358 – 3614
    Beta strandi367 – 3693
    Helixi371 – 3799
    Helixi384 – 40118
    Helixi407 – 4137
    Helixi418 – 43013

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ELJNMR-A354-434[»]
    ProteinModelPortaliQ02336.
    SMRiQ02336. Positions 64-110, 348-434.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ02336.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini60 – 11253SANTPROSITE-ProRule annotationAdd
    BLAST
    Domaini349 – 43486SWIRMPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 SANT domain.PROSITE-ProRule annotation
    Contains 1 SWIRM domain.PROSITE-ProRule annotation
    Contains 1 ZZ-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1 – 4848ZZ-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5114.
    GeneTreeiENSGT00530000063657.
    HOGENOMiHOG000163455.
    KOiK11314.
    OMAiREKVLCN.
    OrthoDBiEOG7XM380.

    Family and domain databases

    Gene3Di1.10.10.60. 1 hit.
    InterProiIPR009057. Homeodomain-like.
    IPR001005. SANT/Myb.
    IPR017884. SANT_dom.
    IPR007526. SWIRM.
    IPR016827. Transcriptional_adaptor_2.
    IPR000433. Znf_ZZ.
    [Graphical view]
    PfamiPF00249. Myb_DNA-binding. 1 hit.
    PF04433. SWIRM. 1 hit.
    PF00569. ZZ. 1 hit.
    [Graphical view]
    PIRSFiPIRSF025024. Transcriptional_adaptor_2. 1 hit.
    SMARTiSM00717. SANT. 1 hit.
    SM00291. ZnF_ZZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF46689. SSF46689. 2 hits.
    PROSITEiPS51293. SANT. 1 hit.
    PS50934. SWIRM. 1 hit.
    PS01357. ZF_ZZ_1. 1 hit.
    PS50135. ZF_ZZ_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q02336-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNKFHCDVC SADCTNRVRV SCAICPEYDL CVPCFSQGSY TGKHRPYHDY    50
    RIIETNSYPI LCPDWGADEE LQLIKGAQTL GLGNWQDIAD HIGSRGKEEV 100
    KEHYLKYYLE SKYYPIPDIT QNIHVPQDEF LEQRRHRIES FRERPLEPPR 150
    KPMASVPSCH EVQGFMPGRL EFETEFENEA EGPVKDMVFE PDDQPLDIEL 200
    KFAILDIYNS RLTTRAEKKR LLFENHLMDY RKLQAIDKKR SKEAKELYNR 250
    IKPFARVMTA QDFEEFSKDI LEELHCRARI QQLQEWRSNG LTTLEAGLKY 300
    ERDKQARISS FEKFGASTAA SLSEGNSRYR SNSAHRSNAE YSQNYSENGG 350
    RKKNMTISDI QHAPDYALLS NDEQQLCIQL KILPKPYLVL KEVMFRELLK 400
    TGGNLSKSAC RELLNIDPIK ANRIYDFFQS QNWM 434
    Length:434
    Mass (Da):50,569
    Last modified:July 1, 1993 - v1
    Checksum:i9637E1EDBBED0AC3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M95396 Genomic DNA. Translation: AAA34393.1.
    U33007 Genomic DNA. Translation: AAB64871.1.
    BK006938 Genomic DNA. Translation: DAA12283.1.
    PIRiA43252.
    RefSeqiNP_010736.3. NM_001180756.3.

    Genome annotation databases

    EnsemblFungiiYDR448W; YDR448W; YDR448W.
    GeneIDi852059.
    KEGGisce:YDR448W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M95396 Genomic DNA. Translation: AAA34393.1 .
    U33007 Genomic DNA. Translation: AAB64871.1 .
    BK006938 Genomic DNA. Translation: DAA12283.1 .
    PIRi A43252.
    RefSeqi NP_010736.3. NM_001180756.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ELJ NMR - A 354-434 [» ]
    ProteinModelPortali Q02336.
    SMRi Q02336. Positions 64-110, 348-434.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32503. 265 interactions.
    DIPi DIP-183N.
    IntActi Q02336. 162 interactions.
    MINTi MINT-403023.
    STRINGi 4932.YDR448W.

    Proteomic databases

    MaxQBi Q02336.
    PaxDbi Q02336.
    PeptideAtlasi Q02336.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR448W ; YDR448W ; YDR448W .
    GeneIDi 852059.
    KEGGi sce:YDR448W.

    Organism-specific databases

    CYGDi YDR448w.
    SGDi S000002856. ADA2.

    Phylogenomic databases

    eggNOGi COG5114.
    GeneTreei ENSGT00530000063657.
    HOGENOMi HOG000163455.
    KOi K11314.
    OMAi REKVLCN.
    OrthoDBi EOG7XM380.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29979-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q02336.
    NextBioi 970331.
    PROi Q02336.

    Gene expression databases

    Genevestigatori Q02336.

    Family and domain databases

    Gene3Di 1.10.10.60. 1 hit.
    InterProi IPR009057. Homeodomain-like.
    IPR001005. SANT/Myb.
    IPR017884. SANT_dom.
    IPR007526. SWIRM.
    IPR016827. Transcriptional_adaptor_2.
    IPR000433. Znf_ZZ.
    [Graphical view ]
    Pfami PF00249. Myb_DNA-binding. 1 hit.
    PF04433. SWIRM. 1 hit.
    PF00569. ZZ. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF025024. Transcriptional_adaptor_2. 1 hit.
    SMARTi SM00717. SANT. 1 hit.
    SM00291. ZnF_ZZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46689. SSF46689. 2 hits.
    PROSITEi PS51293. SANT. 1 hit.
    PS50934. SWIRM. 1 hit.
    PS01357. ZF_ZZ_1. 1 hit.
    PS50135. ZF_ZZ_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genetic isolation of ADA2: a potential transcriptional adaptor required for function of certain acidic activation domains."
      Berger S.L., Pina B., Silverman N., Marcus G.A., Agapite J., Regier J.L., Triezenberg S.J., Guarente L.
      Cell 70:251-265(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Functional similarity and physical association between GCN5 and ADA2: putative transcriptional adaptors."
      Marcus G.A., Silverman N., Berger S.L., Horiuchi J., Guarente L.
      EMBO J. 13:4807-4815(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GCN5.
    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; ADA3 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. "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.
    15. "Solution structure of the SWIRM domain of baker's yeast transcriptional adapter 2."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 348-434.

    Entry informationi

    Entry nameiADA2_YEAST
    AccessioniPrimary (citable) accession number: Q02336
    Secondary accession number(s): D6VT73
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 147 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 1720 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, 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 IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3