mst1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0000785 chromatin	IBA GO_REF:0000033	ACCEPT	Summary: The eukaryotic MYST-family PAINT node correctly places Mst1 at chromatin. Reason: PANTHER:PTN004172926 is broad, but its chromatin placement is appropriate for O94446, a fungal PTHR10615:SF218 ESA1 member with direct fission-yeast evidence for Mst1 chromatin binding and chromatin histone acetyltransferase activity. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN004172926 · Eukaryotic MYST HAT ancestral node SUPPORTS TRANSFER Broad eukaryotic MYST-node chromatin assertion that transfers correctly to the fungal ESA1 subfamily. Supporting Evidence: PMID:16199868 Mst1p, but not Mst2p, is essential for viability. Both proteins are localized to the nucleus and bound to chromatin throughout the cell cycle. file:SCHPO/mst1/mst1-uniprot.txt DR PANTHER; PTHR10615:SF218; HISTONE ACETYLTRANSFERASE ESA1; 1.
GO:0000812 Swr1 complex	IDA PMID:19915592 An acetylated form of histone H2A.Z regulates chromosome arc...	REMOVE	Summary: The Swr1-complex evidence in PMID:19915592 supports the coupled SWR-C/Pht1/Mst1 pathway but not stable Mst1 membership in Swr1C. Reason: Kim et al. showed that Swr1C deposits H2A.Z/Pht1 into chromatin and that Mst1 then acetylates chromatin-associated Pht1; the same paper separates fission-yeast Swr1C from the Mst1 acetyltransferase complex. The distinct NuA4 complex is already captured by the direct GO:0035267 row, so this Swr1C membership assertion should simply be removed. Supporting Evidence: PMID:19915592 Msc1.TAP purification did not identify Mst1 (or any non-shared subunit of the Swr1 and Mst1 Complexes: Supplementary Table 1), and unique members of the Mst1-C do not co-purify Msc1
GO:0003682 chromatin binding	IBA GO_REF:0000033	ACCEPT	Summary: The eukaryotic MYST-family PAINT node gives Mst1 a broad but sound chromatin-binding assertion. Reason: PANTHER:PTN004172926 records a chromatin-binding capacity shared by nuclear MYST acetyltransferases, and S. pombe Mst1 itself is experimentally nuclear, chromatin-bound, and recruited to pericentric heterochromatin and DSB sites. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN004172926 · Eukaryotic MYST HAT ancestral node SUPPORTS TRANSFER The root-node chromatin-binding assertion remains valid for the fungal ESA1 subfamily. Supporting Evidence: PMID:16199868 Both Mst1p and Mst2p behaved like Orp1-HA: they were localized in the nucleus and bound to chromatin throughout the whole cell cycle.
GO:0003712 transcription coregulator activity	IBA GO_REF:0000033	ACCEPT	Summary: Transcription coregulator activity is an appropriate broad activity for Mst1 as a NuA4 catalytic chromatin acetyltransferase. Reason: PANTHER placed this term at the broad eukaryotic MYST node, and the transfer is valid for an ESA1/TIP60 ortholog whose acetylation of H2A.Z and H4-associated NuA4 activity are coupled to chromatin-based transcriptional regulation. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN004172926 · Eukaryotic MYST HAT ancestral node SUPPORTS TRANSFER Broad eukaryotic node supporting transcription coregulator activity for MYST/NuA4 HATs. Supporting Evidence: PMID:19915592 Thus a pathway first identified in Sc also operates in Sp: SWR-C inserts Pht1 into chromatin, where it is acetylated by Mst1. PMID:19915592 A striking observation was that almost all genes were modulated to some degree in pht1 mutants (Fig. 3b), suggesting that the histone acts as a general transcriptional regulator.
GO:0004402 histone acetyltransferase activity	EXP PMID:19915592 An acetylated form of histone H2A.Z regulates chromosome arc...	ACCEPT	Summary: Mst1 is the KAT5-family acetyltransferase responsible for acetylating chromatin-associated H2A.Z/Pht1. Reason: The mst1-L271P temperature-sensitive allele profoundly reduced Pht1 acetylation without reducing total Pht1, supporting the broad histone acetyltransferase activity term. Supporting Evidence: PMID:19915592 WCEs from mst1-L271P cells showed no appreciable change in total Pht1 levels but a profound reduction in Pht1Ac
