ESA1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0000785 chromatin	IBA GO_REF:0000033	ACCEPT	Summary: ESA1 is a core component of the NuA4 complex that acts on chromatin substrates. Phylogenetic inference (IBA) correctly identifies chromatin as the cellular location where ESA1 functions through nucleosome acetylation. Reason: ESA1 functions directly on chromatin through histone acetylation. Multiple experimental sources confirm NuA4 recruitment to chromatin and nucleosome-level acetylation patterns. The IBA evidence is conservative but appropriate. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN004172926 · MYST/KAT acetyltransferase ancestral node SUPPORTS TRANSFER The current PTHR10615 broad MYST/KAT node supports chromatin as the activity context for ESA1 and related nuclear histone acetyltransferases; yeast Esa1 directly seeds this conserved chromatin assertion. Supporting Evidence: PMID:21984211 We have used EM and biochemistry to characterize the structure of NuA4, an essential yeast histone acetyltransferase (HAT) complex conserved throughout eukaryotes, and we have determined the interaction of NuA4 with the nucleosome core particle (NCP).
GO:0000785 chromatin	IDA PMID:10911987 Multiple links between the NuA4 histone acetyltransferase co...	ACCEPT	Summary: Direct experimental evidence (IDA) confirms ESA1 localizes to and functions on chromatin. This duplicate annotation with IBA provides independent confirmation. Reason: Multiple evidence codes for the same essential localization strengthen the annotation. IDA from PMID:10911987 provides direct experimental documentation. Supporting Evidence: PMID:10911987 Accordingly, NuA4 is localized in precise loci within the nucleus and does not overlap with the silent chromatin marker Sir3.
GO:0005634 nucleus	IBA GO_REF:0000033	ACCEPT	Summary: ESA1 is a nuclear protein required for nuclear transcriptional and DNA repair processes. IBA annotation appropriately identifies the nucleus as the functional compartment. Reason: ESA1 participates in nuclear-localized processes (transcription, DNA repair, cell cycle). Nuclear localization is essential and well-documented. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN004172926 · MYST/KAT acetyltransferase ancestral node SUPPORTS TRANSFER The current PTHR10615 broad MYST/KAT node supports nuclear localization for ESA1-family chromatin acetyltransferases and transfers safely to yeast Esa1.
GO:0005634 nucleus	NAS PMID:24843044 Eaf5/7/3 form a functionally independent NuA4 submodule link...	ACCEPT	Summary: NAS (narrative assertion) evidence from PMID:24843044 confirms nuclear localization. Redundant with IBA but provides independent literature support. Reason: Multiple evidence codes strengthen localization annotation. NAS documentation is appropriate for established compartment assignment. Supporting Evidence: PMID:24843044 The NuA4 histone acetyltransferase complex is required for gene regulation, cell cycle progression, and DNA repair.
GO:0004402 histone acetyltransferase activity	IBA GO_REF:0000033	ACCEPT	Summary: ESA1 is the defining histone acetyltransferase of the NuA4 complex. IBA annotation captures the fundamental catalytic function through phylogenetic inference. Reason: This is ESA1's defining enzymatic function. Extensive literature demonstrates HAT activity on all conserved H4 lysines and additional histone tails. IBA reflects phylogenetic conservation of this catalytic function across eukaryotic orthologs.
GO:0004402 histone acetyltransferase activity	IEA GO_REF:0000120	ACCEPT	Summary: Computational inference (IEA) based on InterPro domain IPR002717 (HAT_MYST-type) independently confirms HAT activity. Reason: ESA1 contains the MYST HAT catalytic domain and has experimental HAT activity. IEA based on domain analysis is appropriate and provides independent evidence.
GO:0004402 histone acetyltransferase activity	IDA PMID:17274630 Nucleosome recognition by the Piccolo NuA4 histone acetyltra...	ACCEPT	Summary: Direct experimental evidence (IDA) from nucleosome recognition and acetyltransferase activity studies confirms HAT activity. Reason: IDA evidence from Piccolo NuA4 complex study demonstrates direct enzymatic activity on nucleosomal substrates. Multiple evidence codes strengthen this essential annotation. Supporting Evidence: PMID:17274630 the H2A, H3, and H2B tails do not influence the ability of picNuA4 to tetra-acetylate the H4 tail within the nucleosome
GO:0004402 histone acetyltransferase activity	IMP PMID:10487762 NuA4, an essential transcription adaptor/histone H4 acetyltr...	ACCEPT	Summary: Mutational analysis (IMP) shows esa1 mutations abolish acetyltransferase activity in vitro and in vivo. Reason: Temperature-sensitive esa1 mutants and catalytic site mutations document HAT activity through loss-of-function studies. Supporting Evidence: PMID:10487762 Antibodies against Esa1p specifically immunoprecipitate NuA4 activity whereas the complex purified from a temperature-sensitive esa1 mutant loses its acetyltransferase activity at the restrictive temperature.
GO:0010485 histone H4 acetyltransferase activity	IEA GO_REF:0000117	ACCEPT	Summary: ARBA machine learning inference (IEA) identifies H4 as the primary histone substrate. This is the most mechanistically informative histone acetylation annotation. Reason: ESA1's defining activity is H4 acetylation at K5, K8, K12, K16. This specific substrate annotation is more informative than the generic GO:0004402. IEA inference is appropriate given clear mechanistic focus on H4.
