ESCO2

Summary: ESCO2 has a conserved, directly supported chromatin location.

Reason: The official PTHR45884 tree places human ESCO2 leaf PTN002476323 below IBD node PTN000118027; its ungapped MSA matches the displayed 601-residue sequence. The current IBD assertion is present and no family NOT branch interrupts the target path. The node represents an ancestral functional inference, not a pairwise donor count. Human ESCO2 is recovered in the chromosome fraction in PMID:15958495 Figures 5–6 and in S-phase chromatin in PMID:19907496 Figure 3d. The 2005 localization changes during the cell cycle: tagged ESCO2 is nuclear in interphase, excluded from metaphase chromosomes, and reassociates in telophase. Endogenous antibodies in that study cross-reacted, so tagged imaging and fractionation are distinguished. The 601-residue product and engineered fragments do not establish localization of the natural 239-residue product.

Summary: Human ESCO2 associates with chromatin during S phase.

Reason: PMID:19907496, Figure 3d and the accompanying Results, directly detects ESCO2 in the chromatin fraction of S-phase human cells, alongside the soluble-fraction comparison; DCC1 loss does not abolish this targeting. This is consistent with endogenous HeLa/293T fractionation and tagged human EFO2 localization in PMID:15958495 Figures 5–6. Chromatin is the supported substrate-associated compartment. These experiments do not separately test the current 239-residue product, and the 2005 C-terminal fragments differ from the full 601-residue protein. Public locators: https://doi.org/10.1038/nature08550, Figure 3d; https://doi.org/10.1091/mbc.e04-12-1063, Figures 5–6.

Summary: Retain the conserved meiotic XY-body localization as contextual evidence.

Reason: The donor is mouse Esco2 Q8CIB9, whose official Ensembl protein cross-reference matches the imported ENSMUSP00000022613 identifier. Its IDA source PMID:22699483 Methods and Figure 2 examine postnatal mouse spermatocyte spreads with ESCO2, SYCP3 and H2AFX antibodies; early and late pachytene ESCO2 colocalizes with the XY-body marker. This is positive localization evidence, not a demonstrated meiotic catalytic mechanism or a new human assay. The specialized germ-cell location is retained as non-core with explicit ortholog and stage limits. It does not imply equivalent localization of both human products.

Summary: Correct the donor/acceptor chemistry to protein-lysine acetyltransferase activity.

Reason: The current GO:0004468 definition specifies acetyl phosphate and free L-lysine; GO:0061733 instead specifies acetyl-CoA and a protein lysyl residue. The mouse IMP in PMID:22101327 measures reduced chromatin Smc3 K105/K106 acetylation after Esco2 deletion (Results 25, Figure 7), not an acetyl-phosphate/free-lysine reaction. Independent human PMID:15958495 Figure 2A measures autoacetylation of the purified ESCO2 215–601 fragment using radiolabeled acetyl-CoA. That experiment does not identify the modified residue; human PMID:21111234 Figure 3A/B independently shows the ESCO1/2-dependent protein-lysine endpoint on SMC3. The purified-enzyme experiment in the latter paper uses ESCO1 and Xenopus chromatin and is not relabeled as an ESCO2 reconstitution. This is a reaction-class correction, not evidence that the ortholog lacks acetyltransferase activity. The imported term and donor identifiers remain unchanged.

Proposed replacements: protein-lysine-acetyltransferase activity

Summary: HuRI supports an ESCO2–FXR1 interaction in the tested yeast two-hybrid system.

Reason: PMID:32296183 and its public HuRI PSI table contain the exact pair: ESCO2 clone 100014712, mapped to Q56NI9-1, and FXR1 clone 100002625. The validated-two-hybrid record is line 153434, with screens 1 and 3; corresponding screening records are also present. Both reagents are human proteins tested in Saccharomyces cerevisiae. The original table preserves partner isoform P51114-2. The original describes quadruplicate pairwise retesting and sequence confirmation; it does not establish that this particular pair was independently positive in every orthogonal assay or functions endogenously in ESCO2-mediated cohesion. No evidence-backed specific molecular function follows from this pair alone, so the supported interaction is retained as non-core. Neither the unsequenced clone boundary nor the untested 239-residue ESCO2 product is assumed equivalent to the displayed product. Public locators: https://doi.org/10.1038/s41586-020-2188-x, Generation and characterization of HuRI; https://interactome-atlas.org/data/HuRI.psi, exact clone pair.

