Q02336 (ADA2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcriptional adapter 2

Gene names

Name:	ADA2
Ordered Locus Names:	YDR448W
ORF Names:	D9461.33

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Ada2/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_function	DNA binding Inferred from electronic annotation. Source: InterPro chromatin binding Inferred from direct assay PubMed 19737915. Source: SGD phosphatidylserine binding Inferred from mutant phenotype PubMed 18950642. Source: SGD transcription coactivator activity Inferred from direct assay PubMed 7972120. Source: SGD zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GCN5	Q03330	37	EBI-2186,EBI-7458
NGG1	P32494	27	EBI-2186,EBI-2192
SLT2	Q00772	2	EBI-2186,EBI-17372
THP1	Q08231	2	EBI-2186,EBI-32097
TRA1	P38811	25	EBI-2186,EBI-24638

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 434

434

Transcriptional adapter 2

PRO_0000197082

Regions

Domain

60 – 112

53

SANT

Domain

349 – 434

86

SWIRM

Zinc finger

1 – 48

48

ZZ-type

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

434

Helix Strand Turn

Details...

Helix

358 – 361

4

Beta strand

367 – 369

3

Helix

371 – 379

9

Helix

384 – 401

18

Helix

407 – 413

7

Helix

418 – 430

13

Sequences

	Sequence		Length	Mass (Da)
	Q02336 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 9637E1EDBBED0AC3	FASTA	434	50,569
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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, 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, 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.

PIR

A43252.

RefSeq

NP_010736.3. NM_001180756.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ELJ	NMR	-	A	354-434	[»]

ProteinModelPortal

Q02336.

SMR

Q02336. Positions 64-110, 348-434.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-183N.

IntAct

Q02336. 167 interactions.

MINT

MINT-403023.

STRING

4932.YDR448W.

Proteomic databases

PaxDb

Q02336.

PeptideAtlas

Q02336.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR448W; YDR448W; YDR448W.

GeneID

852059.

KEGG

sce:YDR448W.
sce:YDR452W.

Organism-specific databases

CYGD

YDR448w.

SGD

S000002856. ADA2.

Phylogenomic databases

eggNOG

COG5114.

GeneTree

ENSGT00530000063657.

HOGENOM

HOG000163455.

KO

K06018.
K11314.

OMA

GRSPSHI.

OrthoDB

EOG441TKV.

Gene expression databases

Genevestigator

Q02336.

GermOnline

YDR448W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

1.10.10.60. 1 hit.

InterPro

IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR007526. SWIRM.
IPR016827. Transcriptional_adaptor_2.
IPR000433. Znf_ZZ.
[Graphical view]

Pfam

PF00249. Myb_DNA-binding. 1 hit.
PF04433. SWIRM. 1 hit.
PF00569. ZZ. 1 hit.
[Graphical view]

PIRSF

PIRSF025024. Transcriptional_adaptor_2. 1 hit.

SMART

SM00717. SANT. 1 hit.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]

SUPFAM

SSF46689. Homeodomain_like. 2 hits.

PROSITE

PS51293. SANT. 1 hit.
PS50934. SWIRM. 1 hit.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q02336.

NextBio

970331.

Entry information

Entry name

ADA2_YEAST

Accession

Primary (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:	May 1, 2013
This is version 135 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program