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Q02336

- ADA2_YEAST

UniProt

Q02336 - ADA2_YEAST

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Protein
Transcriptional adapter 2
Gene
ADA2, YDR448W, D9461.33
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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-type
Add
BLAST

GO - Molecular functioni

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

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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434Transcriptional adapter 2
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiQ02336.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini60 – 11253SANT
Add
BLAST
Domaini349 – 43486SWIRM
Add
BLAST

Sequence similaritiesi

Contains 1 SANT domain.
Contains 1 SWIRM domain.

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...

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 146 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.

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

Similar proteinsi