GO:0010485 histone H4 acetyltransferase activity	IDA PMID:12110674 A conserved motif common to the histone acetyltransferase Es...	ACCEPT	Summary: Direct experimental evidence (IDA) from domain mutagenesis studies identifies the ESA1-RPD3 motif as essential for H4 acetyltransferase activity. Reason: IDA from PMID:12110674 provides mechanistic details through mutagenesis of specific residues (W247, N250, L251, etc.) that abolish H4 acetylation activity. This is strong experimental support for H4-specific activity. Supporting Evidence: PMID:12110674 We did alanine-scanning mutagenesis and found that the ER motif regions of Esa1 or Rpd3 are required for HAT activity of Esa1 or HDAC activity of Rpd3, respectively.
GO:0061733 protein-lysine-acetyltransferase activity	IEA GO_REF:0000120	ACCEPT	Summary: Computational annotation (IEA) based on EC 2.3.1.48 mapping captures ESA1's ability to acetylate both histone and non-histone protein substrates. Reason: UniProt EC classification 2.3.1.48 directly maps to 'protein-lysine-acetyltransferase'. This formal enzymatic classification is appropriate and allows inclusion of emerging non-histone substrate functions.
GO:0061733 protein-lysine-acetyltransferase activity	IDA PMID:29765047 Tip60-mediated lipin 1 acetylation and ER translocation dete...	ACCEPT	Summary: Direct experimental evidence (IDA) demonstrates ESA1-mediated acetylation of the non-histone protein PAH1 (lipin) with functional consequences for fatty acid synthesis. Reason: IDA from PMID:29765047 documents non-histone substrate acetylation. Multiple evidence codes strengthen this broader substrate annotation. Supporting Evidence: PMID:29765047 Two acetylation sites, Lys496 and Lys801, were found as the major acetylation sites on PAH1 targeted by ESA1
GO:0106226 peptide 2-hydroxyisobutyryltransferase activity	IEA GO_REF:0000116	UNDECIDED	Summary: Computational annotation (IEA) based on Rhea enzymatic reaction mapping infers 2-hydroxyisobutyryltransferase activity from fission yeast Mst1. However, in vivo activity in budding yeast is undocumented. Reason: UniProt documents potential 2-hydroxyisobutyrylation capability based on sequence homology to Schizosaccharomyces pombe Mst1 (O94446), the SF218 ESA1 ortholog. However: (1) the evidence is sequence-based rather than experimental for budding yeast Esa1; (2) biological relevance in budding yeast is unclear; (3) no literature documents in vivo 2-hydroxyisobutyrylation by Esa1 in budding yeast. Annotation reflects ortholog capability but lacks direct experimental support.
GO:0140064 peptide crotonyltransferase activity	IEA GO_REF:0000116	ACCEPT	Summary: Computational annotation (IEA) based on Rhea enzymatic reaction RHEA:53908 appropriately identifies crotonyl-CoA transferase activity. Reason: PMID:31699900 directly demonstrates ESA1 catalyzes histone crotonylation in vivo. Rhea mapping is appropriate for this documented biochemical activity.
GO:0140068 histone crotonyltransferase activity	IDA PMID:31699900 Gcn5 and Esa1 function as histone crotonyltransferases to re...	ACCEPT	Summary: Direct experimental evidence (IDA) from PMID:31699900 demonstrates ESA1-catalyzed histone crotonylation as a documented biochemical function. Reason: PMID:31699900 directly shows Piccolo NuA4 crotonyltransferase activity toward nucleosomes in vitro, and the catalytically dead Esa1-E338Q substitution abrogates this activity. IDA evidence is strong and direct. Supporting Evidence: PMID:31699900 The Piccolo NuA4 complex, similar to the ADA complex, also exhibited crotonyltransferase activity toward nucleosomes in a manner dependent on its catalytic activity
GO:0016740 transferase activity	IEA GO_REF:0000043	KEEP AS NON CORE	Summary: Generic annotation identifying ESA1 as a transferase enzyme. Technically correct but overly general and subsumed by more specific acetyltransferase annotations. Reason: While accurate (acetyltransferases are transferases), this annotation is uninformative and redundant with GO:0004402 and GO:0061733. Should not be displayed as primary annotation but acceptable as ancestor term coverage.
GO:0003712 transcription coregulator activity	IBA GO_REF:0000033	ACCEPT	Summary: ESA1 as part of NuA4 functions as a transcription coregulator by acetylating histones and facilitating RNA Pol II activity. IBA annotation appropriately identifies this molecular function role. Reason: ESA1 is not a core promoter component but rather a regulatory enzyme recruited by transcription factors. It modulates transcription through chromatin remodeling - the definition of a coregulator. IBA evidence is appropriate for this conserved function. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN004172926 · MYST/KAT acetyltransferase ancestral node SUPPORTS TRANSFER The current PTHR10615 broad MYST/KAT node supports transcription coregulator activity for ESA1-family chromatin acetyltransferases, matching Esa1's NuA4-dependent regulation of Pol II transcription.
GO:0003712 transcription coregulator activity	IDA PMID:31699900 Gcn5 and Esa1 function as histone crotonyltransferases to re...	ACCEPT	Summary: IDA evidence from crotonylation paper documents transcription coregulator function through histone modification. Multiple evidence codes strengthen this essential annotation. Reason: PMID:31699900 demonstrates ESA1-catalyzed histone modifications that regulate transcription, confirming coregulator status through mechanism. Supporting Evidence: PMID:31699900 Thus, we identify the Gcn5- and Esa1-containing ADA and Piccolo NuA4 complexes as bona fide crotonyltransferases that promote crotonylation-dependent transcription.
