Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

SAGA-associated factor 29

Gene

SGF29

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) complexes SAGA and SLIK. 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). 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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei205 – 2051Histone H3K4me3
Binding sitei212 – 2121Histone H3K4me3

GO - Molecular functioni

  • methylated histone binding Source: SGD
  • transcription factor activity, RNA polymerase II transcription factor recruiting Source: SGD

GO - Biological processi

  • cellular protein complex localization Source: SGD
  • cellular protein localization Source: SGD
  • heterochromatin organization involved in chromatin silencing Source: SGD
  • histone H3-K14 acetylation Source: SGD
  • histone H3-K18 acetylation Source: SGD
  • histone H3-K9 acetylation Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-29279-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
SAGA-associated factor 29
Alternative name(s):
29 kDa SAGA-associated factor
SAGA histone acetyltransferase complex 29 kDa subunit
Gene namesi
Name:SGF29
Ordered Locus Names:YCL010C
ORF Names:YCL10C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:YCL010C.
SGDiS000000516. SGF29.

Subcellular locationi

GO - Cellular componenti

  • Ada2/Gcn5/Ada3 transcription activator complex Source: SGD
  • SAGA complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi163 – 1631D → A: Reduces histone H3 acetylation. 1 Publication
Mutagenesisi165 – 1651E → A: Reduces histone H3 acetylation. 1 Publication
Mutagenesisi205 – 2051Y → A: Reduces histone H3 acetylation. 1 Publication
Mutagenesisi210 – 2101T → A: Reduces histone H3 acetylation. 1 Publication
Mutagenesisi212 – 2121Y → A: Reduces histone H3 acetylation. 1 Publication
Mutagenesisi229 – 2291F → A: Reduces histone H3 acetylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 259259SAGA-associated factor 29PRO_0000202539Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei139 – 1391PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP25554.
PeptideAtlasiP25554.

PTM databases

iPTMnetiP25554.

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. Interacts with dimethylated and trimethylated 'Lys-4' of histone H3 (H3K4me2 and H3K4me3), with a preference for the trimethylated form (H3K4me3). 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 TAF9.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HFI1Q120609EBI-21678,EBI-8287
HIST1H3FP6843111EBI-21678,EBI-79722From a different organism.
NGG1P324945EBI-21678,EBI-2192

GO - Molecular functioni

  • methylated histone binding Source: SGD

Protein-protein interaction databases

BioGridi30971. 267 interactions.
DIPiDIP-4871N.
IntActiP25554. 93 interactions.
MINTiMINT-490735.

Structurei

Secondary structure

1
259
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi118 – 1203Combined sources
Beta strandi130 – 1334Combined sources
Turni140 – 1423Combined sources
Beta strandi144 – 15310Combined sources
Turni154 – 1574Combined sources
Beta strandi158 – 1636Combined sources
Beta strandi174 – 1785Combined sources
Helixi180 – 1823Combined sources
Beta strandi183 – 1864Combined sources
Beta strandi200 – 2045Combined sources
Beta strandi209 – 21911Combined sources
Beta strandi225 – 2295Combined sources
Beta strandi232 – 2343Combined sources
Beta strandi239 – 2413Combined sources
Helixi243 – 2453Combined sources
Beta strandi246 – 2483Combined sources
Helixi250 – 2534Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MP1X-ray2.60A111-259[»]
3MP6X-ray1.48A111-259[»]
3MP8X-ray1.92A111-259[»]
ProteinModelPortaliP25554.
SMRiP25554. Positions 111-250.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25554.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini121 – 255135SGF29 C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni163 – 1653Histone H3K4me3 N-terminus binding
Regioni207 – 2104Histone H3K4me3 N-terminus binding
Regioni229 – 2324Histone H3K4me3 binding

Domaini

The SGF29 tudor-like domain mediates binding to methylated 'Lys-4' of histone H3 (H3K4me).PROSITE-ProRule annotation1 Publication

Sequence similaritiesi

Belongs to the SGF29 family.PROSITE-ProRule annotation
Contains 1 SGF29 C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000248873.
InParanoidiP25554.
KOiK11364.
OMAiEWIQCEV.
OrthoDBiEOG7W41PG.