Summary: HuRI supports an ESCO2–GOLGA2 interaction in the tested yeast two-hybrid system.

Reason: PMID:32296183 and its public HuRI PSI table contain the exact pair: ESCO2 clone 100014712, mapped to Q56NI9-1, and GOLGA2 clone 14862. The validated-two-hybrid record is line 144815, with screens 1; corresponding screening records are also present. Both reagents are human proteins tested in Saccharomyces cerevisiae. The partner is represented in the original table as ENSP00000476265.1, with gene ENSG00000167110.17; the current official Q08379 record independently links the same stable Ensembl gene ENSG00000167110. Exact clone-sequence equivalence to a current GOLGA2 isoform is not established. The original describes quadruplicate pairwise retesting and sequence confirmation; it does not establish that this particular pair was independently positive in every orthogonal assay or functions endogenously in ESCO2-mediated cohesion. No evidence-backed specific molecular function follows from this pair alone, so the supported interaction is retained as non-core. Neither the unsequenced clone boundary nor the untested 239-residue ESCO2 product is assumed equivalent to the displayed product. Public locators: https://doi.org/10.1038/s41586-020-2188-x, Generation and characterization of HuRI; https://interactome-atlas.org/data/HuRI.psi, exact clone pair.

Summary: HuRI supports an ESCO2–RABEP1 interaction in the tested yeast two-hybrid system.

Reason: PMID:32296183 and its public HuRI PSI table contain the exact pair: ESCO2 clone 100014712, mapped to Q56NI9-1, and RABEP1 clone 11256. The validated-two-hybrid record is line 50813, with screens 3; corresponding screening records are also present. Both reagents are human proteins tested in Saccharomyces cerevisiae. The original table maps the partner to Q15276-1; the imported unsuffixed partner identifier is preserved. The original describes quadruplicate pairwise retesting and sequence confirmation; it does not establish that this particular pair was independently positive in every orthogonal assay or functions endogenously in ESCO2-mediated cohesion. No evidence-backed specific molecular function follows from this pair alone, so the supported interaction is retained as non-core. Neither the unsequenced clone boundary nor the untested 239-residue ESCO2 product is assumed equivalent to the displayed product. Public locators: https://doi.org/10.1038/s41586-020-2188-x, Generation and characterization of HuRI; https://interactome-atlas.org/data/HuRI.psi, exact clone pair.

Summary: HuRI supports an ESCO2–PICK1 interaction in the tested yeast two-hybrid system.

Reason: PMID:32296183 and its public HuRI PSI table contain the exact pair: ESCO2 clone 100014712, mapped to Q56NI9-1, and PICK1 clone 100000407. The validated-two-hybrid record is line 64560, with screens 3; corresponding screening records are also present. Both reagents are human proteins tested in Saccharomyces cerevisiae. The original table maps the partner to Q9NRD5-1; the imported unsuffixed partner identifier is preserved. The original describes quadruplicate pairwise retesting and sequence confirmation; it does not establish that this particular pair was independently positive in every orthogonal assay or functions endogenously in ESCO2-mediated cohesion. No evidence-backed specific molecular function follows from this pair alone, so the supported interaction is retained as non-core. Neither the unsequenced clone boundary nor the untested 239-residue ESCO2 product is assumed equivalent to the displayed product. Public locators: https://doi.org/10.1038/s41586-020-2188-x, Generation and characterization of HuRI; https://interactome-atlas.org/data/HuRI.psi, exact clone pair.

Summary: Full-length human EFO2/ESCO2 is nuclear in interphase.

Reason: PMID:15958495, Results EFO1 and EFO2 Are Chromosome Binding Proteins and Figure 5E, places HA3-tagged human EFO2 inside interphase nuclei, with exclusion from metaphase chromosomes and reassociation in telophase. The source used tagged immunofluorescence because antibodies to native proteins cross-reacted. Fractionation separately found much endogenous ESCO2 on chromosomes and little soluble nucleoplasmic signal; it therefore does not justify replacing nucleus with soluble nucleoplasm. The broad nuclear location is sound, without asserting cell-cycle invariant localization or extending the assay to the current 239-residue product. Public locator: https://doi.org/10.1091/mbc.e04-12-1063, Methods Tissue Culture/Cellular Fractionation, Figures 5–6.

