ASF1

Existing Annotations Review

Gene Description

Existing Annotations Review

Core Functions

References

Deep Research

Falcon

Perplexity

📚 Additional Documentation

Notes

📄 View Raw YAML

GO Term	Evidence	Action	Reason
GO:0000785 chromatin	IBA GO_REF:0000033	ACCEPT	Summary: Cellular component annotation based on phylogenetic orthology. ASF1 is localized to chromatin where it functions as a histone chaperone component of chromatin assembly complexes. Reason: IBA evidence from conserved orthologous function across eukaryotes. ASF1 localizes to chromatin as documented in deep research and participates in chromatin dynamics. Supporting Evidence: GO_REF:0000033 Phylogenetic annotation based on conserved ASF1 function across orthologs file:yeast/ASF1/ASF1-deep-research-perplexity.md ASF1 (anti-silencing function protein 1), encoded by the ASF1 gene (UniProt P32447) in Saccharomyces cerevisiae, is a highly conserved histone chaperone that serves as a central hub in chromatin assembly, disassembly, and remodeling pathways. file:yeast/ASF1/ASF1-deep-research-falcon.md In yeast, Asf1 is a histone chaperone that binds histones H3–H4 and participates in nucleosome assembly in multiple DNA-templated processes, including DNA replication and transcription-associated chromatin remodeling.
GO:0005634 nucleus	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetically conserved nuclear localization annotation. ASF1 is a nuclear protein required for histone deposition and chromatin dynamics in the nucleus. Reason: IBA evidence is appropriate. ASF1 is a nuclear protein functioning in chromatin assembly. Supported by experimental localization data from multiple PMIDs (11404324, 22932476, 27222517).
GO:0042393 histone binding	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetically conserved histone binding activity. ASF1 is the prototype histone H3-H4 dimer-binding chaperone. Reason: IBA evidence is well-supported. ASF1's defining function is high-affinity H3-H4 dimer binding (Kd ~2 nM). This is the most fundamental and conserved function documented across all eukaryotic orthologs. Falcon deep research confirms Asf1 binds H3-H4 dimers and shields the tetramerization surface. Supporting Evidence: GO_REF:0000033 Conservation of histone binding function across ASF1 orthologs from yeast to mammals file:yeast/ASF1/ASF1-deep-research-falcon.md Core chaperone activity: Asf1 binds H3–H4 dimers and shields the surface needed to form a stable (H3–H4)2 tetramer, thereby controlling histone oligomerization state during handling/transport and handoff.
GO:0006335 DNA replication-dependent chromatin assembly	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetically conserved role in replication-coupled nucleosome assembly. ASF1 interacts with CAF-1 and PCNA-DNAP to transfer H3-H4 dimers to replication forks. Reason: IBA evidence is appropriate. Replication-coupled chromatin assembly is a core ASF1 function conserved across eukaryotes. The deep research documents ASF1-CAF-1 collaboration at replication forks, with CAF-1 accepting H3-H4 via a direct Cac2-Asf1 interaction. Supporting Evidence: GO_REF:0000033 Conserved pathway across eukaryotes from yeast to mammals file:yeast/ASF1/ASF1-deep-research-falcon.md CAF-1 physical link: CAF-1 is reported to accept H3–H4 via direct interaction between CAF-1 subunit Cac2 and Asf1 in one mechanistic account.
GO:0000781 chromosome, telomeric region	IEA GO_REF:0000108	KEEP AS NON CORE	Summary: Computational annotation inferring localization to telomeric chromatin based on genetic interactions and pathway membership. ASF1 participates in SIR-mediated silencing at telomeres. Reason: IEA annotation is valid but represents a secondary/specialized function. ASF1 does associate with telomeric chromatin through its role in silencing complex assembly with SIR proteins, but this is not a core function. The annotation is too narrow and specific given that ASF1 associates with multiple chromosomal regions. Falcon deep research documents a quantitative, S-phase-specific telomere XIV-L peripheral localization defect in asf1 mutants, supporting an indirect role in telomere positioning via the H3K56ac pathway rather than a constitutive structural component of telomeric chromatin. Supporting Evidence: file:yeast/ASF1/ASF1-deep-research-falcon.md In a telomere XIV-L positioning assay, WT cells show ~66.0% peripheral localization (zone 1) in G1 and 67.5% in S phase. In contrast, an asf1 mutant shows 67.4% in G1 (n=46; p=0.05 vs WT) but drops to 43.1% in S phase (n=51; p=4.7×10−4 vs WT), demonstrating a statistically significant S-phase-specific defect.
