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P53165

- SGF73_YEAST

UniProt

P53165 - SGF73_YEAST

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Protein

SAGA-associated factor 73

Gene
SGF73, YGL066W
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 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. protein binding Source: IntAct
  3. 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 Inferred

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. 355 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 – 115
Helixi13 – 186
Turni19 – 224
Beta strandi28 – 303
Helixi32 – 354
Helixi36 – 416
Beta strandi47 – 493
Helixi51 – 577
Beta strandi70 – 723
Beta strandi76 – 783
Turni79 – 813
Beta strandi84 – 863
Helixi87 – 893
Turni90 – 923

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP53165.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini220 – 28667SCA7Add
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.
Contains 1 SCA7 domain.

Phylogenomic databases

eggNOGiNOG285209.
HOGENOMiHOG000142039.
KOiK11365.
OMAiNINEIGH.
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

MRSGDAEIKG IKPKVIEEYS LSQGSGPSND SWKSLMSSAK DTPLQYDHMN    50
RESLKKYFNP NAQLIEDPLD KPIQYRVCEK CGKPLALTAI VDHLENHCAG 100
ASGKSSTDPR DESTRETIRN GVESTGRNNN DDDNSNDNNN DDDDDDDNDD 150
NEDDDDADDD DDNSNGANYK KNDSSFNPLK RSTSMESANT PNMDTKRSKT 200
GTPQTFSSSI KKQKKVKQRN PTEKHLIDFN KQCGVELPEG GYCARSLTCK 250
SHSMGAKRAV SGRSKPYDVL LADYHREHQT KIGAAAEKRA KQQELQKLQK 300
QIQKEQKKHT QQQKQGQRSK QRNVNGGKSA KNGGKSTVHN GNNINEIGHV 350
NLTPEEETTQ VLNGVSRSFP LPLESTVLSS VRYRTKYFRM REMFASSFSV 400
KPGYTSPGYG AIHSRVGCLD LDRTTDYKFR VRTPQPINHL TNQNLNPKQI 450
QRLQQQRALQ AQLLSQQQQQ QQQQQQHHSP QAQAQASTQQ PTQGMVPNHF 500
PGGATNSSFN ANVSSKQIQQ QQQQQQHKSQ DTGLTPLEIQ SQQQKLRQQQ 550
LQQQKFEAAA SYLANATKLM QESNQDSHLS GTHNNNSSKN GNNNLMTMKA 600
SISSPNTSVN SIQSPPSVNS VNGSGQGVST GINVSGNNGR IEVGIGNSVN 650
PYNGRIN 657
Length:657
Mass (Da):72,878
Last modified:October 1, 1996 - v1
Checksum:i4618E2E47824321D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
Z72588 Genomic DNA. Translation: CAA96770.1 .
Z72587 Genomic DNA. Translation: CAA96769.1 .
BK006941 Genomic DNA. Translation: DAA08036.1 .
PIRi S64073.
RefSeqi NP_011449.1. NM_001180931.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LO3 NMR - A 59-102 [» ]
3M99 X-ray 2.70 D 1-104 [» ]
3MHH X-ray 2.45 E 1-96 [» ]
3MHS X-ray 1.89 E 1-96 [» ]
4FIP X-ray 2.69 D/H 1-96 [» ]
4FJC X-ray 2.83 D/H 1-96 [» ]
4FK5 X-ray 2.03 E 1-96 [» ]
ProteinModelPortali P53165.
SMRi P53165. Positions 5-96.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33181. 355 interactions.
DIPi DIP-5211N.
IntActi P53165. 92 interactions.
MINTi MINT-548904.
STRINGi 4932.YGL066W.

Proteomic databases

MaxQBi P53165.
PaxDbi P53165.
PeptideAtlasi P53165.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGL066W ; YGL066W ; YGL066W .
GeneIDi 852814.
KEGGi sce:YGL066W.

Organism-specific databases

CYGDi YGL066w.
SGDi S000003034. SGF73.

Phylogenomic databases

eggNOGi NOG285209.
HOGENOMi HOG000142039.
KOi K11365.
OMAi NINEIGH.
OrthoDBi EOG7NSBB2.

Enzyme and pathway databases

BioCyci YEAST:G3O-30571-MONOMER.

Miscellaneous databases

EvolutionaryTracei P53165.
NextBioi 972348.

Gene expression databases

Genevestigatori P53165.

Family and domain databases

InterProi IPR013243. SCA7_dom.
[Graphical view ]
Pfami PF08313. SCA7. 1 hit.
[Graphical view ]
PROSITEi PS51505. SCA7. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 119 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.

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

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