Summary: The inherited nuclear localization is supported.

Reason: The official PTHR45884 tree places human ESCO2 leaf PTN002476323 below IBD node PTN000118027; its ungapped MSA matches the displayed 601-residue sequence. The current IBD assertion is present and no family NOT branch interrupts the target path. The node represents an ancestral functional inference, not a pairwise donor count. Nuclear localization is supported across interphase imaging, chromatin fractionation and HPA antibody imaging. Because chromatin-associated and microscopically nucleoplasmic signals occur in distinct assays and conditions, the broad nucleus annotation remains a useful supported compartment rather than being replaced by one exclusive subnuclear location. No claim of constitutive nuclear residence or short-product equivalence is made. Human ESCO2 is recovered in the chromosome fraction in PMID:15958495 Figures 5–6 and in S-phase chromatin in PMID:19907496 Figure 3d. The 2005 localization changes during the cell cycle: tagged ESCO2 is nuclear in interphase, excluded from metaphase chromosomes, and reassociates in telophase. Endogenous antibodies in that study cross-reacted, so tagged imaging and fractionation are distinguished. The 601-residue product and engineered fragments do not establish localization of the natural 239-residue product.

Summary: The UniProt nuclear-location mapping agrees with human evidence.

Reason: The actual Q56NI9 UniProt subcellular-location record maps SL-0191 to nucleus and cites PMID:15958495 and PMID:19907496. Nuclear localization is supported across interphase imaging, chromatin fractionation and HPA antibody imaging. Because chromatin-associated and microscopically nucleoplasmic signals occur in distinct assays and conditions, the broad nucleus annotation remains a useful supported compartment rather than being replaced by one exclusive subnuclear location. No claim of constitutive nuclear residence or short-product equivalence is made. Human ESCO2 is recovered in the chromosome fraction in PMID:15958495 Figures 5–6 and in S-phase chromatin in PMID:19907496 Figure 3d. The 2005 localization changes during the cell cycle: tagged ESCO2 is nuclear in interphase, excluded from metaphase chromosomes, and reassociates in telophase. Endogenous antibodies in that study cross-reacted, so tagged imaging and fractionation are distinguished. The 601-residue product and engineered fragments do not establish localization of the natural 239-residue product.

Summary: Human ESCO2 has positive nucleoplasmic immunofluorescence evidence.

Reason: The HPA target record and inspected U2OS images from HPA027243 and HPA053679 provide positive nucleoplasmic immunofluorescence evidence. Their antigens map to canonical ESCO2 residues 313–395 and 4–86. This additional, imaging-defined location is retained as non-core: the principal cohesion/acetylation role is localized more specifically to chromatin by human fractionation and functional studies. GO:0005654 excludes chromosomes, so the staining category is not substituted for the chromatin activity site. Little soluble nucleoplasmic ESCO2 in PMID:15958495 Figure 5A does not negate all other imaging conditions. The two assays have different operational resolutions; neither resolves the natural short product.

Summary: The actual human ESCO2 reaction participant has a nucleoplasm location.

Reason: Reactome 2468039 reaches catalyst 2468053, ESCO1/ESCO2 set 2468046 and human ESCO2 member 2466400 (Q56NI9, residues 1–601). The target entity itself carries GO:0005654; this is a verified source location, not an inference from a parent event. Retain it as a non-core modeled compartment, supported independently by HPA nuclear imaging. The modeled SMC3 substrate and human PMID:15958495/19907496 experiments locate the main acetylation/cohesion role on chromatin. Nucleoplasm is not a parent compartment of chromosomes, and the model is not evidence that a soluble nucleoplasmic pool performs that reaction. Neither the valid target path nor the positive HPA observation is rejected.

Summary: The actual human ESCO2 reaction participant has a nucleoplasm location.

Reason: Reactome 2473152 reaches catalyst 2468053, ESCO1/ESCO2 set 2468046 and human ESCO2 member 2466400 (Q56NI9, residues 1–601). The target entity itself carries GO:0005654; this is a verified source location, not an inference from a parent event. Retain it as a non-core modeled compartment, supported independently by HPA nuclear imaging. The modeled SMC3 substrate and human PMID:15958495/19907496 experiments locate the main acetylation/cohesion role on chromatin. Nucleoplasm is not a parent compartment of chromosomes, and the model is not evidence that a soluble nucleoplasmic pool performs that reaction. Neither the valid target path nor the positive HPA observation is rejected.

