Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping
Automatic assignment of GO terms using logical inference, based on inter-ontology links
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
The yeast SAS (something about silencing) protein complex contains a MYST-type putative acetyltransferase and functions with chromatin assembly factor ASF1.
The silencing complex SAS-I links histone acetylation to the assembly of repressed chromatin by CAF-I and Asf1 in Saccharomyces cerevisiae.
Sas4 and Sas5 are required for the histone acetyltransferase activity of Sas2 in the SAS complex.
Nuclear import of the histone acetyltransferase complex SAS-I in Saccharomyces cerevisiae.
Defining the budding yeast chromatin-associated interactome.
Donor Preference Meets Heterochromatin; Moonlighting Activities of a Recombinational Enhancer in Saccharomyces cerevisiae.
The cellular economy of the Saccharomyces cerevisiae zinc proteome.
The social and structural architecture of the yeast protein interactome.
Falcon deep research report for S. cerevisiae SAS2 (P40963)
-
Sas2 is the catalytic MYST-family histone acetyltransferase subunit of the
SAS-I complex (Sas2-Sas4-Sas5), which acetylates histone H4 at lysine 16
(H4K16ac) and shapes heterochromatin boundaries by antagonizing SIR spreading.
"Sas2 acts in a nuclear complex termed **SAS-I**, composed of **Sas2, Sas4, and Sas5**, which coimmunoprecipitate and coelute as a ~220 kDa complex."
-
The strongest, repeatedly supported in vivo Sas2/SAS-I substrate is histone
H4 lysine 16 (H4K16); falcon found no robust evidence in its retrieved excerpts
for additional primary Sas2 substrates in S. cerevisiae (note: this is absence
of evidence within the falcon excerpt set, not contradiction of the H3K14
activity which is independently supported by PMID:12626510).
"the strongest, repeatedly supported in vivo substrate is **H4K16**"
-
Sas2/SAS-I provides roughly 60% of cellular H4K16ac; sas2-delta cells retain
~40% of wild-type H4K16ac because Esa1 (NuA4) is a redundant contributor.
"sas2Δ cells retain ~40% of wild-type H4K16ac, and genetic experiments indicate Esa1 can compensate for Sas2 for H4K16 acetylation"
-
SAS-I couples histone modification to replication-coupled nucleosome assembly:
it interacts with CAF-I (Cac1) and Asf1 and deposits H4K16ac immediately upon
replication in a SAS-I-dependent manner.
"SAS-I interacts with **Cac1 (CAF-I subunit)** and **Asf1**, supporting recruitment to newly assembled chromatin after replication."
-
GFP-tagged Sas2 predominantly stains the nucleus including the nucleolus, and
ChIP detects weak but reproducible association with rDNA spacer sequences;
genome-wide, Sas2-dependent H4K16ac is deposited broadly across ORF bodies
(especially lowly transcribed genes) independently of transcription and histone exchange.
"GFP-tagged Sas2 predominantly stains the nucleus, including the **nucleolus**."
MYST protein acetyltransferase activity requires active site lysine autoacetylation.
Dynamics of SAS-I mediated H4 K16 acetylation during DNA replication in yeast.
-
SAS-I establishes H4 K16 acetylation on chromatin immediately after replication, consistent with recruitment through CAF-I and Asf1 during chromatin assembly.
"H4 K16Ac appears in chromatin immediately upon replication. Importantly, this increase depends on the presence of functional SAS-I complex."
GTP-dependent regulation of heterochromatin fluctuations at subtelomeric regions in Saccharomyces cerevisiae.
PTHR10615 PAINT IBD export
-
PTN007449682 is the PTHR10615 node that currently propagates both the supported histone H4K16 acetyltransferase activity and the bad NuA4 complex component assertion to S. cerevisiae Sas2.
"PTHR10615 PTN007449682 GO:0046972 F IBD false CGD:CAL0000189453|FB:FBgn0014340|MGI:MGI:1915023|UniProtKB:Q92993 taxon:33154 20241119"
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Global landscape of protein complexes in the yeast Saccharomyces cerevisiae.