Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
The something about silencing protein, Sas3, is the catalytic subunit of NuA3, a yTAF(II)30-containing HAT complex that interacts with the Spt16 subunit of the yeast CP (Cdc68/Pob3)-FACT complex.
The yeast SAS (something about silencing) protein complex contains a MYST-type putative acetyltransferase and functions with chromatin assembly factor ASF1.
Yeast SAS silencing genes and human genes associated with AML and HIV-1 Tat interactions are homologous with acetyltransferases.
Methylation of histone H3 mediates the association of the NuA3 histone acetyltransferase with chromatin.
Yng1p modulates the activity of Sas3p as a component of the yeast NuA3 Hhistone acetyltransferase complex.
Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs.
A PWWP domain-containing protein targets the NuA3 acetyltransferase complex via histone H3 lysine 36 trimethylation to coordinate transcriptional elongation at coding regions.
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Opposite role of yeast ING family members in p53-dependent transcriptional activation.
Comprehensive analysis of interacting proteins and genome-wide location studies of the Sas3-dependent NuA3 histone acetyltransferase complex.
Molecular insight into interactions between the Taf14, Yng1 and Sas3 subunits of the NuA3 complex.
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Taf14 binds motifs in both Sas3 and Yng1, and disrupting these interactions compromises NuA3-dependent transcription and DNA-repair functions in yeast.
"In vivo assays in yeast demonstrate that the interactions of Taf14 with both Sas3 and Yng1 are required for proper function of the NuA3 complex in gene transcription and DNA repair."
Mechanistic insights into histone recognition and H3K14 acetylation by the NuA3 histone acetyltransferase complex.
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Cryo-EM and enzymatic assays show how a six-subunit S. cerevisiae NuA3 complex uses Sas3 and Nto1 to position the histone H3 tail for H3K14 acetylation.
"Our structure shows that the histone tail-binding cleft of NuA3 is formed cooperatively by two subunits, the catalytic subunit Sas3 and the non-catalytic subunit Nto1."
The cellular economy of the Saccharomyces cerevisiae zinc proteome.
The social and structural architecture of the yeast protein interactome.
PTHR10615 PAINT IBD export
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PTN004172926 carries the broad eukaryotic MYST-family Sas3 IBA rows, while fungal node PTN008308138 carries the NuA3a histone acetyltransferase complex assertion.
"PTHR10615 PTN008308138 GO:1990467 C IBD false SGD:S000000148 taxon:4751 20230926"
Deep research report on SAS3 (Saccharomyces cerevisiae, UniProt P34218) synthesizing yeast-specific literature on NuA3 catalytic HAT function, substrate specificity, complex architecture, chromatin targeting, and the 2024 Taf14-Sas3/Yng1 interface advance.
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SAS3 is a MYST-family histone acetyltransferase and the catalytic subunit of the NuA3 complex, which primarily acetylates histone H3 lysine 14 (H3K14) and is also associated with H3K23 acetylation in yeast chromatin.
"*S. cerevisiae* **Sas3** is a **MYST-family histone acetyltransferase (HAT)** and the **catalytic subunit of the NuA3 complex**, which primarily acetylates **histone H3 lysine 14 (H3K14)** and is also associated with **H3K23 acetylation** in yeast chromatin."
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Sas3 catalyzes acetyl-CoA-dependent lysine acetylation of histone H3, transferring an acetyl group from acetyl-CoA to the epsilon-amino group of a lysine residue, with H3K14 the best-supported primary physiological target.
"A HAT transfers an acetyl group from **acetyl-CoA** to the ε-amino group of a **lysine** residue on histones (a post-translational modification linked to chromatin accessibility and transcription)."
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Loss of SAS3 abolishes NuA3 HAT activity and disrupts complex integrity, establishing Sas3 as required for both activity and integrity of the NuA3 complex.
"Early purification identified Sas3 by peptide sequencing in a ~0.4–0.5 MDa NuA3 complex; loss of **SAS3** abolishes NuA3 HAT activity and disrupts complex integrity."
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NuA3 combines a writer (Sas3) with multiple reader domains - Yng1 PHD binds H3K4me3, Pdp3 PWWP binds H3K36me3, and Taf14 YEATS binds acyl-lysine marks - enabling chromatin-context-sensitive recruitment.
"Reader modules: **Yng1 PHD** binds **H3K4me3**; **Pdp3 PWWP** binds **H3K36me3**; **Taf14 YEATS** binds acylated histone marks including **H3K9ac/crotonylation**; Taf14 ET binds EBMs in Yng1 and Sas3."
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Sas3 mediates NuA3 interaction with the FACT subunit Spt16 through an acidic C-terminal region, connecting NuA3 to transcription elongation through nucleosomes; SAS3 disruption enhances 6-azauracil sensitivity in an Spt16-mutant background.
"Sas3 mediates NuA3 interaction with **Spt16** (in vivo and in vitro), through an acidic C-terminal region; genetic interaction includes enhanced **6-azauracil (6-AU)** sensitivity when SAS3 is disrupted in an spt16-truncation background."
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Sas3/NuA3 functions in the nucleus on chromatin, associating with transcribed genes; ChIP-on-chip mapping found Sas3 preferentially in the 5' half of coding regions, supporting involvement in transcriptional elongation.
"ChIP-on-chip mapping found Sas3 preferentially in the **5′ half of coding regions**, supporting involvement in **transcriptional elongation**."
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Best-supported roles for Sas3/NuA3 are in transcriptional regulation, coupling histone acetylation to active chromatin and antagonizing the Rpd3S/Rpd3L HDAC pathways to optimize mRNA and lncRNA expression dynamics.
"NuA3 antagonizes **Rpd3S/Rpd3L** to optimize mRNA and lncRNA expression dynamics; Sas3 disruption enhances **6-azauracil** sensitivity in an Spt16-mutant background, consistent with elongation defects."
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SAS3 belongs to the MYST (SAS/MOZ) family and is the yeast homolog/counterpart of human MOZ/MORF-type MYST HATs, with a Zf-MYST zinc-finger domain among its key domains.
"The symbol **SAS3** can refer to MYST-family HAT orthologs in other fungi (e.g., pathogens), but the target here is explicitly **budding yeast SAS3 (P34218; YBL052C)**. Foundational yeast studies purifying **NuA3** identified **Sas3 as its catalytic HAT subunit** and described Sas3 as the **yeast homolog/counterpart of human MOZ/MORF**-type MYST HATs"
Sas3 is a histone acetyltransferase and requires a zinc finger motif.