GO:0004402 histone acetyltransferase activity	EXP PMID:20299449 A chromodomain switch mediated by histone H3 Lys 4 acetylati...	ACCEPT	Summary: Mst1 directly acetylates histone H3 at Lys-4 in the assay supporting this row. Reason: Xhemalce and Kouzarides identified H3K4ac in S. pombe, showed it was reduced in an mst1 temperature-sensitive mutant, and directly assayed purified Mst1 on histone H3, so the broad histone acetyltransferase activity row is well supported. Supporting Evidence: PMID:20299449 Importantly, the Mst1 protein purified from Bacculovirus -infected insect cells—as well as its human homolog, TIP60—directly acetylated histone H3 at K4 in an in vitro HAT assay
GO:0004402 histone acetyltransferase activity	IEA GO_REF:0000120	ACCEPT	Summary: The InterPro/Rhea automated histone acetyltransferase row is broad but matches Mst1's experimentally established chromatin HAT activity. Reason: IPR002717 marks the conserved MYST acetyltransferase domain in O94446, and direct fission-yeast experiments support Mst1-catalyzed acetylation of H2A.Z/Pht1 and H3K4 on chromatin. Supporting Evidence: file:SCHPO/mst1/mst1-uniprot.txt DR InterPro; IPR002717; HAT_MYST-type.
GO:0005634 nucleus	EXP PMID:16199868 Schizosaccharomyces pombe mst2+ encodes a MYST family histon...	KEEP AS NON CORE	Summary: Gomez et al. tagged endogenous Mst1 and localized it to the nucleus. Reason: The direct 2005 localization result showed Mst1 is nuclear and remains chromatin-bound through the cell cycle. The nucleus annotation is correct but broad and less informative than the precise chromatin, pericentric-heterochromatin, NuA4, and DSB location rows. Supporting Evidence: PMID:16199868 Both Mst1p and Mst2p behaved like Orp1-HA: they were localized in the nucleus and bound to chromatin throughout the whole cell cycle.
GO:0005634 nucleus	HDA PMID:10759889 Large-scale screening of intracellular protein localization ...	KEEP AS NON CORE	Summary: The large-scale GFP-fusion screen placed Mst1 in the nucleus. Reason: The publication cache is abstract-only and does not expose the individual Mst1 row, but this high-throughput PomBase localization agrees with the direct endogenous tagging in PMID:16199868 and with Mst1's chromatin HAT function. It should be retained as a broad, non-core nuclear-localization row. Supporting Evidence: file:SCHPO/mst1/mst1-uniprot.txt Nucleus {ECO:0000269\|PubMed:10759889, CC ECO:0000269\|PubMed:16199868}
GO:0005634 nucleus	HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ...	KEEP AS NON CORE	Summary: The ORFeome localization screen independently supports nuclear Mst1. Reason: The cached record is abstract-only and cannot be used to verify the SPAC637.12c image directly, but the screened nuclear localization is consistent with direct Mst1 localization and with UniProt's curated nuclear subcellular-location statement. The row is correct but broad relative to the more specific chromatin and complex localizations. Supporting Evidence: file:SCHPO/mst1/mst1-uniprot.txt Nucleus {ECO:0000269\|PubMed:10759889, CC ECO:0000269\|PubMed:16199868}
GO:0005634 nucleus	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: The eukaryotic MYST-family PAINT node correctly transfers nuclear localization to Mst1. Reason: PANTHER:PTN004172926 places MYST acetyltransferases in the nucleus, and S. pombe Mst1 has its own direct PomBase evidence for nuclear localization and chromatin binding. This IBA is sound but reports the shared broad compartment rather than a specific core chromatin site. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN004172926 · Eukaryotic MYST HAT ancestral node SUPPORTS TRANSFER Nuclear localization is conserved for chromatin-regulatory MYST HATs and is directly supported in the target species. Supporting Evidence: PMID:16199868 Mst1p, but not Mst2p, is essential for viability. Both proteins are localized to the nucleus and bound to chromatin throughout the cell cycle.