Family and domain databases

InterProiIPR010750. SGF29_tudor-like_dom.
[Graphical view]
PfamiPF07039. DUF1325. 1 hit.
[Graphical view]
PROSITEiPS51518. SGF29_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25554-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDGYWDVVVS SLQDIYNANE VIPFDDELQT KKLNFLNMSK DQLQLHLNTF
60 70 80 90 100
QEHMENVNRV HRILDNVRSN LSLMLNQSRE EKSEENTEDA EEGEGTRMAL
110 120 130 140 150
SQGKKAVGKV GRSYWTSEYN PNAPILVGSE VAYKPRRGSA DGEWIQCEVL
160 170 180 190 200
KVVADGTRFE VRDPEPDELG NSGKVYKCNR KELLLIPPGF PTKNYPPGTK
210 220 230 240 250
VLARYPETTT FYPAIVIGTK RDGTCRLRFD GEEEVDKETE VTRRLVLPSP

TALANLARK
Length:259
Mass (Da):29,381
Last modified:May 30, 2000 - v2
Checksum:i4DD51E36BB01C073
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAA42349.1.
BK006937 Genomic DNA. Translation: DAA07471.1.
PIRiS74287.
RefSeqiNP_009917.1. NM_001178659.1.

Genome annotation databases

EnsemblFungiiCAA42349; CAA42349; CAA42349.
YCL010C; YCL010C; YCL010C.
GeneIDi850347.
KEGGisce:YCL010C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAA42349.1.
BK006937 Genomic DNA. Translation: DAA07471.1.
PIRiS74287.
RefSeqiNP_009917.1. NM_001178659.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MP1X-ray2.60A111-259[»]
3MP6X-ray1.48A111-259[»]
3MP8X-ray1.92A111-259[»]
ProteinModelPortaliP25554.
SMRiP25554. Positions 111-250.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi30971. 267 interactions.
DIPiDIP-4871N.
IntActiP25554. 93 interactions.
MINTiMINT-490735.

PTM databases

iPTMnetiP25554.

Proteomic databases

MaxQBiP25554.
PeptideAtlasiP25554.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAA42349; CAA42349; CAA42349.
YCL010C; YCL010C; YCL010C.
GeneIDi850347.
KEGGisce:YCL010C.

Organism-specific databases

EuPathDBiFungiDB:YCL010C.
SGDiS000000516. SGF29.

Phylogenomic databases

HOGENOMiHOG000248873.
InParanoidiP25554.
KOiK11364.
OMAiEWIQCEV.
OrthoDBiEOG7W41PG.

Enzyme and pathway databases

BioCyciYEAST:G3O-29279-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP25554.
NextBioi965803.
PROiP25554.

Family and domain databases

InterProiIPR010750. SGF29_tudor-like_dom.
[Graphical view]
PfamiPF07039. DUF1325. 1 hit.
[Graphical view]
PROSITEiPS51518. SGF29_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete DNA sequence of yeast chromosome III."
    Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
    , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
    Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Gromadka R.
    Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "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.
  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. "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-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  8. "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.
  9. "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-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "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-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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.
  13. "Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation."
    Bian C., Xu C., Ruan J., Lee K.K., Burke T.L., Tempel W., Barsyte D., Li J., Wu M., Zhou B.O., Fleharty B.E., Paulson A., Allali-Hassani A., Zhou J.Q., Mer G., Grant P.A., Workman J.L., Zang J., Min J.
    EMBO J. 30:2829-2842(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 113-259 IN COMPLEX WITH H3K4ME3 PEPTIDE, INTERACTION WITH H3K4ME2 AND H3K4ME3, FUNCTION, DOMAIN, MUTAGENESIS OF ASP-163; GLU-165; TYR-205; THR-210; TYR-212 AND PHE-229.

Entry informationi

Entry nameiSGF29_YEAST
AccessioniPrimary (citable) accession number: P25554
Secondary accession number(s): D6VR02, P87008
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 30, 2000
Last modified: May 11, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1750 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 III
    Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

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 one 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.