GO:0005634 nucleus	IEA GO_REF:0000120	ACCEPT	Summary: Combined automated IEA annotation indicating nuclear localization inferred from multiple sources including InterPro domain-based prediction. Reason: IEA annotation is consistent with multiple experimental confirmations (PMID:11404324, 22932476, 27222517). Nuclear localization is experimentally documented.
GO:0006325 chromatin organization	IEA GO_REF:0000120	ACCEPT	Summary: IEA annotation indicating chromatin organization function inferred from InterPro domain analysis. Reason: Appropriate umbrella term supported by experimental data. ASF1 participates in multiple chromatin organization processes (nucleosome assembly, disassembly, remodeling). Documentation of these activities is found in the deep research.
GO:0006334 nucleosome assembly	IEA GO_REF:0000002	ACCEPT	Summary: InterPro-based IEA annotation. ASF1 is a documented histone deposition protein required for nucleosome assembly. Reason: IEA evidence is appropriate. Nucleosome assembly is documented core function supported by multiple experimental studies (nucleosome assembly with CAF-1, HIRA complexes). Supporting Evidence: file:yeast/ASF1/ASF1-deep-research-falcon.md In yeast, Asf1 is a histone chaperone that binds histones H3–H4 and participates in nucleosome assembly in multiple DNA-templated processes, including DNA replication and transcription-associated chromatin remodeling.
GO:0006337 nucleosome disassembly	IEA GO_REF:0000002	ACCEPT	Summary: InterPro-based IEA annotation. ASF1 participates in nucleosome disassembly during transcription. Reason: IEA is supported by experimental evidence (PMID:16678113 - IMP annotation showing ASF1 mediates histone eviction during RNA polymerase II elongation).
GO:0006351 DNA-templated transcription	IEA GO_REF:0000043	KEEP AS NON CORE	Summary: UniProtKB keyword mapping (KW-0804 transcription) to GO term. ASF1 participates in transcriptional regulation through chromatin dynamics. Reason: IEA annotation is valid but too general. ASF1 participates in transcription-related chromatin remodeling (nucleosome disassembly at promoters, H3 K56ac-mediated chromatin opening), but this is indirect. The term "DNA-templated transcription" itself is not a core ASF1 function - rather ASF1 supports transcription through chromatin modification. More specific terms (GO:0006357, GO:0032968) better capture ASF1's transcription-related roles.
GO:0042393 histone binding	IEA GO_REF:0000002	ACCEPT	Summary: InterPro domain-based IEA annotation confirming histone binding activity. Reason: IEA annotation is consistent with strong IBA evidence and experimental validation. Histone H3-H4 dimer binding is ASF1's defining function and is a core annotation across all evidence types.
GO:0005515 protein binding	IPI PMID:11404324 Yeast ASF1 protein is required for cell cycle regulation of ...	KEEP AS NON CORE	Summary: IPI annotation from the yeast ASF1 cell cycle regulation study. The two GOA WITH/FROM entries for this reference are UniProtKB:P32479 (Hir1, HIR complex) and UniProtKB:Q04003 (Sas4, SAS complex) - both chromatin-regulatory complex subunits, not histones and not CAF-1 subunits. Reason: Valid IPI annotation but the generic "protein binding" term is uninformative. ASF1 binds many proteins (histones, CAF-1, HIR/HIRA, Rad53, FACT, etc.). The term should be kept as evidence of protein interactions but marked non-core because a more specific function term describing the type of binding would be more informative. No replacement term is proposed on this row, because the interactors recorded in WITH/FROM are Hir1 and Sas4, so this evidence cannot support a histone binding replacement. ASF1's histone binding is already annotated separately (IEA from GO_REF:0000002 and IBA). Supporting Evidence: PMID:11404324 Yeast ASF1 protein is required for cell cycle regulation of histone gene transcription.