GO:0005634 nucleus	IEA GO_REF:0000044	KEEP AS NON CORE	Summary: The UniProt subcellular-location mapping to the nucleus agrees with direct fission-yeast localization evidence. Reason: UniProt's nuclear localization statement is backed by the Ding 2000 GFP screen and the Gomez 2005 endogenous Mst1 localization, so the electronic mapping is correct. The mapped parent compartment is non-core relative to direct chromatin and damage-site locations. Supporting Evidence: file:SCHPO/mst1/mst1-uniprot.txt Nucleus {ECO:0000269\|PubMed:10759889, CC ECO:0000269\|PubMed:16199868}
GO:0005694 chromosome	EXP PMID:20299449 A chromodomain switch mediated by histone H3 Lys 4 acetylati...	KEEP AS NON CORE	Summary: H3K4ac, the product of Mst1 activity, is enriched at pericentric repeats. Reason: This localization row is a broad chromosome component assertion for the Mst1 activity detected at pericentric heterochromatin in ChIP assays, and is consistent with Mst1's chromatin association. It should be retained as a valid non-core parent of the more precise pericentric row. Supporting Evidence: PMID:20299449 H3K4ac was enriched specifically at the pericentric repeats compared with the euchromatic ura4-DS/E or adh1 gene PMID:20299449 Moreover, the acetyltransferase Mst1 was modestly enriched at the pericentric repeats
GO:0005694 chromosome	EXP PMID:33723569 Schizosaccharomyces pombe KAT5 contributes to resection and ...	KEEP AS NON CORE	Summary: Mst1 is recruited to chromosomal double-strand breaks. Reason: Li et al. directly localized Mst1 to an induced DSB and then showed that mst1 mutations disrupt downstream repair-protein recruitment and resection. The broad chromosome parent is correct but less informative than the site-of-DSB row. Supporting Evidence: PMID:33723569 Here we show that Mst1 is recruited to DSBs. Mutation of mst1 + disrupts recruitment of repair proteins and delays resection.
GO:0005694 chromosome	IEA GO_REF:0000044	KEEP AS NON CORE	Summary: UniProt's chromosome mapping follows curated pericentric and DSB localization evidence. Reason: The chromosome term is broader than the specific Mst1 pools at pericentric heterochromatin and DSBs, but it is a valid parent-level localization for those chromosomal sites and should be kept as non-core. Supporting Evidence: file:SCHPO/mst1/mst1-uniprot.txt Chromosome {ECO:0000269\|PubMed:20299449, CC ECO:0000269\|PubMed:33723569}. Note=Localizes to pericentric CC heterochromatin (PubMed:20299449). Following DNA damage, localizes to CC sites of DNA damage, such as double strand breaks (DSBs) CC (PubMed:33723569).
GO:0005721 pericentric heterochromatin	IDA PMID:20299449 A chromodomain switch mediated by histone H3 Lys 4 acetylati...	ACCEPT	Summary: Mst1-catalyzed H3K4ac is enriched at pericentric heterochromatin during heterochromatin reassembly. Reason: The ChIP and mst1 temperature-sensitive data show Mst1 activity at the pericentric repeats, so this is an appropriately specific location for the H3K4 acetyltransferase role. Supporting Evidence: PMID:20299449 Moreover, the acetyltransferase Mst1 was modestly enriched at the pericentric repeats
GO:0006355 regulation of DNA-templated transcription	IEA GO_REF:0000002	MODIFY	Summary: The InterPro transcription-regulation transfer is valid but could be refined to the polymerase II-specific child term. Reason: Mst1 regulates chromatin for nuclear RNA polymerase II transcription through NuA4/H2A.Z acetylation, and the PAINT project already places the more precise GO:0006357 term on this protein from the MYST root node. Proposed replacements: regulation of transcription by RNA polymerase II Supporting Evidence: PMID:19915592 A striking observation was that almost all genes were modulated to some degree in pht1 mutants (Fig. 3b), suggesting that the histone acts as a general transcriptional regulator.
GO:0006357 regulation of transcription by RNA polymerase II	IBA GO_REF:0000033	ACCEPT	Summary: The MYST root-node PAINT process row correctly transfers broad Pol II-transcription regulation to Mst1. Reason: PANTHER:PTN004172926 is a broad eukaryotic node, but this process term is likewise broad and follows from the conserved role of MYST/NuA4 HATs in chromatin-based transcriptional regulation. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN004172926 · Eukaryotic MYST HAT ancestral node SUPPORTS TRANSFER The Pol II-transcription process assertion is broad enough to apply to fungal ESA1/TIP60-family NuA4 catalytic subunits. Supporting Evidence: PMID:19915592 Thus a pathway first identified in Sc also operates in Sp: SWR-C inserts Pht1 into chromatin, where it is acetylated by Mst1. PMID:19915592 A striking observation was that almost all genes were modulated to some degree in pht1 mutants (Fig. 3b), suggesting that the histone acts as a general transcriptional regulator.
