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P53165 (SGF73_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. 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:
SAGA-associated factor 73
Alternative name(s):
73 kDa SAGA-associated factor
SAGA histone acetyltransferase complex 73 kDa subunit
Gene names
Name:SGF73
Ordered Locus Names:YGL066W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length657 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as component of the transcription regulatory histone acetylation (HAT) complex SAGA. 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).

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. Ref.5

Subcellular location

Nucleus Probable.

Miscellaneous

Present with 486 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the ataxin-7 family.

Contains 1 SCA7 domain.

Ontologies

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

Inferred from mutant phenotype PubMed 15932941PubMed 17090597. Source: SGD

histone acetylation

Inferred from mutant phenotype PubMed 15932941. Source: SGD

histone deubiquitination

Inferred from mutant phenotype PubMed 19226466. Source: SGD

mRNA export from nucleus

Inferred from mutant phenotype PubMed 18488019. Source: SGD

positive regulation of RNA polymerase II transcriptional preinitiation complex assembly

Inferred from mutant phenotype PubMed 17090597. Source: SGD

positive regulation of catalytic activity

Inferred from direct assay PubMed 18488019. Source: GOC

protein complex assembly

Inferred from mutant phenotype PubMed 19226466. Source: SGD

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentDUBm complex

Inferred from direct assay PubMed 20395473. Source: SGD

SAGA complex

Inferred from direct assay Ref.5PubMed 17090597. Source: SGD

SLIK (SAGA-like) complex

Inferred from physical interaction PubMed 15932941. Source: SGD

cytosol

Inferred from direct assay PubMed 22932476. Source: SGD

nucleus

Inferred from direct assay PubMed 22932476. Source: SGD

   Molecular_functionenzyme activator activity

Inferred from direct assay PubMed 18488019. Source: SGD

protein binding

Inferred from physical interaction PubMed 16429126PubMed 20634802PubMed 21734642. Source: IntAct

structural molecule activity

Inferred from mutant phenotype PubMed 15932941. Source: SGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SPT20P508755EBI-23812,EBI-17751

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 657657SAGA-associated factor 73
PRO_0000202764

Regions

Domain220 – 28667SCA7
Compositional bias141 – 15010Poly-Asp
Compositional bias153 – 16210Poly-Asp
Compositional bias466 – 47611Poly-Gln
Compositional bias517 – 52610Poly-Gln

Secondary structure

........................ 657
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P53165 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 4618E2E47824321D

FASTA65772,878
        10         20         30         40         50         60 
MRSGDAEIKG IKPKVIEEYS LSQGSGPSND SWKSLMSSAK DTPLQYDHMN RESLKKYFNP 

        70         80         90        100        110        120 
NAQLIEDPLD KPIQYRVCEK CGKPLALTAI VDHLENHCAG ASGKSSTDPR DESTRETIRN 

       130        140        150        160        170        180 
GVESTGRNNN DDDNSNDNNN DDDDDDDNDD NEDDDDADDD DDNSNGANYK KNDSSFNPLK 

       190        200        210        220        230        240 
RSTSMESANT PNMDTKRSKT GTPQTFSSSI KKQKKVKQRN PTEKHLIDFN KQCGVELPEG 

       250        260        270        280        290        300 
GYCARSLTCK SHSMGAKRAV SGRSKPYDVL LADYHREHQT KIGAAAEKRA KQQELQKLQK 

       310        320        330        340        350        360 
QIQKEQKKHT QQQKQGQRSK QRNVNGGKSA KNGGKSTVHN GNNINEIGHV NLTPEEETTQ 

       370        380        390        400        410        420 
VLNGVSRSFP LPLESTVLSS VRYRTKYFRM REMFASSFSV KPGYTSPGYG AIHSRVGCLD 

       430        440        450        460        470        480 
LDRTTDYKFR VRTPQPINHL TNQNLNPKQI QRLQQQRALQ AQLLSQQQQQ QQQQQQHHSP 

       490        500        510        520        530        540 
QAQAQASTQQ PTQGMVPNHF PGGATNSSFN ANVSSKQIQQ QQQQQQHKSQ DTGLTPLEIQ 

       550        560        570        580        590        600 
SQQQKLRQQQ LQQQKFEAAA SYLANATKLM QESNQDSHLS GTHNNNSSKN GNNNLMTMKA 

       610        620        630        640        650 
SISSPNTSVN SIQSPPSVNS VNGSGQGVST GINVSGNNGR IEVGIGNSVN PYNGRIN 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII."
Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.
Yeast 13:1077-1090(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The characterization of two new clusters of duplicated genes suggests a 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes."
Feuermann M., de Montigny J., Potier S., Souciet J.-L.
Yeast 13:861-869(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 115-657.
Strain: ATCC 204508 / S288c.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"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.
[5]"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: IDENTIFICATION IN THE SAGA COMPLEX.
[6]"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].
[7]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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
Z72588 Genomic DNA. Translation: CAA96770.1.
Z72587 Genomic DNA. Translation: CAA96769.1.
BK006941 Genomic DNA. Translation: DAA08036.1.
PIRS64073.
RefSeqNP_011449.1. NM_001180931.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LO3NMR-A59-102[»]
3M99X-ray2.70D1-104[»]
3MHHX-ray2.45E1-96[»]
3MHSX-ray1.89E1-96[»]
4FIPX-ray2.69D/H1-96[»]
4FJCX-ray2.83D/H1-96[»]
4FK5X-ray2.03E1-96[»]
ProteinModelPortalP53165.
SMRP53165. Positions 5-96.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33181. 353 interactions.
DIPDIP-5211N.
IntActP53165. 92 interactions.
MINTMINT-548904.
STRING4932.YGL066W.

Proteomic databases

MaxQBP53165.
PaxDbP53165.
PeptideAtlasP53165.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL066W; YGL066W; YGL066W.
GeneID852814.
KEGGsce:YGL066W.

Organism-specific databases

CYGDYGL066w.
SGDS000003034. SGF73.

Phylogenomic databases

eggNOGNOG285209.
HOGENOMHOG000142039.
KOK11365.
OMANINEIGH.
OrthoDBEOG7NSBB2.

Enzyme and pathway databases

BioCycYEAST:G3O-30571-MONOMER.

Gene expression databases

GenevestigatorP53165.

Family and domain databases

InterProIPR013243. SCA7_dom.
[Graphical view]
PfamPF08313. SCA7. 1 hit.
[Graphical view]
PROSITEPS51505. SCA7. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP53165.
NextBio972348.

Entry information

Entry nameSGF73_YEAST
AccessionPrimary (citable) accession number: P53165
Secondary accession number(s): D6VU75
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 118 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 VII

Yeast (Saccharomyces cerevisiae) chromosome VII: 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