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Protein

SAGA-associated factor 73

Gene

SGF73

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).

GO - Molecular functioni

  1. enzyme activator activity Source: SGD
  2. structural molecule activity Source: SGD

GO - Biological processi

  1. chromatin modification Source: SGD
  2. histone acetylation Source: SGD
  3. histone deubiquitination Source: SGD
  4. mRNA export from nucleus Source: SGD
  5. positive regulation of catalytic activity Source: GOC
  6. positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: SGD
  7. protein complex assembly Source: SGD
  8. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-30571-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
SAGA-associated factor 73
Alternative name(s):
73 kDa SAGA-associated factor
SAGA histone acetyltransferase complex 73 kDa subunit
Gene namesi
Name:SGF73
Ordered Locus Names:YGL066W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGL066w.
SGDiS000003034. SGF73.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. cytosol Source: SGD
  2. DUBm complex Source: SGD
  3. nucleus Source: SGD
  4. SAGA complex Source: SGD
  5. SLIK (SAGA-like) complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 657657SAGA-associated factor 73PRO_0000202764Add
BLAST

Proteomic databases

MaxQBiP53165.
PaxDbiP53165.
PeptideAtlasiP53165.

Expressioni

Gene expression databases

GenevestigatoriP53165.

Interactioni

Subunit structurei

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SPT20P508755EBI-23812,EBI-17751

Protein-protein interaction databases

BioGridi33181. 356 interactions.
DIPiDIP-5211N.
IntActiP53165. 92 interactions.
MINTiMINT-548904.
STRINGi4932.YGL066W.

Structurei

Secondary structure

1
657
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 115Combined sources
Helixi13 – 186Combined sources
Turni19 – 224Combined sources
Beta strandi28 – 303Combined sources
Helixi32 – 354Combined sources
Helixi36 – 416Combined sources
Beta strandi47 – 493Combined sources
Helixi51 – 577Combined sources
Beta strandi70 – 723Combined sources
Beta strandi76 – 783Combined sources
Turni79 – 813Combined sources
Beta strandi84 – 863Combined sources
Helixi87 – 893Combined sources
Turni90 – 923Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP53165.
SMRiP53165. Positions 5-96.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53165.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini220 – 28667SCA7PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi141 – 15010Poly-Asp
Compositional biasi153 – 16210Poly-Asp
Compositional biasi466 – 47611Poly-GlnAdd
BLAST
Compositional biasi517 – 52610Poly-Gln

Sequence similaritiesi

Belongs to the ataxin-7 family.Curated
Contains 1 SCA7 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG285209.
HOGENOMiHOG000142039.
InParanoidiP53165.
KOiK11365.
OMAiMREMFAS.
OrthoDBiEOG7NSBB2.

Family and domain databases

InterProiIPR013243. SCA7_dom.
[Graphical view]
PfamiPF08313. SCA7. 1 hit.
[Graphical view]
PROSITEiPS51505. SCA7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53165-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRSGDAEIKG IKPKVIEEYS LSQGSGPSND SWKSLMSSAK DTPLQYDHMN
60 70 80 90 100
RESLKKYFNP NAQLIEDPLD KPIQYRVCEK CGKPLALTAI VDHLENHCAG
110 120 130 140 150
ASGKSSTDPR DESTRETIRN GVESTGRNNN DDDNSNDNNN DDDDDDDNDD
160 170 180 190 200
NEDDDDADDD DDNSNGANYK KNDSSFNPLK RSTSMESANT PNMDTKRSKT
210 220 230 240 250
GTPQTFSSSI KKQKKVKQRN PTEKHLIDFN KQCGVELPEG GYCARSLTCK
260 270 280 290 300
SHSMGAKRAV SGRSKPYDVL LADYHREHQT KIGAAAEKRA KQQELQKLQK
310 320 330 340 350
QIQKEQKKHT QQQKQGQRSK QRNVNGGKSA KNGGKSTVHN GNNINEIGHV
360 370 380 390 400
NLTPEEETTQ VLNGVSRSFP LPLESTVLSS VRYRTKYFRM REMFASSFSV
410 420 430 440 450
KPGYTSPGYG AIHSRVGCLD LDRTTDYKFR VRTPQPINHL TNQNLNPKQI
460 470 480 490 500
QRLQQQRALQ AQLLSQQQQQ QQQQQQHHSP QAQAQASTQQ PTQGMVPNHF
510 520 530 540 550
PGGATNSSFN ANVSSKQIQQ QQQQQQHKSQ DTGLTPLEIQ SQQQKLRQQQ
560 570 580 590 600
LQQQKFEAAA SYLANATKLM QESNQDSHLS GTHNNNSSKN GNNNLMTMKA
610 620 630 640 650
SISSPNTSVN SIQSPPSVNS VNGSGQGVST GINVSGNNGR IEVGIGNSVN

PYNGRIN
Length:657
Mass (Da):72,878
Last modified:October 1, 1996 - v1
Checksum:i4618E2E47824321D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72588 Genomic DNA. Translation: CAA96770.1.
Z72587 Genomic DNA. Translation: CAA96769.1.
BK006941 Genomic DNA. Translation: DAA08036.1.
PIRiS64073.
RefSeqiNP_011449.1. NM_001180931.1.

Genome annotation databases

EnsemblFungiiYGL066W; YGL066W; YGL066W.
GeneIDi852814.
KEGGisce:YGL066W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72588 Genomic DNA. Translation: CAA96770.1.
Z72587 Genomic DNA. Translation: CAA96769.1.
BK006941 Genomic DNA. Translation: DAA08036.1.
PIRiS64073.
RefSeqiNP_011449.1. NM_001180931.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP53165.
SMRiP53165. Positions 5-96.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33181. 356 interactions.
DIPiDIP-5211N.
IntActiP53165. 92 interactions.
MINTiMINT-548904.
STRINGi4932.YGL066W.

Proteomic databases

MaxQBiP53165.
PaxDbiP53165.
PeptideAtlasiP53165.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL066W; YGL066W; YGL066W.
GeneIDi852814.
KEGGisce:YGL066W.

Organism-specific databases

CYGDiYGL066w.
SGDiS000003034. SGF73.

Phylogenomic databases

eggNOGiNOG285209.
HOGENOMiHOG000142039.
InParanoidiP53165.
KOiK11365.
OMAiMREMFAS.
OrthoDBiEOG7NSBB2.

Enzyme and pathway databases

BioCyciYEAST:G3O-30571-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP53165.
NextBioi972348.

Gene expression databases

GenevestigatoriP53165.

Family and domain databases

InterProiIPR013243. SCA7_dom.
[Graphical view]
PfamiPF08313. SCA7. 1 hit.
[Graphical view]
PROSITEiPS51505. SCA7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiSGF73_YEAST
AccessioniPrimary (citable) accession number: P53165
Secondary accession number(s): D6VU75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 4, 2015
This is version 123 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 486 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, 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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.