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Q03761 (TAF12_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:
Transcription initiation factor TFIID subunit 12
Alternative name(s):
TAFII-61
Short name=TAFII61
TAFII-68
Short name=TAFII68
TBP-associated factor 12
TBP-associated factor 61 kDa
Gene names
Name:TAF12
Synonyms:TAF61, TAF68
Ordered Locus Names:YDR145W
ORF Names:YD8358.02
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length539 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. 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. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.14

Subunit structure

In TFIID, TAF12 heterodimerizes with TAF4, forming ultimately an octamer consisting of a TAF6/TAF9 heterotetramer core flanked by TAF4/TAF12 dimers on either side, similar to the histone H2A/H2B/H3/H4 octamer. The 1.2 MDa TFIID complex is composed of TATA binding protein (TBP) and the 14 TBP-associated factors. One copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three copies of TAF14. Component of the 1.8 MDa SAGA complex, which consists of at least 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. Ref.4 Ref.6 Ref.10 Ref.11 Ref.13 Ref.18

Subcellular location

Nucleus Ref.15.

Miscellaneous

Present with 930 (+/-45) molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the TAF12 family.

Contains 1 histone-fold domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself4EBI-35097,EBI-35097
BDF1P358172EBI-35097,EBI-3493
TAF10Q1203011EBI-35097,EBI-18889
TAF4P501058EBI-35097,EBI-11231

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 539539Transcription initiation factor TFIID subunit 12
PRO_0000118909

Regions

Domain413 – 49078Histone-fold
Coiled coil153 – 20250 Potential
Coiled coil239 – 28547 Potential
Compositional bias116 – 309194Gln-rich

Amino acid modifications

Modified residue1291Phosphoserine Ref.22
Modified residue2861Phosphoserine Ref.17 Ref.20 Ref.21 Ref.22
Modified residue2871Phosphoserine Ref.22
Modified residue2901Phosphoserine Ref.22
Modified residue2911Phosphothreonine Ref.21
Modified residue3251Phosphoserine Ref.22
Modified residue3421Phosphoserine Ref.22
Modified residue3521Phosphoserine Ref.22
Modified residue4941Phosphoserine Ref.22

Sequences

Sequence LengthMass (Da)Tools
Q03761 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: A8FC84E46F8370D3

FASTA53961,073
        10         20         30         40         50         60 
MSSNPENSGV NANNNTGTGN ADAITGAQQN MVLQPRQLQE MAAKFRTLLT EARNVGETTP 

        70         80         90        100        110        120 
RGKELMFQAA KIKQVYDALT LNRRRQQAAQ AYNNTSNSNS SNPASIPTEN VPNSSQQQQQ 

       130        140        150        160        170        180 
QQQQTRNNSN KFSNMIKQVL TPEENQEYEK LWQNFQVRHT SIKEKETYLK QNIDRLEQEI 

       190        200        210        220        230        240 
NKQTDEGPKQ QLQEKKIELL NDWKVLKIEY TKLFNNYQNS KKTFYVECAR HNPALHKFLQ 

       250        260        270        280        290        300 
ESTQQQRVQQ QRVQQQQQQQ QQQQQQQQQQ QQQQQQRQGQ NQRKISSSNS TEIPSVTGPD 

       310        320        330        340        350        360 
ALKSQQQQQN TITATNNPRG NVNTSQTEQS KAKVTNVNAT ASMLNNISSS KSAIFKQTEP 

       370        380        390        400        410        420 
AIPISENIST KTPAPVAYRS NRPTITGGSA MNASALNTPA TTKLPPYEMD TQRVMSKRKL 

       430        440        450        460        470        480 
RELVKTVGID EGDGETVIDG DVEELLLDLA DDFVTNVTAF SCRLAKHRKS DNLEARDIQL 