GO:0005515 protein binding	IPI PMID:11731480 The silencing complex SAS-I links histone acetylation to the...	KEEP AS NON CORE	Summary: IPI annotation with two GOA WITH/FROM entries, UniProtKB:P40963 (Sas2) and UniProtKB:Q04003 (Sas4), both subunits of the SAS-I histone acetyltransferase complex, from the study linking SAS-I histone acetylation to the assembly of repressed chromatin by CAF-I and Asf1. Reason: Valid IPI but generic protein binding term. The ASF1-Sas2/Sas4 (SAS-I complex) interactions are documented, but a more specific annotation would be warranted. See earlier protein binding annotation for rationale. Supporting Evidence: PMID:11731480 The silencing complex SAS-I links histone acetylation to the assembly of repressed chromatin by CAF-I and Asf1 in Saccharomyces cerevisiae.
GO:0005515 protein binding	IPI PMID:11805826 Functional organization of the yeast proteome by systematic ...	KEEP AS NON CORE	Summary: IPI annotation from high-throughput proteome complex analysis documenting protein interactions. Reason: Valid IPI but generic protein binding. High-throughput proteomics provide useful interaction data but less mechanistic detail than studies with specific genetic or biochemical focus. Supporting Evidence: PMID:11805826 Functional organization of the yeast proteome by systematic analysis of protein complexes.
GO:0005515 protein binding	IPI PMID:11805837 Systematic identification of protein complexes in Saccharomy...	KEEP AS NON CORE	Summary: IPI annotation from mass spectrometry-based protein complex identification in yeast. Reason: Valid IPI but generic protein binding. Similar to previous high-throughput proteomics data. Supporting Evidence: PMID:11805837 Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry.
GO:0005515 protein binding	IPI PMID:15755447 Uncoupling of unwinding from DNA synthesis implies regulatio...	KEEP AS NON CORE	Summary: IPI annotation whose sole WITH/FROM accession is UniProtKB:P22216, i.e. Rad53 - not an MCM subunit. Reason: Valid IPI but generic protein binding. The recorded partner is Rad53 - the IntAct block in ASF1-uniprot.txt pairs P32447 with P22216 under the name RAD53 (NbExp=11), and that block lists no MCM subunit among its seven partners. The earlier "MCM2 helicase" reading came from the paper title rather than from the accession. ASF1-Rad53 is a real and well-supported interaction, but its biology is DNA-damage-checkpoint recovery, already captured by the GO:2000002 and GO:0006282 rows from PMID:27222517; here "protein binding" remains insufficiently specific. Supporting Evidence: PMID:15755447 Uncoupling of unwinding from DNA synthesis implies regulation of MCM helicase by Tof1/Mrc1/Csm3 checkpoint complex.
GO:0005515 protein binding	IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine...	KEEP AS NON CORE	Summary: IPI annotations from a proteome-wide survey of yeast protein complexes; the WITH/FROM accessions recorded on these rows are UniProtKB:P11484, UniProtKB:P22216 and UniProtKB:P47171. Reason: Valid IPI but generic protein binding, and the recorded accessions are named here rather than inferred from the paper. P11484 is Ssb1, a ribosome-associated Hsp70 (SSB1-uniprot.txt), and P22216 is Rad53; P47171 is not identifiable from any record committed to this repository, so no identity is asserted for it. The earlier "DNA polymerase, MCM, and CAF-1 subunits" description matched none of the three and has been withdrawn. Several distinct interactions are collapsed into one uninformative term, which is why the row is retained as non-core rather than treated as evidence for a specific function. Supporting Evidence: PMID:16429126 Proteome survey reveals modularity of the yeast cell machinery.
