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P38129

- TAF5_YEAST

UniProt

P38129 - TAF5_YEAST

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Protein

Transcription initiation factor TFIID subunit 5

Gene

TAF5

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 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.6 Publications

GO - Molecular functioni

  1. chromatin binding Source: SGD
  2. identical protein binding Source: IntAct
  3. protein complex scaffold Source: SGD
  4. ubiquitin binding Source: SGD

GO - Biological processi

  1. chromatin modification Source: SGD
  2. histone acetylation Source: SGD
  3. regulation of transcription, DNA-templated Source: UniProtKB-KW
  4. RNA polymerase II transcriptional preinitiation complex assembly Source: SGD
  5. transcription from RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-29139-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription initiation factor TFIID subunit 5
Alternative name(s):
TAFII-90
TBP-associated factor 5
TBP-associated factor 90 kDa
Gene namesi
Name:TAF5
Synonyms:TAF90
Ordered Locus Names:YBR198C
ORF Names:YBR1410
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome II

Organism-specific databases

CYGDiYBR198c.
SGDiS000000402. TAF5.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. SAGA complex Source: SGD
  2. SLIK (SAGA-like) complex Source: SGD
  3. transcription factor TFIID complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 798798Transcription initiation factor TFIID subunit 5PRO_0000051260Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei299 – 2991Phosphoserine1 Publication
Modified residuei411 – 4111Phosphoserine1 Publication
Modified residuei415 – 4151Phosphoserine1 Publication
Modified residuei787 – 7871Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38129.
PaxDbiP38129.
PeptideAtlasiP38129.

Expressioni

Gene expression databases

GenevestigatoriP38129.

Interactioni

Subunit structurei

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 TAF9.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself9EBI-18868,EBI-18868
HFI1Q1206015EBI-18868,EBI-8287
TAF2P2325510EBI-18868,EBI-18862
TAF4P5010512EBI-18868,EBI-11231
TAF6P5304013EBI-18868,EBI-18876

Protein-protein interaction databases

BioGridi32895. 305 interactions.
DIPiDIP-740N.
IntActiP38129. 197 interactions.
MINTiMINT-475651.
STRINGi4932.YBR198C.

Structurei

Secondary structure

1
798
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi152 – 16413
Turni168 – 1703
Helixi171 – 19222
Helixi194 – 20411
Helixi205 – 2084
Helixi209 – 2179
Turni218 – 2214
Helixi225 – 2306
Helixi232 – 2387
Beta strandi242 – 2465
Helixi248 – 26013
Helixi262 – 2643
Helixi266 – 27611
Beta strandi277 – 2815

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J49X-ray2.30A147-290[»]
ProteinModelPortaliP38129.
SMRiP38129. Positions 149-282, 422-794.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38129.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 8833LisHPROSITE-ProRule annotationAdd
BLAST
Repeati464 – 50340WD 1Add
BLAST
Repeati523 – 56240WD 2Add
BLAST
Repeati565 – 60440WD 3Add
BLAST
Repeati607 – 64640WD 4Add
BLAST
Repeati649 – 68840WD 5Add
BLAST
Repeati692 – 73140WD 6Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili329 – 34921Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3 – 4846Gln-richAdd
BLAST

Sequence similaritiesi

Belongs to the WD repeat TAF5 family.Curated
Contains 1 LisH domain.PROSITE-ProRule annotation
Contains 6 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00760000119293.
HOGENOMiHOG000212424.
InParanoidiP38129.
KOiK03130.
OMAiRFRIEGR.
OrthoDBiEOG7KQ29H.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR006594. LisH_dimerisation.
IPR013720. LisH_dimerisation_subgr.
IPR007582. TFIID-su_WD40-assoc_reg.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF08513. LisH. 1 hit.
PF04494. TFIID_90kDa. 1 hit.
PF00400. WD40. 6 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00667. LisH. 1 hit.
SM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 2 hits.
PROSITEiPS50896. LISH. 1 hit.
PS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38129 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSQKQSTNQN QNGTHQPQPV KNQRTNNAAG ANSGQQPQQQ SQGQSQQQGR
60 70 80 90 100
SNGPFSASDL NRIVLEYLNK KGYHRTEAML RAESGRTLTP QNKQSPANTK
110 120 130 140 150
TGKFPEQSSI PPNPGKTAKP ISNPTNLSSK RDAEGGIVSS GRLEGLNAPE
160 170 180 190 200
NYIRAYSMLK NWVDSSLEIY KPELSYIMYP IFIYLFLNLV AKNPVYARRF
210 220 230 240 250
FDRFSPDFKD FHGSEINRLF SVNSIDHIKE NEVASAFQSH KYRITMSKTT
260 270 280 290 300
LNLLLYFLNE NESIGGSLII SVINQHLDPN IVESVTAREK LADGIKVLSD
310 320 330 340 350
SENGNGKQNL EMNSVPVKLG PFPKDEEFVK EIETELKIKD DQEKQLNQQT
360 370 380 390 400
AGDNYSGANN RTLLQEYKAM NNEKFKDNTG DDDKDKIKDK IAKDEEKKES
410 420 430 440 450
ELKVDGEKKD SNLSSPARDI LPLPPKTALD LKLEIQKVKE SRDAIKLDNL
460 470 480 490 500
QLALPSVCMY TFQNTNKDMS CLDFSDDCRI AAAGFQDSYI KIWSLDGSSL
510 520 530 540 550
NNPNIALNNN DKDEDPTCKT LVGHSGTVYS TSFSPDNKYL LSGSEDKTVR
560 570 580 590 600
LWSMDTHTAL VSYKGHNHPV WDVSFSPLGH YFATASHDQT ARLWSCDHIY
610 620 630 640 650
PLRIFAGHLN DVDCVSFHPN GCYVFTGSSD KTCRMWDVST GDSVRLFLGH
660 670 680 690 700
TAPVISIAVC PDGRWLSTGS EDGIINVWDI GTGKRLKQMR GHGKNAIYSL
710 720 730 740 750
SYSKEGNVLI SGGADHTVRV WDLKKATTEP SAEPDEPFIG YLGDVTASIN
760 770 780 790
QDIKEYGRRR TVIPTSDLVA SFYTKKTPVF KVKFSRSNLA LAGGAFRP
Length:798
Mass (Da):88,968
Last modified:October 1, 1994 - v1
Checksum:iB42315B8C752D0B6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z21487 Genomic DNA. Translation: CAA79685.1.
Z36067 Genomic DNA. Translation: CAA85160.1.
AY692890 Genomic DNA. Translation: AAT92909.1.
BK006936 Genomic DNA. Translation: DAA07314.1.
PIRiS34023.
RefSeqiNP_009757.1. NM_001178546.1.