       490        500        510        520        530 
HLERNWNIRI PGYSADEIRS TRKWNPSQNY NQKLQSITSD KVAAAKNNGN NVASLNTKK

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family."
Birck C., Poch O., Romier C., Ruff M., Mengus G., Lavigne A.C., Davidson I., Moras D.
Cell 94:239-249(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TAF-TAF INTERACTION THROUGH HISTONE-FOLD DOMAIN.
[4]"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: FUNCTION, IDENTIFICATION IN THE SAGA COMPLEX, MASS SPECTROMETRY.
[5]"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.
[6]"Identification of two novel TAF subunits of the yeast Saccharomyces cerevisiae TFIID complex."
Sanders S.L., Weil P.A.
J. Biol. Chem. 275:13895-13900(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE TFIID COMPLEX.
[7]"Histone folds mediate selective heterodimerization of yeast TAF(II)25 with TFIID components yTAF(II)47 and yTAF(II)65 and with SAGA component ySPT7."
Gangloff Y.G., Sanders S.L., Romier C., Kirschner D.B., Weil P.A., Tora L., Davidson I.
Mol. Cell. Biol. 21:1841-1853(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION IN TFIID AND SAGA.
[8]"The histone fold is a key structural motif of transcription factor TFIID."
Gangloff Y.G., Romier C., Thuault S., Werten S., Davidson I.
Trends Biochem. Sci. 26:250-257(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, HISTONE-FOLD DOMAIN CHARACTERIZATION.
[9]"A histone fold TAF octamer within the yeast TFIID transcriptional coactivator."
Selleck W., Howley R., Fang Q., Podolny V., Fried M.G., Buratowski S., Tan S.
Nat. Struct. Biol. 8:695-700(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TAF OCTAMER FORMATION.
[10]"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.
[11]"Proteomics of the eukaryotic transcription machinery: identification of proteins associated with components of yeast TFIID by multidimensional mass spectrometry."
Sanders S.L., Jennings J., Canutescu A., Link A.J., Weil P.A.
Mol. Cell. Biol. 22:4723-4738(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE SAGA COMPLEX.
[12]"Molecular characterization of Saccharomyces cerevisiae TFIID."
Sanders S.L., Garbett K.A., Weil P.A.
Mol. Cell. Biol. 22:6000-6013(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TFIID STOICHIOMETRY.
[13]"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.
[14]"Multi-protein complexes in eukaryotic gene transcription."
Martinez E.
Plant Mol. Biol. 50:925-947(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[16]"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].
[17]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286, MASS SPECTROMETRY.
Strain: YAL6B.
[18]"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.
[19]"Mapping histone fold TAFs within yeast TFIID."
Leurent C., Sanders S.L., Ruhlmann C., Mallouh V., Weil P.A., Kirschner D.B., Tora L., Schultz P.
EMBO J. 21:3424-3433(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE, ELECTRON MICROSCOPY OF TFIID.
[20]"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-286, MASS SPECTROMETRY.
Strain: ADR376.
[21]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286 AND THR-291, MASS SPECTROMETRY.
[22]"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-129; SER-286; SER-287; SER-290; SER-325; SER-342; SER-352 AND SER-494, MASS SPECTROMETRY.
[23]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z50046 Genomic DNA. Translation: CAA90368.1.
BK006938 Genomic DNA. Translation: DAA11988.1.
PIRS57972.
RefSeqNP_010429.1. NM_001180452.1.

3D structure databases

ProteinModelPortalQ03761.
SMRQ03761. Positions 414-490.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1302N.
IntActQ03761. 117 interactions.
MINTMINT-408447.
STRING4932.YDR145W.

Proteomic databases

PaxDbQ03761.
PeptideAtlasQ03761.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR145W; YDR145W; YDR145W.
GeneID851723.
KEGGsce:YDR145W.

Organism-specific databases

CYGDYDR145w.
SGDS000002552. TAF12.

Phylogenomic databases

eggNOGCOG5624.
GeneTreeENSGT00390000002144.
HOGENOMHOG000141888.
KOK03126.
OMAYRSNRPT.
OrthoDBEOG45TGXB.

Gene expression databases

GenevestigatorQ03761.
GermOnlineYDR145W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR003228. TFIID_sub.
[Graphical view]
PfamPF03847. TFIID_20kDa. 1 hit.
[Graphical view]
ProDomPD012998. PD012998. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF47113. Histone-fold. 1 hit.
ProtoNetSearch...

Other

NextBio969433.

Entry information

Entry nameTAF12_YEAST
AccessionPrimary (citable) accession number: Q03761
Secondary accession number(s): D6VSC8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome IV

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents