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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

Chromatin reader component of the transcription regulatory histone acetylation (HAT) complexes SAGA and SLIK (PubMed:10026213, PubMed:15647753, PubMed:21685874, PubMed:24307402). In the SAGA complex, SGF29 specifically recognizes and binds methylated 'Lys-4' of histone H3 (H3K4me), with a preference for trimethylated form (H3K4me3) (PubMed:21685874). SGF29 is also required for heterochromatin boundary formation function (PubMed:24307402). 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 (PubMed:10026213). 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) (PubMed:10026213). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs) (PubMed:10026213). SLIK is proposed to have partly overlapping functions with SAGA (PubMed:15647753). It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus (PubMed:15647753).4 Publications

Miscellaneous

Present with 1750 molecules/cell in log phase SD medium.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei205Histone H3K4me31 Publication1
Binding sitei212Histone H3K4me31 Publication1

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

Keywordsi

Molecular functionChromatin regulator
Biological processTranscription, 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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi163D → A: Reduces histone H3 acetylation. 1 Publication1
Mutagenesisi165E → A: Reduces histone H3 acetylation. 1 Publication1
Mutagenesisi205Y → A: Reduces histone H3 acetylation. 1 Publication1
Mutagenesisi210T → A: Reduces histone H3 acetylation. 1 Publication1
Mutagenesisi212Y → A: Reduces histone H3 acetylation. 1 Publication1
Mutagenesisi229F → A: Reduces histone H3 acetylation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002025391 – 259SAGA-associated factor 29Add BLAST259

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei139PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP25554.
PRIDEiP25554.

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

Show more details

GO - Molecular functioni

  • methylated histone binding Source: SGD

Protein-protein interaction databases

BioGridi30971. 546 interactors.
DIPiDIP-4871N.
IntActiP25554. 93 interactors.
MINTiMINT-490735.
STRINGi4932.YCL010C.

Structurei

Secondary structure

1259
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi118 – 120Combined sources3
Beta strandi130 – 133Combined sources4
Turni140 – 142Combined sources3
Beta strandi144 – 153Combined sources10
Turni154 – 157Combined sources4
Beta strandi158 – 163Combined sources6
Beta strandi174 – 178Combined sources5
Helixi180 – 182Combined sources3
Beta strandi183 – 186Combined sources4
Beta strandi200 – 204Combined sources5
Beta strandi209 – 219Combined sources11
Beta strandi225 – 229Combined sources5
Beta strandi232 – 234Combined sources3
Beta strandi239 – 241Combined sources3
Helixi243 – 245Combined sources3
Beta strandi246 – 248Combined sources3
Helixi250 – 253Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP25554.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini121 – 255SGF29 C-terminalPROSITE-ProRule annotationAdd BLAST135

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni163 – 165Histone H3K4me3 N-terminus binding1 Publication3
Regioni207 – 210Histone H3K4me3 N-terminus binding1 Publication4
Regioni229 – 232Histone H3K4me3 binding1 Publication4

Domaini

The SGF29 C-terminal (also named 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

Phylogenomic databases

HOGENOMiHOG000248873.
InParanoidiP25554.
KOiK11364.
OMAiEEWIQCE.
OrthoDBiEOG092C3A9R.

Family and domain databases

InterProiView protein in InterPro
IPR010750. SGF29_tudor-like_dom.
PfamiView protein in Pfam
PF07039. DUF1325. 1 hit.
PROSITEiView protein in PROSITE
PS51518. SGF29_C. 1 hit.

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.

Similar proteinsi

Entry informationi

Entry nameiSGF29_YEAST
AccessioniPrimary (citable) accession number: P25554
Secondary accession number(s): D6VR02, P87008
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 30, 2000
Last modified: November 22, 2017
This is version 146 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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