Genome annotation databases

EnsemblFungiiYBR198C; YBR198C; YBR198C.
GeneIDi852497.
KEGGisce:YBR198C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z21487 Genomic DNA. Translation: CAA79685.1 .
Z36067 Genomic DNA. Translation: CAA85160.1 .
AY692890 Genomic DNA. Translation: AAT92909.1 .
BK006936 Genomic DNA. Translation: DAA07314.1 .
PIRi S34023.
RefSeqi NP_009757.1. NM_001178546.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2J49 X-ray 2.30 A 147-290 [» ]
ProteinModelPortali P38129.
SMRi P38129. Positions 149-282, 422-794.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32895. 305 interactions.
DIPi DIP-740N.
IntActi P38129. 197 interactions.
MINTi MINT-475651.
STRINGi 4932.YBR198C.

Proteomic databases

MaxQBi P38129.
PaxDbi P38129.
PeptideAtlasi P38129.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YBR198C ; YBR198C ; YBR198C .
GeneIDi 852497.
KEGGi sce:YBR198C.

Organism-specific databases

CYGDi YBR198c.
SGDi S000000402. TAF5.

Phylogenomic databases

eggNOGi COG2319.
GeneTreei ENSGT00760000119293.
HOGENOMi HOG000212424.
InParanoidi P38129.
KOi K03130.
OMAi RFRIEGR.
OrthoDBi EOG7KQ29H.

Enzyme and pathway databases

BioCyci YEAST:G3O-29139-MONOMER.

Miscellaneous databases

EvolutionaryTracei P38129.
NextBioi 971495.
PROi P38129.

Gene expression databases

Genevestigatori P38129.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
InterProi IPR020472. G-protein_beta_WD-40_rep.
IPR006594. LisH_dimerisation.
IPR013720. LisH_dimerisation_subgr.
IPR007582. TFIID-su_WD40-assoc_reg.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view ]
Pfami PF08513. LisH. 1 hit.
PF04494. TFIID_90kDa. 1 hit.
PF00400. WD40. 6 hits.
[Graphical view ]
PRINTSi PR00320. GPROTEINBRPT.
SMARTi SM00667. LisH. 1 hit.
SM00320. WD40. 6 hits.
[Graphical view ]
SUPFAMi SSF50978. SSF50978. 2 hits.
PROSITEi PS50896. LISH. 1 hit.
PS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence analysis of an 11.7 kb fragment of yeast chromosome II including BEM1, a new gene of the WD-40 repeat family and a new member of the KRE2/MNT1 family."
    Mallet L., Bussereau F., Jacquet M.
    Yeast 10:819-831(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Yeast TAFIIS in a multisubunit complex required for activated transcription."
    Reese J.C., Apone L., Walker S.S., Griffin L.A., Green M.R.
    Nature 371:523-527(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 726-747, CHARACTERIZATION.
    Strain: Y57.
  6. "Identification and characterization of a TFIID-like multiprotein complex from Saccharomyces cerevisiae."
    Poon D., Bai Y., Campbell A.M., Bjorklund S., Kim Y.-J., Zhou S., Kornberg R.D., Weil P.A.
    Proc. Natl. Acad. Sci. U.S.A. 92:8224-8228(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-63 AND 726-752, CHARACTERIZATION.
    Strain: ATCC 76621 / YPH252.
  7. "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 IN SAGA COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  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.
  9. "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 TFIID COMPLEX.
  10. "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 IN SAGA COMPLEX.
  11. "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.
  12. "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.
  13. Cited for: 3D-STRUCTURE, ELECTRON MICROSCOPY OF TFIID.
  14. "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.
  15. "Multi-protein complexes in eukaryotic gene transcription."
    Martinez E.
    Plant Mol. Biol. 50:925-947(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  17. "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.
  18. "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-299; SER-411 AND SER-787, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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.

Entry informationi

Entry nameiTAF5_YEAST
AccessioniPrimary (citable) accession number: P38129
Secondary accession number(s): D6VQJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: October 29, 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 14834 (+/-203) molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

External Data

Dasty 3