Summary: Specify chromatin association of interphase ESCO2.

Reason: PMID:15958495 Figures 5A and 6B and their Results show endogenous human ESCO2 in the chromosome-associated fraction and N-terminal-dependent association of tagged EFO2 constructs. The full-length source protein is 601 residues; its C-terminal catalytic fragments alone were soluble. PMID:19907496 Figure 3d independently identifies chromatin-associated ESCO2 in S-phase human cells. GO:0000785 chromatin names the DNA–protein material associated with ESCO2 more precisely than the whole chromosome and is linked to GO:0005694 through part_of, not is_a. This does not imply a constitutive metaphase-chromosome constituent or direct DNA recognition from fractionation alone. Public locators: https://doi.org/10.1091/mbc.e04-12-1063, Figures 5–6; https://doi.org/10.1038/nature08550, Figure 3d.

Proposed replacements: chromatin

Summary: Refine the chromosome location to chromatin.

Reason: The official Q56NI9 SL-0468 mapping is grounded in the human localization studies. Human ESCO2 is recovered in the chromosome fraction in PMID:15958495 Figures 5–6 and in S-phase chromatin in PMID:19907496 Figure 3d. The 2005 localization changes during the cell cycle: tagged ESCO2 is nuclear in interphase, excluded from metaphase chromosomes, and reassociates in telophase. Endogenous antibodies in that study cross-reacted, so tagged imaging and fractionation are distinguished. The 601-residue product and engineered fragments do not establish localization of the natural 239-residue product. The replacement describes the chromosome material actually associated with ESCO2; chromatin is part_of chromosome, not an is_a subtype.

Proposed replacements: chromatin

Summary: Retain the conserved pericentric heterochromatin localization.

Reason: The official mouse Q8CIB9/ENSMUSP00000022613 mapping leads to IDA PMID:22101327. Actual Results 14–16 and Figures 3–4 show Esco2 enrichment at pericentric heterochromatin in mid-to-late S phase, using cortical progenitors/MEFs, Pcna and Hp1-alpha markers, DAPI-rich foci and major-satellite ChIP. The original distinguishes pericentric chromatin from the centromere core; the term is not broadened to every centromeric site. This positive ortholog evidence is biologically consistent with the human cohesion/chromatin role, but is not a direct human short-product localization assay.

Summary: Specify positive regulation of replication-fork progression.

Reason: PMID:19907496 Figure 3e measures reduced fork velocity in cells from two Roberts syndrome patients; Figure 4e independently shows slowing after ESCO2 RNAi in human HeLa cells and reversal after WAPL or PDS5A depletion. The Results relate this to the acetylation state of cohesin, supported by the non-acetylatable SMC3 comparison. Thus ESCO2 promotes replication progression through protein acetylation and cohesin regulation, rather than executing DNA polymerization. GO:0045740 captures the experimentally positive direction of the imported regulation term. The proposed fork-occlusion geometry remains a model, and the data do not show that every ESCO2 product has this effect. Public locator: https://doi.org/10.1038/nature08550, Figures 3e and 4c–e and Methods Summary (IdU/CldU fiber measurements).

Proposed replacements: positive regulation of DNA replication

Summary: Refine the cohesion process to mitotic sister-chromatid cohesion.

Reason: Reactome R-HSA-2468052 models S-phase establishment of mitotic cohesion through SMC3 acetylation, with its catalyst set explicitly containing human ESCO2. GO:0007064 is the supported mitotic descendant of the broader GO:0007062 and is already present independently. Human PMID:15958495 Figure 3 shows cohesion defects after ESCO2 depletion, while mouse PMID:22101327 Figures 6–7 links Esco2 loss to pericentric cohesion defects, reduced Smc3 K105/K106 acetylation and reduced Sororin recruitment. ESCO2 performs acetyl-transfer work in this process. The overlapping contribution measured by the specific combined-depletion HeLa immunoblot in PMID:21111234 Figure 3A does not imply general functional interchangeability with ESCO1.

Proposed replacements: mitotic sister chromatid cohesion

Summary: The ancestral mitotic cohesion role is supported.

Reason: The official PTHR45884 tree places human ESCO2 PTN002476323 below the current positive IBD node PTN000118027; the ungapped MSA matches the 601-residue target and no family NOT branch interrupts inheritance. The donor list represents a curator’s ancestral inference, not a pairwise donor-count test. Independent human PMID:15958495 Figure 3 shows cohesion defects after either ESCO1 or ESCO2 depletion, and mouse PMID:22101327 Figures 6–7 establishes an Esco2-specific requirement for pericentric cohesion, Smc3 acetylation and Sororin association. This supports the mitotic-cohesion assertion without claiming general ESCO1/ESCO2 redundancy. The combined-depletion result in PMID:21111234 Figure 3A concerns a particular S-phase HeLa chromatin-SMC3 immunoblot.

Summary: Specify protein-lysine acetyltransferase activity for the modeled SMC3 reaction.

Reason: Reactome 2468039 supplies acetyl-CoA and chromatin-associated cohesin, produces acetylated cohesin and CoA, and assigns catalyst 2468053 to set 2468046 containing human ESCO2 2466400. GO:0061733 is the protein-lysine-specific descendant of the broad N-acetyltransferase term and matches this reaction. Independent human ESCO2-fragment autoacetylation in PMID:15958495 Figure 2A establishes acetyl-CoA transfer, while human PMID:21111234 Figure 3A/B and mouse PMID:22101327 Figure 7 establish the SMC3 lysine endpoint. The human combined-depletion endpoint is distinct from the mouse Esco2-only loss and from the separate ESCO1/Xenopus reconstitution.

Proposed replacements: protein-lysine-acetyltransferase activity

Summary: Specify protein-lysine acetyltransferase activity for the modeled SMC3 reaction.

Reason: Reactome 2473152 supplies acetyl-CoA and chromatin-associated cohesin, produces acetylated cohesin and CoA, and assigns catalyst 2468053 to set 2468046 containing human ESCO2 2466400. GO:0061733 is the protein-lysine-specific descendant of the broad N-acetyltransferase term and matches this reaction. Independent human ESCO2-fragment autoacetylation in PMID:15958495 Figure 2A establishes acetyl-CoA transfer, while human PMID:21111234 Figure 3A/B and mouse PMID:22101327 Figure 7 establish the SMC3 lysine endpoint. The human combined-depletion endpoint is distinct from the mouse Esco2-only loss and from the separate ESCO1/Xenopus reconstitution.

Proposed replacements: protein-lysine-acetyltransferase activity

Summary: Retain the conserved chromocenters localization.

Reason: The official mouse Q8CIB9/ENSMUSP00000022613 source maps to IDA PMID:22101327. Figures 3–4 and the associated Results show Esco2 enrichment in DAPI-dense chromocenter cores, overlap with Hp1-alpha and major-satellite ChIP enrichment in mid-to-late S-phase cortical progenitors/MEFs. This is positive evidence for the defined chromocenter compartment, consistent with the target’s independently established chromatin/cohesion role. The tested mouse localization is not presented as a direct human product-specific assay.

Summary: Specify acetyl-CoA-dependent protein-lysine acetyltransferase activity.

Reason: PMID:15958495 Figure 1B defines human EFO2-C2 as residues 215–601; Figure 2A and the acetyltransferase Methods/Results show the purified His6-tagged fragment incorporating label from [14C]acetyl-CoA by autoacetylation, with an unlabeled BSA control. The mutant series in Figure 2B is EFO1/ESCO1, not ESCO2. The source alone does not map the autoacetylated residue. Independent human evidence in PMID:21111234 Figure 3A/B shows that combined ESCO1/ESCO2 depletion reduces SMC3 K105/K106 acetylation; its purified-enzyme/Xenopus experiment is ESCO1-specific. Together these support the existing more informative protein-lysine-acetyltransferase term, rather than a donor-unspecified acetyltransferase. The recombinant fragment is not the source-described 239-residue splice product. Public locators: https://doi.org/10.1091/mbc.e04-12-1063, Figures 1B and 2A; https://doi.org/10.1016/j.cell.2010.10.031, Figure 3A/B.

Proposed replacements: protein-lysine-acetyltransferase activity

Summary: ESCO2 contributes directly to post-translational protein acetylation.

Reason: PMID:21111234 includes human ESCO2 experiments despite its Sororin-focused title. In its S-phase HeLa chromatin immunoblot, only combined ESCO1/ESCO2 depletion substantially lowers the measured SMC3 acetylation; Figure 3A/B then connects reduced acetylation to reduced Sororin association. This demonstrates overlapping contribution to that endpoint under those conditions, not general functional redundancy. Human PMID:15958495 Figure 3 and mouse PMID:22101327 Figures 6–7 independently establish nonredundant cohesion requirements. Human ESCO2-fragment autoacetylation with acetyl-CoA in PMID:15958495 Figure 2A establishes acetyl-transfer capacity. The separate Figure 3F reconstitution in PMID:21111234 uses ESCO1 and Xenopus chromatin, not purified human ESCO2. Public locators are printed pp. 741–742, Figure 3A/B, DOI:10.1016/j.cell.2010.10.031, and Figure 2A/3, DOI:10.1091/mbc.e04-12-1063.

Summary: Retain the meiotic break-associated chromatin location with assay limits.

Reason: GO:0035861 denotes a chromosomal region where a double-strand break has occurred; it does not require a protein to bind an exposed DNA end or catalyze repair. The verified mouse Q8CIB9 donor carries IDA records citing PMID:22614755 and PMID:22699483. The former original remains inaccessible. In the independently read latter original, Methods describe anti-ESCO2 A301-689A, phospho-H2AFX and SYCP3 immunofluorescence on meiotic spreads. Results and Figures 4–5 show ESCO2/phospho-H2AFX-positive clumps extending from synaptonemal complexes in E18.5 pachytene oocytes, distinct from the male XY-body experiment in Figure 2. Retain this positive region-level localization as non-core because it is a specialized meiotic setting, with marker-based imaging resolution and no direct lesion mapping. The authors’ cautious inference does not negate the regional CC evidence or establish a specific repair mechanism; human germ-cell distribution is not directly assayed.

Summary: Retain protein-lysine-acetyltransferase activity with its assay boundaries.

Reason: The current GO:0061733 definition specifies transfer from acetyl-CoA to a protein lysyl residue. PMID:15958495 directly tests acetyl-CoA-dependent autoacetylation of purified human EFO2 residues 215–601, with BSA as a negative control (Figures 1B and 2A); it does not itself map the acceptor residue or test purified full-length ESCO2 against SMC3. PMID:21111234 Figure 3A/B provides independent human cellular SMC3 K105/K106 acetylation evidence using combined ESCO1/ESCO2 depletion. These complementary results support the lysine acetyltransferase function, while the separate ESCO1 recombinant assay, ESCO1 mutant controls and the untested 239-residue ESCO2 product remain distinct. Public locators: https://doi.org/10.1091/mbc.e04-12-1063, Acetyltransferase Activity Assay and Figures 1–2; https://doi.org/10.1016/j.cell.2010.10.031, Figure 3A/B.

Summary: ESCO2 has conserved protein-lysine acetyltransferase activity.

Reason: The current positive PTHR45884 IBD node PTN000118027 lies on the verified human ESCO2 PTN002476323 path; the target MSA matches its displayed 601-residue sequence and no NOT branch interrupts inheritance. Human PMID:15958495 Figure 2A directly measures acetyl-CoA-dependent autoacetylation of the ESCO2 215–601 fragment. Human PMID:21111234 Figure 3A/B provides the ESCO1/2-dependent SMC3 lysine-acetylation endpoint, and mouse PMID:22101327 Figure 7 independently shows reduced Smc3 K105/K106 acetylation after Esco2 loss. These complementary assays support the inherited protein-lysine-acetyltransferase activity without substituting the separate ESCO1/Xenopus reconstitution for a purified human ESCO2–SMC3 reaction.

Summary: The RHEA mapping specifies the experimentally supported protein-lysine reaction.

Reason: The Q56NI9 UniProt catalytic statement maps to RHEA:45948. The captured official RHEA equation uses acetyl-CoA and a protein lysyl residue and directly cross-references GO:0061733. Human ESCO2-fragment autoacetylation in PMID:15958495 Figure 2A and the cellular SMC3 lysine-acetylation evidence in PMID:21111234 Figure 3A/B and mouse PMID:22101327 Figure 7 independently support this mapping. This is protein acetylation rather than the acetyl-phosphate/free-lysine reaction assigned by the separate GO:0004468 donor annotation.