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Q02336 (ADA2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcriptional adapter 2
Gene names
Name:ADA2
Ordered Locus Names:YDR448W
ORF Names:D9461.33
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8

Subunit structure

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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.13

Subcellular location

Nucleus.

Miscellaneous

Present with 1720 molecules/cell in log phase SD medium.

Sequence similarities

Contains 1 SANT domain.

Contains 1 SWIRM domain.

Contains 1 ZZ-type zinc finger.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin modification

Inferred from direct assay Ref.6. Source: SGD

chromatin silencing at rDNA

Inferred from mutant phenotype PubMed 19737915. Source: SGD

chromatin silencing at telomere

Inferred from mutant phenotype PubMed 19737915. Source: SGD

histone acetylation

Inferred from direct assay PubMed 11773077. Source: GOC

positive regulation of histone acetylation

Inferred from mutant phenotype PubMed 12419236. Source: SGD

regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 18950642. Source: SGD

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentAda2/Gcn5/Ada3 transcription activator complex

Inferred from direct assay Ref.9PubMed 7862114. Source: SGD

SAGA complex

Inferred from direct assay PubMed 9224714Ref.6. Source: SGD

SLIK (SAGA-like) complex

Inferred from direct assay Ref.10. Source: SGD

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

chromatin binding

Inferred from direct assay PubMed 19737915. Source: SGD

phosphatidylserine binding

Inferred from direct assay PubMed 18950642. Source: SGD

protein binding

Inferred from physical interaction Ref.9PubMed 10688190PubMed 11283351Ref.11Ref.10PubMed 14660704PubMed 15506919PubMed 16429126PubMed 16888622PubMed 20434206PubMed 20489023PubMed 21179020PubMed 21376235PubMed 21734642Ref.6PubMed 9756893. Source: IntAct

transcription coactivator activity

Inferred from direct assay PubMed 7972120. Source: SGD

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 434434Transcriptional adapter 2
PRO_0000197082

Regions

Domain60 – 11253SANT
Domain349 – 43486SWIRM
Zinc finger1 – 4848ZZ-type

Secondary structure

............. 434
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q02336 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 9637E1EDBBED0AC3

FASTA43450,569
        10         20         30         40         50         60 
MSNKFHCDVC SADCTNRVRV SCAICPEYDL CVPCFSQGSY TGKHRPYHDY RIIETNSYPI 

        70         80         90        100        110        120 
LCPDWGADEE LQLIKGAQTL GLGNWQDIAD HIGSRGKEEV KEHYLKYYLE SKYYPIPDIT 

       130        140        150        160        170        180 
QNIHVPQDEF LEQRRHRIES FRERPLEPPR KPMASVPSCH EVQGFMPGRL EFETEFENEA 

       190        200        210        220        230        240 
EGPVKDMVFE PDDQPLDIEL KFAILDIYNS RLTTRAEKKR LLFENHLMDY RKLQAIDKKR 

       250        260        270        280        290        300 
SKEAKELYNR IKPFARVMTA QDFEEFSKDI LEELHCRARI QQLQEWRSNG LTTLEAGLKY 

       310        320        330        340        350        360 
ERDKQARISS FEKFGASTAA SLSEGNSRYR SNSAHRSNAE YSQNYSENGG RKKNMTISDI 

       370        380        390        400        410        420 
QHAPDYALLS NDEQQLCIQL KILPKPYLVL KEVMFRELLK TGGNLSKSAC RELLNIDPIK 

       430 
ANRIYDFFQS QNWM 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M95396 Genomic DNA. Translation: AAA34393.1.
U33007 Genomic DNA. Translation: AAB64871.1.
BK006938 Genomic DNA. Translation: DAA12283.1.
PIRA43252.
RefSeqNP_010736.3. NM_001180756.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ELJNMR-A354-434[»]
ProteinModelPortalQ02336.
SMRQ02336. Positions 64-110, 348-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32503. 265 interactions.
DIPDIP-183N.
IntActQ02336. 162 interactions.
MINTMINT-403023.
STRING4932.YDR448W.

Proteomic databases

MaxQBQ02336.
PaxDbQ02336.
PeptideAtlasQ02336.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR448W; YDR448W; YDR448W.
GeneID852059.
KEGGsce:YDR448W.

Organism-specific databases

CYGDYDR448w.
SGDS000002856. ADA2.

Phylogenomic databases

eggNOGCOG5114.
GeneTreeENSGT00530000063657.
HOGENOMHOG000163455.
KOK11314.
OMAREKVLCN.
OrthoDBEOG7XM380.

Enzyme and pathway databases

BioCycYEAST:G3O-29979-MONOMER.

Gene expression databases

GenevestigatorQ02336.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
InterProIPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR007526. SWIRM.
IPR016827. Transcriptional_adaptor_2.
IPR000433. Znf_ZZ.
[Graphical view]
PfamPF00249. Myb_DNA-binding. 1 hit.
PF04433. SWIRM. 1 hit.
PF00569. ZZ. 1 hit.
[Graphical view]
PIRSFPIRSF025024. Transcriptional_adaptor_2. 1 hit.
SMARTSM00717. SANT. 1 hit.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMSSF46689. SSF46689. 2 hits.
PROSITEPS51293. SANT. 1 hit.
PS50934. SWIRM. 1 hit.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ02336.
NextBio970331.
PROQ02336.

Entry information

Entry nameADA2_YEAST
AccessionPrimary (citable) accession number: Q02336
Secondary accession number(s): D6VT73
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

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

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references