GO:0005515 protein binding	IPI PMID:16554755 Global landscape of protein complexes in the yeast Saccharom...	KEEP AS NON CORE	Summary: IPI annotations from a comprehensive global protein complex landscape study, documenting ASF1 interactions with histone proteins and multiple other chromatin proteins. Reason: Valid IPI but generic protein binding. Comprehensive interaction data but term lacks specificity. The histone interactions are particularly important and are captured in GO:0042393 (histone binding). Supporting Evidence: PMID:16554755 Global landscape of protein complexes in the yeast Saccharomyces cerevisiae.
GO:0005515 protein binding	IPI PMID:18467557 An in vivo map of the yeast protein interactome.	KEEP AS NON CORE	Summary: IPI annotation from yeast in vivo protein interactome mapping documenting protein interactions. Reason: Valid IPI but generic protein binding term. Genome-wide mapping data less specific than targeted mechanistic studies. Supporting Evidence: PMID:18467557 2008 May 8. An in vivo map of the yeast protein interactome.
GO:0005515 protein binding	IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ...	KEEP AS NON CORE	Summary: IPI annotation from a chaperone-protein interaction atlas; the single WITH/FROM accession is UniProtKB:P11484 (Ssb1). Reason: Valid IPI but generic protein binding. The row records one partner, Ssb1 - a ribosome-associated Hsp70, not a histone chaperone - so the earlier "multiple histone chaperone partners" description overstated both the number and the nature of the interactors. ASF1's histone binding is annotated independently and does not rest on this row. Supporting Evidence: PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell.
GO:0005515 protein binding	IPI PMID:21179020 Defining the budding yeast chromatin-associated interactome.	KEEP AS NON CORE	Summary: IPI annotations from chromatin-associated interactome study documenting ASF1 interactions with histone proteins and chromatin regulators. Reason: Valid IPI but generic protein binding. Chromatin-associated interactions include histones and regulatory proteins, but histone binding is already specifically annotated. Supporting Evidence: PMID:21179020 Defining the budding yeast chromatin-associated interactome.
GO:0005515 protein binding	IPI PMID:24209620 A Cul4 E3 ubiquitin ligase regulates histone hand-off during...	KEEP AS NON CORE	Summary: IPI annotation from study of Cul4 E3 ubiquitin ligase documenting protein-protein interactions during nucleosome assembly. Reason: Valid IPI but generic protein binding. Documents interaction with histone proteins. Supporting Evidence: PMID:24209620 A Cul4 E3 ubiquitin ligase regulates histone hand-off during nucleosome assembly.
GO:0005515 protein binding	IPI PMID:37968396 The social and structural architecture of the yeast protein ...	KEEP AS NON CORE	Summary: IPI annotations from recent comprehensive yeast protein interactome study documenting multiple ASF1 protein interaction partners. Reason: Valid IPI but generic protein binding. Recent high-quality interactome data but term lacks specificity. Supporting Evidence: PMID:37968396 Nov 15. The social and structural architecture of the yeast protein interactome.
GO:0006335 DNA replication-dependent chromatin assembly	IDA PMID:21256037 Structure of the Rtt109-AcCoA/Vps75 complex and implications...	ACCEPT	Summary: IDA annotation from structure of Rtt109-AcCoA/Vps75 complex study documenting ASF1's role in replication-dependent chromatin assembly and H3 K56 acetylation. Reason: Strong IDA evidence from mechanistic structural study. PMID:21256037 directly demonstrates ASF1's role in H3 K56 acetylation during replication-dependent chromatin assembly. Core function. Supporting Evidence: PMID:21256037 Jan 20. Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated histone acetylation.
GO:0006338 chromatin remodeling	IDA PMID:31194870 Two factor authentication: Asf1 mediates crosstalk between H...	ACCEPT	Summary: IDA annotation from "Two factor authentication" study documenting ASF1 mediation of crosstalk between H3 K14 and K56 acetylation in chromatin dynamics. Reason: Strong IDA evidence. PMID:31194870 directly demonstrates ASF1-mediated chromatin remodeling through coordination of multiple histone acetylation sites. Documented core function. Supporting Evidence: PMID:31194870 Two factor authentication: Asf1 mediates crosstalk between H3 K14 and K56 acetylation
GO:0005634 nucleus	IDA PMID:27222517 Asf1 facilitates dephosphorylation of Rad53 after DNA double...	ACCEPT	Summary: IDA annotation from Complex Portal placing ASF1 in the nucleus as part of the RAD53-ASF1 complex (CPX-1322). Reason: ASF1 is a nuclear protein and the call is right. ASF1 belongs to exactly one Complex Portal complex, CPX-1322 RAD53-ASF1 (ASF1-uniprot.txt:625), and the GOA row carries no WITH/FROM, so the supporting quote is this paper's statement of the Asf1-Rad53 relationship that the complex records. The cached full text makes no direct statement about nuclear localization, so the localization itself rests on the curator's full record plus the independent SGD nucleus IDAs on PMID:11404324 and PMID:22932476 recorded in the GOA file. Supporting Evidence: PMID:27222517 Asf1 facilitates dephosphorylation of Rad53 after DNA double-strand break repair
GO:0006282 regulation of DNA repair	NAS PMID:27222517 Asf1 facilitates dephosphorylation of Rad53 after DNA double...	KEEP AS NON CORE	Summary: NAS (author statement) annotation indicating ASF1's role in regulating DNA repair processes through Rad53 checkpoint kinase interaction. Reason: NAS annotation is supported by the documented ASF1-Rad53 interaction, but it captures an indirect regulatory role rather than direct participation in DNA repair. ASF1 does NOT directly perform DNA repair; rather it facilitates recovery from the DNA damage checkpoint through Rad53 dephosphorylation. This is a secondary function and should be non-core. The more precise checkpoint-recovery biology is already captured by the sibling GO:2000002 annotation from the same reference. Supporting Evidence: PMID:27222517 Asf1 is required for complete dephosphorylation of Rad53 when the upstream DNA damage checkpoint signaling is turned off
GO:2000002 negative regulation of DNA damage checkpoint	NAS PMID:27222517 Asf1 facilitates dephosphorylation of Rad53 after DNA double...	ACCEPT	Summary: NAS annotation indicating ASF1 facilitates recovery from DNA damage checkpoint by enabling Rad53 dephosphorylation. Reason: NAS evidence is well-supported by deep research findings. PMID:27222517 documents that ASF1 deletion reduces recovery from DNA damage checkpoint, and mechanistic studies show ASF1 facilitates Rad53 dephosphorylation after DSB repair. This is a documented and important function. Falcon deep research independently notes the Asf1-Rad53 interaction (mediated by the Asf1 C-terminal cNLS). Supporting Evidence: PMID:27222517 Asf1 facilitates dephosphorylation of Rad53 after DNA double-strand break repair file:yeast/ASF1/ASF1-deep-research-falcon.md The Asf1 C-terminal cNLS is required for full H3K56 acetylation and for interactions with Rad53 and Hir1.
GO:0006325 chromatin organization	IDA PMID:16303565 Replication-independent histone deposition by the HIR comple...	ACCEPT	Summary: IDA annotation from "Replication-independent histone deposition by HIR complex and Asf1" documenting ASF1's role in chromatin organization through replication-independent pathways. Reason: Strong IDA evidence documenting ASF1's role in replication-independent chromatin assembly with HIRA complex. Core function. Falcon deep research corroborates this with recent (2024) structural work on the HIR complex. Supporting Evidence: PMID:16303565 Replication-independent histone deposition by the HIR complex and Asf1 file:yeast/ASF1/ASF1-deep-research-falcon.md A 2024 Molecular Cell study supports that Asf1 works together with the HIR complex (and with Rtt106) to mediate replication-independent H3–H4 deposition and maintain promoter fidelity, connecting Asf1 to transcriptional regulation through chromatin assembly/disassembly dynamics.
GO:0006357 regulation of transcription by RNA polymerase II	IMP PMID:19620280 Cooperation between the INO80 complex and histone chaperones...	ACCEPT	Summary: IMP annotation from "Cooperation between INO80 complex and histone chaperones" study showing ASF1 role in stress gene transcription adaptation. Reason: Strong IMP evidence. PMID:19620280 documents ASF1's requirement for proper transcriptional response to stress through cooperation with chromatin remodeling complexes. Core function in transcriptional regulation. Supporting Evidence: PMID:19620280 Jul 20. Cooperation between the INO80 complex and histone chaperones determines adaptation of stress gene transcription in the yeast Saccharomyces cerevisiae.
GO:0033554 cellular response to stress	IMP PMID:19620280 Cooperation between the INO80 complex and histone chaperones...	ACCEPT	Summary: IMP annotation from same INO80 study documenting ASF1's role in cellular stress response through transcriptional remodeling. Reason: IMP evidence is strong. PMID:19620280 demonstrates ASF1 is required for proper cellular response to stress through transcriptional regulation. Core biological process function. Supporting Evidence: PMID:19620280 Jul 20. Cooperation between the INO80 complex and histone chaperones determines adaptation of stress gene transcription in the yeast Saccharomyces cerevisiae.
GO:0031509 subtelomeric heterochromatin formation	IGI PMID:15840725 Structural basis for the interaction of Asf1 with histone H3...	ACCEPT	Summary: IGI annotation from "Structural basis for Asf1-H3 interaction" study showing genetic interaction between ASF1 and SIR proteins in telomeric silencing. Reason: Strong IGI evidence from mechanistic structural and genetic study. PMID:15840725 demonstrates ASF1's role in SIR-mediated telomeric silencing through specific H3-H4 binding interactions. Well-documented core function in heterochromatin. Supporting Evidence: PMID:15840725 Structural basis for the interaction of Asf1 with histone H3 and its functional implications.
GO:0005515 protein binding	IPI PMID:29300933 Structural characterization of the Asf1-Rtt109 interaction a...	KEEP AS NON CORE	Summary: IPI annotation from recent study documenting ASF1-Rtt109 interaction essential for histone acetylation. Reason: Valid IPI but generic protein binding. ASF1-Rtt109 interaction is functionally important, but the interaction is captured by the acetyltransferase activator activity function. Generic term is less informative. Supporting Evidence: PMID:29300933 Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation.
GO:0010698 acetyltransferase activator activity	IDA PMID:21256037 Structure of the Rtt109-AcCoA/Vps75 complex and implications...	ACCEPT	Summary: IDA annotation documenting ASF1 as activator of Rtt109 histone acetyltransferase activity on H3 K56. Reason: Strong IDA evidence. PMID:21256037 (Rtt109 complex structure) demonstrates ASF1 is required as a cofactor/activator enabling Rtt109 catalytic activity on histone H3 K56. Specific and well-documented molecular function. Falcon deep research confirms Asf1 presents H3-H4 to Rtt109 for H3K56 acetylation and that loss of Asf1 markedly decreases Rtt109 activity and H3K56ac. Supporting Evidence: PMID:21256037 Jan 20. Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated histone acetylation. file:yeast/ASF1/ASF1-deep-research-falcon.md Asf1 is described as solely required for H3K56ac in yeast cells in the Dannah thesis excerpts, and loss of Asf1 markedly decreases Rtt109 activity and H3K56ac.
GO:0005515 protein binding	IPI PMID:31387991 Histone chaperone exploits intrinsic disorder to switch acet...	KEEP AS NON CORE	Summary: IPI annotation from "Histone chaperone exploits intrinsic disorder to switch acetylation specificity" study documenting ASF1-Rtt109 interaction. Reason: Valid IPI but generic protein binding. ASF1-Rtt109 interaction is important but better captured in acetyltransferase activator activity (GO:0010698) annotation. Supporting Evidence: PMID:31387991 Histone chaperone exploits intrinsic disorder to switch acetylation specificity.
GO:0070775 H3 histone acetyltransferase complex	IDA PMID:31387991 Histone chaperone exploits intrinsic disorder to switch acet...	ACCEPT	Summary: IDA annotation from "Histone chaperone exploits intrinsic disorder" study showing ASF1 is component of H3 histone acetyltransferase complex with Rtt109. Reason: Strong IDA evidence. PMID:31387991 demonstrates ASF1 is integral component of H3-specific acetyltransferase complex with Rtt109 for K56 acetylation. Core cellular component function. Supporting Evidence: PMID:31387991 Histone chaperone exploits intrinsic disorder to switch acetylation specificity.
GO:0042393 histone binding	IDA PMID:31194870 Two factor authentication: Asf1 mediates crosstalk between H...	ACCEPT	Summary: Third histone binding annotation with IDA evidence from "Two factor authentication" study. Reason: Strong IDA evidence documenting ASF1's histone binding function in chromatin dynamics. PMID:31194870 directly demonstrates ASF1-histone interactions are essential for coordination of multiple acetylation sites. Core molecular function. Supporting Evidence: PMID:31194870 Two factor authentication: Asf1 mediates crosstalk between H3 K14 and K56 acetylation.
GO:0005829 cytosol	IDA PMID:22932476 The nuclear localization of SWI/SNF proteins is subjected to...	KEEP AS NON CORE	Summary: IDA annotation from "Nuclear localization of SWI/SNF proteins" study documenting ASF1 localization in cytosol. Reason: Valid IDA annotation but ASF1's primary function is nuclear. Cytosolic localization is a secondary/minor localization. Asf1 binds newly synthesized H3-H4 in the cytoplasm before nuclear import (falcon deep research), but its core functions are nuclear: a functional cNLS in the acidic C-terminal tail is required for nuclear localization, and its loss makes Asf1 fully cytoplasmic with loss of H3K56ac pathway output. The cytosol annotation therefore reflects the transient histone-loading/import step rather than a primary site of function. Supporting Evidence: PMID:22932476 The nuclear localization of SWI/SNF proteins is subjected to oxygen regulation. file:yeast/ASF1/ASF1-deep-research-falcon.md - Asf1 binds newly synthesized H3–H4 (described as occurring in the cytoplasm in one mechanistic account), promotes nuclear import/availability, and presents H3–H4 to Rtt109 for acetylation of H3K56. file:yeast/ASF1/ASF1-deep-research-falcon.md Asf1 contains a functional classical nuclear localization signal (cNLS) in its highly acidic C-terminal tail, and that removal of this motif makes Asf1 fully cytoplasmic, indicating the motif is required for nuclear localization.
GO:0001932 regulation of protein phosphorylation	IMP PMID:27222517 Asf1 facilitates dephosphorylation of Rad53 after DNA double...	MARK AS OVER ANNOTATED	Summary: IMP annotation from Rad53 dephosphorylation study showing ASF1 regulates phosphorylation state of checkpoint kinase. Reason: While ASF1 does facilitate Rad53 dephosphorylation (negative regulation of phosphorylation), the broader term "regulation of protein phosphorylation" is too general. ASF1 doesn't directly phosphorylate or dephosphorylate proteins; it acts as a cofactor binding Rad53 and enabling protein phosphatase interaction. The specific function is better captured as "negative regulation of DNA damage checkpoint" (GO:2000002, already annotated). This represents an indirect regulatory role. Supporting Evidence: PMID:27222517 Asf1 facilitates dephosphorylation of Rad53 after DNA double-strand break repair.
GO:0010468 regulation of gene expression	IMP PMID:26941319 Expression homeostasis during DNA replication.	ACCEPT	Summary: IMP annotation from "Expression homeostasis during DNA replication" study showing ASF1 maintains histone levels and gene expression during S phase. Reason: IMP evidence is strong. PMID:26941319 demonstrates ASF1's role in maintaining expression homeostasis during DNA replication, which is essential for balanced histone supply and gene expression coordination. Core biological process. Falcon deep research adds that Asf1 participates in cell-cycle-coupled histone gene transcription (activation in S phase, repression outside S phase) together with Hir1. Supporting Evidence: PMID:26941319 Expression homeostasis during DNA replication file:yeast/ASF1/ASF1-deep-research-falcon.md In yeast-focused statements summarized in a 2024 preprint, Asf1 is described as participating in histone gene transcriptional activation in S phase and transcriptional repression outside S phase in combination with Hir1 (a yeast counterpart of metazoan HIRA pathway components).