GO:0010485 histone H4 acetyltransferase activity	IBA GO_REF:0000033	ACCEPT	Summary: The 2026 fungal PAINT node appropriately transfers H4 acetyltransferase activity to the ESA1 subfamily. Reason: PANTHER:PTN000834946 is placed within fungi on the PTHR10615:SF218 ESA1 clade, and O94446 is the S. pombe member of that clade. The annotation is more specific than the root MYST histone acetyltransferase row and captures the conserved ESA1/NuA4 catalytic activity. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000834946 · Fungal ESA1 H4 HAT ancestral node SUPPORTS TRANSFER Fungal node supporting histone H4 acetyltransferase activity for ESA1-family members, including S. pombe Mst1. Supporting Evidence: file:SCHPO/mst1/mst1-uniprot.txt DR PANTHER; PTHR10615:SF218; HISTONE ACETYLTRANSFERASE ESA1; 1.
GO:0010485 histone H4 acetyltransferase activity	ISO GO_REF:0000024	ACCEPT	Summary: The older budding-yeast ESA1 ISO transfer agrees with the newer PAINT H4 transfer. Reason: PomBase's ISO from budding-yeast ESA1 lands on the same H4 acetyltransferase activity now placed by PAINT at a fungal ESA1 node, so the conserved enzymatic assertion is sound for Mst1. Propagation Review Root cause: NO FAILURE CORE Sources checked: SGD:S000005770 · ESA1 SUPPORTS TRANSFER Budding-yeast ESA1 is the experimentally characterized orthologous H4 acetyltransferase and supports this conserved ISO transfer. Supporting Evidence: file:SCHPO/mst1/mst1-uniprot.txt DR PANTHER; PTHR10615:SF218; HISTONE ACETYLTRANSFERASE ESA1; 1.
GO:0031453 positive regulation of heterochromatin formation	IMP PMID:20299449 A chromodomain switch mediated by histone H3 Lys 4 acetylati...	ACCEPT	Summary: Mst1-dependent H3K4 acetylation directly contributes to pericentric heterochromatin reassembly. Reason: Xhemalce and Kouzarides showed that Mst1 is the major H3K4 acetyltransferase, that H3K4ac occurs at pericentric repeats, and that H3K4R causes centromeric desilencing by altering the Chp1/Swi6/Chp2 chromodomain switch. Supporting Evidence: PMID:20299449 H3K4ac, mediated by Mst1, is enriched at pericentromeres concomitantly with heterochromatin reassembly. PMID:20299449 H3K4R (Lys → Arg) mutation increases Chp1 and decreases Chp2/Swi6 pericentric occupancy and exhibits centromeric desilencing.
GO:0035267 NuA4 histone acetyltransferase complex	IDA PMID:19040720 Chromatin Central: towards the comparative proteome by accur...	ACCEPT	Summary: Comparative affinity purification places fission-yeast Mst1 in NuA4, not Swr1C. Reason: PMID:19040720 identified Mst1/SPAC637.12c as the fission-yeast ortholog of S. cerevisiae Esa1 in the NuA4 histone acetyltransferase complex, and the Mst1-Swr1C functional connection in PMID:19915592 is explained by Swr1C-mediated Pht1 deposition followed by Mst1 acetylation. Supporting Evidence: PMID:19040720 Complex IV (Sp_NuA4) comprises orthologues of the 12 core members of the Sc_NuA4 complex, including its catalytic subunit Sp_Mst1p (ORF name SPAC637.12c)
GO:0035861 site of double-strand break	IDA PMID:33723569 Schizosaccharomyces pombe KAT5 contributes to resection and ...	ACCEPT	Summary: Mst1 is directly recruited to double-strand breaks. Reason: The 2021 Genetics study localized Mst1 to a chromosomal HO-induced DSB and connected Mst1 function to resection and repair-protein recruitment. Supporting Evidence: PMID:33723569 Here we show that Mst1 is recruited to DSBs. Mutation of mst1 + disrupts recruitment of repair proteins and delays resection.
GO:0044016 histone H3K4 acetyltransferase activity	IDA PMID:20299449 A chromodomain switch mediated by histone H3 Lys 4 acetylati...	ACCEPT	Summary: Mst1 directly acetylates histone H3 at Lys-4. Reason: This is the exact molecular activity identified by the 2010 H3K4ac study: purified Mst1 directly acetylated H3K4 in vitro, and the modification was strongly reduced in an mst1 temperature-sensitive mutant in cells. Supporting Evidence: PMID:20299449 Importantly, the Mst1 protein purified from Bacculovirus -infected insect cells—as well as its human homolog, TIP60—directly acetylated histone H3 at K4 in an in vitro HAT assay
GO:0061733 protein-lysine-acetyltransferase activity	IEA GO_REF:0000120	ACCEPT	Summary: The Rhea protein-lysine acetyltransferase row is a broad but correct parent of Mst1's histone-lysine acetyltransferase activity. Reason: Histone lysines are protein lysines, and the EC/Rhea transfer agrees with direct fission-yeast evidence that Mst1 acetylates histone H3K4 and H2A.Z/Pht1. Supporting Evidence: PMID:20299449 Importantly, the Mst1 protein purified from Bacculovirus -infected insect cells—as well as its human homolog, TIP60—directly acetylated histone H3 at K4 in an in vitro HAT assay
GO:0061733 protein-lysine-acetyltransferase activity	ISS GO_REF:0000024	ACCEPT	Summary: Orthology to budding-yeast ESA1 supports broad protein-lysine acetyltransferase activity. Reason: The transferred term is less specific than the curated histone-specific Mst1 rows but is not biologically wrong, because Mst1 is an ESA1-family lysine acetyltransferase. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:Q08649 · ESA1 SUPPORTS TRANSFER The S. cerevisiae ESA1 ortholog supports the general protein-lysine acetyltransferase capacity inherited by fungal Mst1. Supporting Evidence: file:SCHPO/mst1/mst1-uniprot.txt CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] CC + CoA + H(+); Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA- CC COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; CC Evidence={ECO:0000250\|UniProtKB:Q08649}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949; CC Evidence={ECO:0000250\|UniProtKB:Q08649};
GO:0106226 peptide 2-hydroxyisobutyryltransferase activity	EXP PMID:29192674 Landscape of the regulatory elements for lysine 2-hydroxyiso...	MARK AS OVER ANNOTATED	Summary: The 2018 acyltransferase paper supports this chemistry for the ESA1/TIP60 lineage but did not directly test S. pombe Mst1. Reason: Huang et al. assayed budding-yeast Esa1 and human TIP60, showing that the conserved active site can use 2-hydroxyisobutyryl-CoA on H4 substrates. This supports an ESA1/TIP60-family secondary acyltransferase capacity, but the paper provides no fission-yeast experiment, so the GOA EXP row overstates the evidence when read as direct support for S. pombe Mst1. Supporting Evidence: PMID:29192674 Here we show that Esa1p in budding yeast and its homologue Tip60 in human could add K hib to substrate proteins both in vitro and in vivo
GO:0106226 peptide 2-hydroxyisobutyryltransferase activity	IEA GO_REF:0000116	MARK AS OVER ANNOTATED	Summary: The Rhea 2-hydroxyisobutyryltransferase transfer extrapolates from budding-yeast and human ESA1/TIP60-family assays. Reason: The Rhea mapping is chemically consistent with ESA1/TIP60-family substrate flexibility, but the cited literature establishes this non-acetyl acyltransferase activity for S. cerevisiae Esa1 and human TIP60 rather than directly for S. pombe Mst1, so the electronic transfer is plausible but over-asserted as a direct Mst1 activity. Supporting Evidence: PMID:29192674 Esa1p's human homolog Tip60, a well-known MYST family acetyltransferase member 25 , is also identified as a “writer” able to catalyze K hib in mammalian cells both in vitro and in vivo .
GO:0120261 regulation of heterochromatin organization	IEA GO_REF:0000117	MODIFY	Summary: Regulation of heterochromatin organization is supported, but the direct PomBase row is more specific. Reason: This ARBA process transfer is broader and less informative than the direct H3K4ac/positive heterochromatin-formation annotation, but it captures a demonstrated S. pombe role of Mst1 in pericentric heterochromatin reassembly and should be replaced by the polarity-bearing PomBase child term. Proposed replacements: positive regulation of heterochromatin formation Supporting Evidence: PMID:20299449 H3K4ac mediates a chromodomain switch from Chp1/Clr4 to Swi6/Chp2 to allow heterochromatin reassembly.
GO:0140064 peptide crotonyltransferase activity	IEA GO_REF:0000116	KEEP AS NON CORE	Summary: Crotonyltransferase activity is an orthology/Rhea-based secondary acyltransferase inference. Reason: UniProt infers Mst1 crotonyl-CoA use by similarity to budding-yeast ESA1. This is plausible for a MYST-family acyltransferase but is not directly supported for S. pombe in the cached Mst1 papers. Supporting Evidence: file:SCHPO/mst1/mst1-uniprot.txt CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-butenoyl-CoA + L-lysyl-[protein] = N(6)-(2E)-butenoyl-L- CC lysyl-[protein] + CoA + H(+); Xref=Rhea:RHEA:53908, Rhea:RHEA- CC COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57332, CC ChEBI:CHEBI:137954; Evidence={ECO:0000250\|UniProtKB:Q08649}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53909; CC Evidence={ECO:0000250\|UniProtKB:Q08649};
GO:0140064 peptide crotonyltransferase activity	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: The manual ortholog transfer of crotonyltransferase activity is plausible but remains secondary to the established HAT function. Reason: The S. cerevisiae ESA1 source supports a conserved secondary acyltransferase capacity, but GOA has no direct S. pombe crotonyl-CoA assay, so this row should be retained as non-core. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:Q08649 · ESA1 SUPPORTS TRANSFER Budding-yeast ESA1 is the ortholog used for this conservative secondary acyltransferase transfer. Supporting Evidence: file:SCHPO/mst1/mst1-uniprot.txt CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-butenoyl-CoA + L-lysyl-[protein] = N(6)-(2E)-butenoyl-L- CC lysyl-[protein] + CoA + H(+); Xref=Rhea:RHEA:53908, Rhea:RHEA- CC COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57332, CC ChEBI:CHEBI:137954; Evidence={ECO:0000250\|UniProtKB:Q08649}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53909; CC Evidence={ECO:0000250\|UniProtKB:Q08649};
GO:0140065 peptide butyryltransferase activity	IDA PMID:29192674 Landscape of the regulatory elements for lysine 2-hydroxyiso...	REMOVE	Summary: PMID:29192674 does not directly support peptide butyryltransferase activity for Mst1. Reason: The cited study assayed 2-hydroxyisobutyryl-CoA use by S. cerevisiae Esa1 and human TIP60; the cached full text does not report a butyryl-CoA assay for S. pombe Mst1. This row is therefore unsupported, in contrast to the separate 2-hydroxyisobutyryltransferase assertions. Supporting Evidence: PMID:29192674 Here we show that Esa1p in budding yeast and its homologue Tip60 in human could add K hib to substrate proteins both in vitro and in vivo
GO:0140861 DNA repair-dependent chromatin remodeling	IMP PMID:33723569 Schizosaccharomyces pombe KAT5 contributes to resection and ...	ACCEPT	Summary: Mst1 directly contributes to DSB-repair chromatin remodeling. Reason: Li et al. showed that Mst1 is recruited to a chromosomal DSB and that mst1 mutants disrupt repair-protein recruitment and resection. The newer W66R chromodomain study supports a related but separable Mst1 role in CPT-induced damage repair. Supporting Evidence: PMID:33723569 Taken together, our data suggest that SpMst1contributes to repair of a variety of DNA lesions. PMID:38662722 Our data further suggest that Mst1 is required for the global response to CPT and assembly of appropriate repair proteins.

Gene Description

Existing Annotations Review

Core Functions

Mst1 is the fission-yeast ESA1/TIP60 catalytic subunit of NuA4 and acetylates histones on chromatin, including H4-family substrates and H2A.Z/Pht1, to regulate RNA polymerase II transcription.

At pericentric heterochromatin, Mst1 acetylates histone H3K4 and promotes the chromodomain-protein switch that allows Swi6/Chp2-mediated heterochromatin reassembly.

Mst1 is recruited to DNA double-strand breaks and promotes chromatin remodeling needed for efficient repair-protein recruitment and long-range resection.

References

Suggested Questions for Experts

Suggested Experiments

📚 Additional Documentation

Notes

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