GO:0003682 chromatin binding	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Chromatin binding is plausible for ESA1 but too generic to represent a core mechanistic function. Reason: Esa1 does associate with chromatin as the catalytic subunit of NuA4/Piccolo NuA4, so the term is true, but chromatin binding here is a consequence of substrate engagement by the complex rather than a separately characterised binding activity of Esa1. No more specific descendant binding term is supported by the evidence, so the term is retained at this level as peripheral to the core H4 acetyltransferase activity. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN004172926 · MYST/KAT acetyltransferase ancestral node SUPPORTS TRANSFER The current PTHR10615 broad MYST/KAT node supports conserved chromatin association. For ESA1 this is true but secondary to the more informative histone acetyltransferase and chromatin-location assertions.
GO:0006281 DNA repair	IEA GO_REF:0000043	ACCEPT	Summary: ESA1 is required for DNA double-strand break repair through H4 acetylation enabling repair machinery accessibility. IEA annotation based on UniProt 'DNA repair' keyword is appropriate. Reason: PMID:12353039 provides strong experimental evidence for DNA repair requirement. IEA from keyword is conservative but appropriate for this well-documented function.
GO:0006281 DNA repair	IMP PMID:12353039 Acetylation of histone H4 by Esa1 is required for DNA double...	ACCEPT	Summary: Mutational analysis (IMP) directly demonstrates that esa1 mutations result in DNA repair defects. This is the strongest evidence for DNA repair function. Reason: PMID:12353039 shows temperature-sensitive esa1 mutants are defective in both nonhomologous end joining and replication-coupled repair. Mutational analysis provides definitive functional proof. Supporting Evidence: PMID:12353039 Both pathways require the ESA1 histone acetyl transferase (HAT), which is responsible for acetylating all H4 tail lysines, including ectopic lysines that restore repair capacity to a mutant H4 tail.
GO:0006281 DNA repair	IDA PMID:16135807 Regulation of NuA4 histone acetyltransferase activity in tra...	ACCEPT	Summary: IDA evidence from phosphorylation regulation study documents NuA4/ESA1 involvement in DNA repair. Multiple evidence codes strengthen this critical annotation. Reason: PMID:16135807 'Regulation of NuA4 histone acetyltransferase activity in transcription and DNA repair' documents functional role through direct experimental analysis. Supporting Evidence: PMID:16135807 Chromatin immunoprecipitation experiments also link local phosphorylation of H4 with its deacetylation, during both transcription and DNA repair.
GO:0006281 DNA repair	IGI PMID:25628362 A moonlighting metabolic protein influences repair at DNA do...	ACCEPT	Summary: Genetic interaction (IGI) evidence documents functional relationship between ESA1 and DNA repair machinery components. Reason: IGI evidence provides functional validation of repair requirement. However, IMP evidence from PMID:12353039 is more direct. Supporting Evidence: PMID:25628362 Lys20 was recruited to sites of DNA damage, and its overexpression promoted enhanced recruitment of the INO80 remodeling complex to restore normal histone eviction at the damage sites.
GO:0006974 DNA damage response	IEA GO_REF:0000043	ACCEPT	Summary: ESA1 is specifically recruited to DNA damage sites and activated in response to DSBs. IEA annotation from UniProt 'DNA damage' keyword is appropriate. Reason: PMID:12353039 and other literature show Arp4 component of NuA4 is recruited to DSBs and ESA1 activity is required for repair response. This is a well-documented DNA damage response function.
GO:0006325 chromatin organization	IEA GO_REF:0000043	ACCEPT	Summary: Histone acetylation fundamentally alters chromatin structure by disrupting histone-DNA contacts and affecting nucleosome positioning. ESA1-catalyzed acetylation contributes to chromatin organization. Reason: Histone acetylation is a key mechanism for chromatin remodeling and nucleosome organization. IEA inference from 'chromatin' keyword is appropriate for this mechanistic consequence of HAT activity.
GO:0006351 DNA-templated transcription	IEA GO_REF:0000043	KEEP AS NON CORE	Summary: While ESA1 does affect transcription through chromatin modifications, it is not a core transcription component. This annotation inappropriately suggests ESA1 performs transcription rather than regulating it. Reason: Annotation is not incorrect but lacks specificity and may be misleading. ESA1's role is regulatory (GO:0006357, GO:0032968), not core transcriptional machinery (GO:0006351). IEA inference from UniProt 'Chromatin' and 'DNA repair' keywords led to automatic broad annotation. Prefer more specific regulatory terms.
GO:0006351 DNA-templated transcription	NAS PMID:24843044 Eaf5/7/3 form a functionally independent NuA4 submodule link...	MARK AS OVER ANNOTATED	Summary: NAS evidence from PMID:24843044 broadly connects NuA4 to gene regulation, but DNA-templated transcription is too general beside Esa1's accepted transcription-regulatory annotations. Reason: ESA1 affects transcription through histone acetylation and chromatin modification, not as a core transcriptional component. The specific accepted GO:0006357 Pol II transcription-regulation rows capture this function more informatively than the generic GO:0006351 parent. Supporting Evidence: PMID:24843044 The NuA4 histone acetyltransferase complex is required for gene regulation, cell cycle progression, and DNA repair.
GO:0006355 regulation of DNA-templated transcription	IEA GO_REF:0000002	ACCEPT	Summary: ESA1 regulates transcription initiation and maintenance through chromatin acetylation. InterPro-based inference is appropriate for this regulatory role. Reason: This annotation correctly distinguishes ESA1's regulatory role from core transcription machinery. IEA from InterPro domain analysis is appropriate.
GO:0006357 regulation of transcription by RNA polymerase II	IBA GO_REF:0000033	ACCEPT	Summary: ESA1-containing NuA4 complex is recruited to Pol II genes and regulates transcription. IBA annotation captures this core biological function through phylogenetic inference. Reason: Extensive literature demonstrates NuA4 recruitment to Pol II-transcribed genes, acetylation of promoter and coding region nucleosomes, and requirement for normal transcription initiation and elongation. This is a well-established and essential function. IBA evidence reflects phylogenetic conservation across eukaryotes. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN004172926 · MYST/KAT acetyltransferase ancestral node SUPPORTS TRANSFER The current PTHR10615 broad MYST/KAT node supports conserved Pol II transcriptional regulation, a core consequence of Esa1/NuA4 histone acetylation.
GO:0006357 regulation of transcription by RNA polymerase II	IEA GO_REF:0000117	ACCEPT	Summary: ARBA machine learning inference (IEA) independently confirms Pol II transcription regulation function. Duplicate annotation with IBA provides computational confirmation. Reason: Both IBA and IEA converge on this annotation, providing confidence. IEA from ARBA model is appropriate.
GO:0006357 regulation of transcription by RNA polymerase II	IMP PMID:11036083 The yeast NuA4 and Drosophila MSL complexes contain homologo...	ACCEPT	Summary: Mutational analysis (IMP) documents that esa1 is required for Pol II transcription regulation. This is strong experimental support for transcription function. Reason: PMID:11036083 demonstrates through functional analysis that NuA4/ESA1 is required for transcription regulation. Multiple evidence codes strengthen this essential annotation. Supporting Evidence: PMID:11036083 The EAF3 deletion and the ESA1 mutation lead to a decrease in PHO5 gene expression; the EAF3 deletion also significantly reduces HIS4 and TRP4 expressions.
GO:0006354 DNA-templated transcription elongation	IDA PMID:15949446 Dynamic lysine methylation on histone H3 defines the regulat...	ACCEPT	Summary: Direct experimental evidence (IDA) documents ESA1 involvement in transcription elongation through interplay with H3 methylation marks. Reason: PMID:15949446 documents dynamic lysine acetylation patterns during transcription elongation. This is a specific and important ESA1 function distinct from initiation. Supporting Evidence: PMID:15949446 are required for transient NuA4-dependent H4K8ac. This releases RNAPII from Isw1 control and promotes controlled transcription elongation and termination.
GO:0006354 DNA-templated transcription elongation	IMP PMID:15949446 Dynamic lysine methylation on histone H3 defines the regulat...	ACCEPT	Summary: Mutational/functional analysis (IMP) documents ESA1 is required for transcription elongation as distinct from initiation. Reason: IMP evidence strengthens this specific annotation. Multiple evidence codes document elongation-specific function. Supporting Evidence: PMID:15949446 are required for transient NuA4-dependent H4K8ac. This releases RNAPII from Isw1 control and promotes controlled transcription elongation and termination.
GO:0032968 positive regulation of transcription elongation by RNA polymerase II	IMP PMID:19822662 NuA4 lysine acetyltransferase Esa1 is targeted to coding reg...	ACCEPT	Summary: ESA1 positively stimulates transcription elongation through H4 acetylation. IMP evidence is strong and specific. Reason: PMID:19822662 is explicit: 'NuA4 lysine acetyltransferase Esa1 is targeted to coding regions and stimulates transcription elongation with Gcn5.' This is more specific and informative than generic transcription regulation. Supporting Evidence: PMID:19822662 The NuA4 KAT, Esa1, mediates increased H4 acetylation and enhanced RSC occupancy and histone eviction in coding sequences and stimulates the rate of transcription elongation.
GO:0032968 positive regulation of transcription elongation by RNA polymerase II	IGI PMID:19822662 NuA4 lysine acetyltransferase Esa1 is targeted to coding reg...	ACCEPT	Summary: Genetic interaction evidence (IGI) provides additional functional confirmation of ESA1's elongation stimulation role. Reason: IGI from same paper as IMP documents genetic evidence for elongation function. Supporting Evidence: PMID:19822662 The NuA4 KAT, Esa1, mediates increased H4 acetylation and enhanced RSC occupancy and histone eviction in coding sequences and stimulates the rate of transcription elongation.
GO:0010629 negative regulation of gene expression	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: Esa1 participates in rDNA and telomeric silencing, but this ARBA negative-regulation parent is secondary beside the specific rDNA heterochromatin rows and Esa1's dominant positive transcriptional roles. Reason: PMID:16436512 directly implicates Esa1 in silencing Pol II-transcribed genes at telomeres and within rDNA. rDNA heterochromatin formation is a descendant of negative regulation of gene expression, so the electronic parent is biologically consistent but secondary to Esa1's core H4-acetyltransferase role and its activating Pol II transcription-regulation functions. Supporting Evidence: PMID:16436512 Here we report that Esa1p also plays a key role in silencing RNA polymerase II (Pol II)-transcribed genes at telomeres and within the ribosomal DNA (rDNA)
GO:0035267 NuA4 histone acetyltransferase complex	IEA GO_REF:0000117	ACCEPT	Summary: ESA1 is the catalytic subunit and core component of the NuA4 complex. ARBA inference appropriately identifies complex membership. Reason: ESA1 is essential for NuA4 assembly and catalysis - it is the catalytic heart of the complex. This is a fundamental annotation.
GO:0035267 NuA4 histone acetyltransferase complex	IDA PMID:15485911 The Yaf9 component of the SWR1 and NuA4 complexes is require...	ACCEPT	Summary: IDA evidence from Yaf9 paper documents ESA1 as core NuA4 component. Multiple evidence codes strengthen complex membership annotation. Reason: PMID:15485911 'The Yaf9 component of the SWR1 and NuA4 complexes is required for proper gene expression' confirms ESA1 as NuA4 component through protein interaction and functional analysis. Supporting Evidence: PMID:15485911 We verify that Yaf9 is a stable component of NuA4, an essential histone H4 acetyltransferase complex.
GO:0035267 NuA4 histone acetyltransferase complex	IDA PMID:10911987 Multiple links between the NuA4 histone acetyltransferase co...	ACCEPT	Summary: IDA evidence from foundational NuA4 characterization paper documents ESA1 as core complex component. Reason: PMID:10911987 is a landmark paper establishing NuA4 complex composition including ESA1. Provides comprehensive evidence for complex membership. Supporting Evidence: PMID:10911987 These data along with the known epigenetic roles of Act3/Arp4 and homologs of Epl1 and Esa1 strongly support an essential role for chromatin structure modification by NuA4 in transcription regulation in vivo.
GO:0032777 piccolo histone acetyltransferase complex	IDA PMID:12782659 Yeast enhancer of polycomb defines global Esa1-dependent ace...	ACCEPT	Summary: ESA1 is also a component of the Piccolo-NuA4 complex variant. IDA evidence documents this complex variant membership. Reason: PMID:12782659 'Yeast enhancer of polycomb defines global Esa1-dependent acetylation of chromatin' identifies the Epl1-containing Piccolo NuA4 as a NuA4 variant. ESA1 serves as catalytic subunit in both NuA4 and Piccolo NuA4 complexes. Supporting Evidence: PMID:12782659 The picNuA4 complex contains Esa1, Epl1, and Yng2 as subunits and strongly prefers chromatin over free histones as substrate.
GO:0033554 cellular response to stress	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: ESA1 participates in DNA damage response (a cellular stress response). Annotation is correct but overly generic. Reason: While technically accurate (DNA damage response is a stress response), this annotation is too broad and is subsumed by more specific annotations (GO:0006974 DNA damage response, GO:0006281 DNA repair). Prefer specific stress response annotations rather than the generic cellular response to stress.
GO:0010867 positive regulation of triglyceride biosynthetic process	IDA PMID:29765047 Tip60-mediated lipin 1 acetylation and ER translocation dete...	KEEP AS NON CORE	Summary: ESA1 acetylates PAH1 (lipin), promoting ER translocation and fatty acid synthesis. IDA evidence documents this secondary metabolic function. Reason: PMID:29765047 documents conserved NuA4/Tip60 regulation of lipin/Pah1-family lipid metabolism, and the yeast NuA4-Pah1 relationship was extended in PMID:38961766. This is a documented secondary function; ESA1's primary roles are chromatin/epigenetics and DNA repair, not lipid metabolism. Mark as non-core. Supporting Evidence: PMID:38961766 Two NuA4-dependent acetylation sites have been identified on Pah1, and lysine to arginine mutations at these two sites, in tandem, resulted in a reduction in lipid droplet formation. PMID:38961766 Mutation of a NuA4-dependent acetylation site on Pah1 also resulted in aberrant Pah1 localization and defects in nuclear morphology and NVJ.
GO:0016239 positive regulation of macroautophagy	IMP PMID:22539722 Function and molecular mechanism of acetylation in autophagy...	KEEP AS NON CORE	Summary: ESA1 positively regulates autophagy through acetylation of ATG3. IMP evidence documents this emerging function. Reason: PMID:22539722 'Function and molecular mechanism of acetylation in autophagy regulation' demonstrates ESA1-mediated acetylation of ATG3 K19/K48 controls autophagy. Mechanistically sound but not a primary ESA1 function. Mark as non-core. Supporting Evidence: PMID:22539722 We used genetic analysis of Saccharomyces cerevisiae to identify Esa1 as a histone acetyltransferase required for autophagy.
GO:0008270 zinc ion binding	RCA PMID:30358795 The cellular economy of the Saccharomyces cerevisiae zinc pr...	KEEP AS NON CORE	Summary: ESA1 contains a C2HC MYST-type zinc finger that coordinates zinc as a structural element of the catalytic domain. Reason: UniProt confirms the degenerate C2HC MYST zinc finger at residues 195..220, and PMID:30358795 identifies this feature in a yeast zinc-proteome survey. Zinc coordination is a structural contribution to the catalytic domain rather than a separate core molecular function. Supporting Evidence: file:yeast/ESA1/ESA1-uniprot.txt FT ZN_FING 195..220 FT /note="C2HC MYST-type; degenerate" FT /evidence="ECO:0000255\|PROSITE-ProRule:PRU01063"
GO:0051726 regulation of cell cycle	IMP PMID:10082517 Esa1p is an essential histone acetyltransferase required for...	ACCEPT	Summary: ESA1 is essential for cell cycle progression, particularly through the mitosis/cytokinesis checkpoint. IMP evidence is strong. Reason: PMID:10082517 'Esa1p is an essential histone acetyltransferase required for cell cycle progression' demonstrates through temperature-sensitive mutant analysis that esa1 is required for mitosis. Temperature-sensitive esa1 mutants complete DNA replication but block at mitosis/cytokinesis. Supporting Evidence: PMID:10082517 Strains carrying these mutations are also blocked in the cell cycle such that at restrictive temperatures, esa1 mutants succeed in replicating their DNA but fail to proceed normally through mitosis and cytokinesis.
GO:0000183 rDNA heterochromatin formation	IMP PMID:16436512 Distinct roles for the essential MYST family HAT Esa1p in tr...	KEEP AS NON CORE	Summary: ESA1 has documented but mechanistically unclear roles in rDNA silencing. This appears paradoxical given ESA1's primary role as a transcriptional activator. Reason: PMID:16436512 'Distinct roles for the essential MYST family HAT Esa1p in transcriptional silencing' demonstrates ESA1 involvement in rDNA heterochromatin. However: (1) Mechanistically counterintuitive - how does H4 acetylation (typically euchromatin mark) promote heterochromatin formation? (2) The paper title emphasizes 'distinct roles' suggesting indirect or complex mechanism; (3) ESA1's primary documented function is transcriptional activation, not silencing. Mark as non-core. Supporting Evidence: PMID:16436512 Here we report that Esa1p also plays a key role in silencing RNA polymerase II (Pol II)-transcribed genes at telomeres and within the ribosomal DNA (rDNA) of the nucleolus.
GO:0000183 rDNA heterochromatin formation	IGI PMID:16436512 Distinct roles for the essential MYST family HAT Esa1p in tr...	KEEP AS NON CORE	Summary: Genetic interaction evidence (IGI) from same paper as IMP documents functional relationship with rDNA silencing machinery. Reason: IGI provides additional evidence for rDNA silencing involvement, but same mechanistic concerns apply. Multiple evidence codes strengthen annotation but don't resolve mechanism. Supporting Evidence: PMID:16436512 Here we report that Esa1p also plays a key role in silencing RNA polymerase II (Pol II)-transcribed genes at telomeres and within the ribosomal DNA (rDNA) of the nucleolus.
GO:0005515 protein binding	IPI PMID:10487762 NuA4, an essential transcription adaptor/histone H4 acetyltr...	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and UniProtKB:P38811. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0005515 protein binding	IPI PMID:10911987 Multiple links between the NuA4 histone acetyltransferase co...	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and UniProtKB:P80428. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0005515 protein binding	IPI PMID:11036083 The yeast NuA4 and Drosophila MSL complexes contain homologo...	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and UniProtKB:Q12432. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0005515 protein binding	IPI PMID:12672825 Opposite role of yeast ING family members in p53-dependent t...	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and an older IntAct partner. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0005515 protein binding	IPI PMID:15045029 A protein complex containing the conserved Swi2/Snf2-related...	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and UniProtKB:P38811. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0005515 protein binding	IPI PMID:15353583 Regulation of chromosome stability by the histone H2A varian...	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and UniProtKB:Q12432. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0005515 protein binding	IPI PMID:15485911 The Yaf9 component of the SWR1 and NuA4 complexes is require...	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and UniProtKB:P38811. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0005515 protein binding	IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine...	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and UniProtKB:P38811. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0005515 protein binding	IPI PMID:16554755 Global landscape of protein complexes in the yeast Saccharom...	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and an older IntAct partner. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0005515 protein binding	IPI PMID:20489023 A global protein kinase and phosphatase interaction network ...	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and UniProtKB:P38811. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0005515 protein binding	IPI PMID:21179020 Defining the budding yeast chromatin-associated interactome.	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and UniProtKB:P02309. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0005515 protein binding	IPI PMID:21183953 Gcn4p-mediated transcriptional repression of ribosomal prote...	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and UniProtKB:P11938. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0005515 protein binding	IPI PMID:21984211 Structure and nucleosome interaction of the yeast NuA4 and P...	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and an older IntAct partner. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0005515 protein binding	IPI PMID:22020126 MYST protein acetyltransferase activity requires active site...	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and UniProtKB:P02309. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0005515 protein binding	IPI PMID:24843044 Eaf5/7/3 form a functionally independent NuA4 submodule link...	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and UniProtKB:P80428. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0005515 protein binding	IPI PMID:37968396 The social and structural architecture of the yeast protein ...	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and UniProtKB:P38811. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0000786 nucleosome	IDA PMID:21984211 Structure and nucleosome interaction of the yeast NuA4 and P...	MODIFY	Summary: ComplexPortal-derived nucleosome component assertion for Esa1. Reason: PMID:21984211 established the structure and nucleosome interaction of NuA4 and Piccolo NuA4, and PMID:40100634 directly resolved Piccolo NuA4 bound to nucleosomes. A molecular-function replacement, nucleosome binding, matches those assays and avoids asserting that Esa1 is part of the histone-DNA nucleosome particle itself. Proposed replacements: nucleosome binding Supporting Evidence: PMID:21984211 EM analysis of a NuA4-NCP complex shows the NCP bound at the periphery of NuA4. PMID:40100634 Here, using cryoelectron microscopy (cryo-EM) single particle analysis, we present seven cryo-EM structures of piccolo NuA4 (pNuA4) in complex with wild-type H2A.Z or H2A.Z-mutant-containing nucleosomes in the absence or presence of acetyl coenzyme A (Ac-CoA).
GO:0004402 histone acetyltransferase activity	EXP PMID:12368900 The catalytic mechanism of the ESA1 histone acetyltransferas...	ACCEPT	Summary: Direct experimental support for Esa1 histone acetyltransferase activity. Reason: Esa1 acetylates multiple histone substrates through NuA4 and Piccolo NuA4, including H4, H3, H2B, H2A, and H2A.Z, so the parent histone acetyltransferase molecular-function assertion remains correct in addition to the H4-specific rows. UniProt's curated function block summarizes the specific H4K5/8/12/16, H3K14, H2BK16, H2AK4/7, and H2A.ZK14 sites. Supporting Evidence: PMID:12368900 Yeast ESA1 is a member of the MYST subfamily of histone acetyltransferases
GO:0004402 histone acetyltransferase activity	EXP PMID:17223684 Catalytic mechanism of a MYST family histone acetyltransfera...	ACCEPT	Summary: Direct experimental support for Esa1 histone acetyltransferase activity. Reason: Esa1 acetylates multiple histone substrates through NuA4 and Piccolo NuA4, including H4, H3, H2B, H2A, and H2A.Z, so the parent histone acetyltransferase molecular-function assertion remains correct in addition to the H4-specific rows. UniProt's curated function block summarizes the specific H4K5/8/12/16, H3K14, H2BK16, H2AK4/7, and H2A.ZK14 sites. Supporting Evidence: PMID:17223684 Together, the results suggest that MYST family HATs utilize a direct-attack mechanism within an Esa1 x acetyl-CoA x histone ternary complex.
GO:0004402 histone acetyltransferase activity	EXP PMID:18245364 Catalytic-site mutations in the MYST family histone Acetyltr...	ACCEPT	Summary: Direct experimental support for Esa1 histone acetyltransferase activity. Reason: Esa1 acetylates multiple histone substrates through NuA4 and Piccolo NuA4, including H4, H3, H2B, H2A, and H2A.Z, so the parent histone acetyltransferase molecular-function assertion remains correct in addition to the H4-specific rows. UniProt's curated function block summarizes the specific H4K5/8/12/16, H3K14, H2BK16, H2AK4/7, and H2A.ZK14 sites. Supporting Evidence: PMID:18245364 Esa1 is the only essential histone acetyltransferase (HAT) in budding yeast.
GO:0004402 histone acetyltransferase activity	EXP PMID:22020126 MYST protein acetyltransferase activity requires active site...	ACCEPT	Summary: Direct experimental support for Esa1 histone acetyltransferase activity. Reason: Esa1 acetylates multiple histone substrates through NuA4 and Piccolo NuA4, including H4, H3, H2B, H2A, and H2A.Z, so the parent histone acetyltransferase molecular-function assertion remains correct in addition to the H4-specific rows. UniProt's curated function block summarizes the specific H4K5/8/12/16, H3K14, H2BK16, H2AK4/7, and H2A.ZK14 sites. Supporting Evidence: PMID:22020126 we present mass spectrometry data and biochemical experiments to demonstrate that this lysine autoacetylation on yEsa1, hMOF and its yeast orthologue, ySas2 (KAT8) occurs in solution and is required for acetylation and protein substrate binding in vitro
GO:0004402 histone acetyltransferase activity	EXP PMID:9520405 ESA1 is a histone acetyltransferase that is essential for gr...	ACCEPT	Summary: Direct experimental support for Esa1 histone acetyltransferase activity. Reason: Esa1 acetylates multiple histone substrates through NuA4 and Piccolo NuA4, including H4, H3, H2B, H2A, and H2A.Z, so the parent histone acetyltransferase molecular-function assertion remains correct in addition to the H4-specific rows. UniProt's curated function block summarizes the specific H4K5/8/12/16, H3K14, H2BK16, H2AK4/7, and H2A.ZK14 sites. Supporting Evidence: PMID:9520405 we express a yeast ORF with homology to MYST family members and show it possesses histone acetyltransferase activity
GO:0005515 protein binding	IPI PMID:15485911 The Yaf9 component of the SWR1 and NuA4 complexes is require...	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and UniProtKB:P80428. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0005515 protein binding	IPI PMID:15485911 The Yaf9 component of the SWR1 and NuA4 complexes is require...	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and UniProtKB:Q12432. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0005515 protein binding	IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine...	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and UniProtKB:P80428. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0005515 protein binding	IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine...	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and UniProtKB:Q12432. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0005515 protein binding	IPI PMID:21179020 Defining the budding yeast chromatin-associated interactome.	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and UniProtKB:P38811. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0005515 protein binding	IPI PMID:21179020 Defining the budding yeast chromatin-associated interactome.	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and UniProtKB:P80428. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0005515 protein binding	IPI PMID:21179020 Defining the budding yeast chromatin-associated interactome.	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and UniProtKB:Q12432. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0005515 protein binding	IPI PMID:24843044 Eaf5/7/3 form a functionally independent NuA4 submodule link...	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and UniProtKB:Q12432. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0005515 protein binding	IPI PMID:37968396 The social and structural architecture of the yeast protein ...	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and UniProtKB:P80428. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0005515 protein binding	IPI PMID:37968396 The social and structural architecture of the yeast protein ...	REMOVE	Summary: Generic IntAct protein-binding evidence for ESA1 and UniProtKB:Q12432. Reason: The reported interaction may be real, but GO:0005515 is a generic binding term that does not add a molecular function for ESA1. ESA1's informative activities and complex memberships are captured by the NuA4/Piccolo component rows and acetyltransferase rows, and this IPI row does not by itself support a more specific replacement molecular function.
GO:0006974 DNA damage response	IEA GO_REF:0000117	ACCEPT	Summary: ARBA electronic assertion of the DNA-damage response role. Reason: DNA double-strand break repair and damage response are established Esa1/NuA4 functions supported by multiple direct SGD DNA-repair rows, so this broad electronic DNA-damage response row is biologically consistent.
GO:0010485 histone H4 acetyltransferase activity	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic transfer of histone H4 acetyltransferase activity from the fungal Esa1/NuA4 clade. Reason: Histone H4 acetyltransferase activity is the most specific core molecular function for yeast Esa1. The current PTHR10615 PTN000834946 IBD node is a safe fungal transfer and includes direct ESA1 evidence among its seeds. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000834946 · fungal Esa1/NuA4 H4 acetyltransferase node SUPPORTS TRANSFER The current PTHR10615 fungal Esa1/NuA4 node supports histone H4 acetyltransferase activity and includes direct yeast ESA1 evidence as one of its seeds, which is expected rather than circular.
GO:0032777 piccolo histone acetyltransferase complex	IPI PMID:21984211 Structure and nucleosome interaction of the yeast NuA4 and P...	ACCEPT	Summary: ComplexPortal/Piccolo evidence that Esa1 is part of the Piccolo NuA4 HAT complex. Reason: Esa1 is the catalytic subunit of Piccolo NuA4, so this complex-membership row is core and correct. Supporting Evidence: PMID:21984211 Three NuA4 subunits (Esa1, Yng2, and Epl1) are responsible for NuA4's HAT activity, and they comprise the Piccolo-NuA4 (Piccolo) catalytic subcomplex
GO:0035267 NuA4 histone acetyltransferase complex	IPI PMID:24843044 Eaf5/7/3 form a functionally independent NuA4 submodule link...	ACCEPT	Summary: ComplexPortal evidence that Esa1 is part of the NuA4 HAT complex. Reason: Esa1 is the catalytic subunit of the NuA4 histone acetyltransferase complex, so this complex-membership row is core and correct. Supporting Evidence: PMID:38961766 NuA4 is comprised of 13 subunits, including the catalytic component, Esa1, and the scaffolding unit, Eaf1. PMID:24843044 The NuA4 histone acetyltransferase complex is required for gene regulation, cell cycle progression, and DNA repair.
GO:0061733 protein-lysine-acetyltransferase activity	EXP PMID:22539722 Function and molecular mechanism of acetylation in autophagy...	ACCEPT	Summary: Experimental UniProt assertion of Esa1 protein-lysine acetyltransferase activity. Reason: GO:0061733 is broader than the histone-specific terms and covers documented non-histone substrates such as Atg3; it is an appropriate general catalytic row for Esa1. Supporting Evidence: PMID:22539722 We further identified the autophagy signaling component Atg3 as a substrate for Esa1.
GO:0106226 peptide 2-hydroxyisobutyryltransferase activity	ISS GO_REF:0000024	UNDECIDED	Summary: Sequence-similarity transfer of peptide 2-hydroxyisobutyryltransferase activity from fission yeast Mst1. Reason: This row is transferred from Schizosaccharomyces pombe Mst1 and no direct S. cerevisiae Esa1 2-hydroxyisobutyryltransferase evidence is cited in the current GOA row. Keep unresolved until the source-side evidence and transfer to budding yeast Esa1 are reviewed.
GO:0140064 peptide crotonyltransferase activity	EXP PMID:31699900 Gcn5 and Esa1 function as histone crotonyltransferases to re...	ACCEPT	Summary: Experimental UniProt assertion of Esa1 peptide crotonyltransferase activity. Reason: This is the broad Rhea-level crotonyltransferase activity corresponding to the direct histone crotonyltransferase evidence from Fellows et al. Supporting Evidence: PMID:31699900 The Piccolo NuA4 complex, similar to the ADA complex, also exhibited crotonyltransferase activity toward nucleosomes in a manner dependent on its catalytic activity

Gene Description

Existing Annotations Review

Core Functions

Catalytic component of Piccolo NuA4 that can transfer crotonyl groups from crotonyl-CoA to nucleosomal histones, supporting crotonylation-dependent transcriptional regulation.

References

Suggested Questions for Experts

Suggested Experiments

Deep Research

Falcon

SGD

SGD gene description for ESA1 (yeast)

📚 Additional Documentation

Notes

Curation Analysis

Curation Complete

Curation Summary

Files Index

Readme Curation

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