NAA10 (N-alpha-acetyltransferase 10, ARD1A) is the catalytic subunit of the NatA N-terminal acetyltransferase complex, the major co-translational N-terminal acetyltransferase in human cells. In complex with its auxiliary subunit NAA15, which anchors the enzyme to the ribosome, NAA10 transfers an acetyl group from acetyl-CoA to the free alpha-amino group of nascent polypeptide N-termini that begin with small residues (Ser, Ala, Thr, Gly, Cys, Val) exposed after initiator-methionine excision. This irreversible modification affects protein folding, stability, complex assembly, targeting and degradation. NatA activity is further modulated by the associated factors HYPK and NAA50 (the NatE catalytic subunit). NAA10 acts predominantly in the cytoplasm on ribosome-associated nascent chains, with an additional nuclear pool. The free (NAA15-unbound) form has been reported to perform internal (lysine) acetylation of selected substrates (e.g. HIF1A, HSPA1A/B, histone H4), and NAA10 has been implicated in several context-dependent regulatory roles. NAA10 is X-linked (Xq28); pathogenic variants cause Ogden syndrome and related N-terminal acetyltransferase deficiency disorders.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:1990189 protein N-terminal-serine acetyltransferase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetic inference of NatA-type N-terminal serine acetylation, a core, experimentally confirmed activity of NAA10. Reason: N-terminal Ser acetylation is a documented NatA substrate specificity directly demonstrated for human NAA10; IBA transfer is correct. Supporting Evidence: file:human/NAA10/NAA10-uniprot.txt N-terminal L-seryl-[protein] + acetyl-CoA = N-terminal N(alpha)-acetyl-L-seryl-[protein] + CoA + H(+) |
| GO:1990190 protein-N-terminal-glutamate acetyltransferase activity | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: Phylogenetic inference of N-terminal glutamate acetylation. Acidic (Glu/Asp) N-termini are the specificity of NatB/NatC-type complexes, not of NatA/NAA10, whose substrates are small residues exposed after Met removal. Reason: NAA10/NatA acetylates Ser/Ala/Thr/Gly/Cys/Val N-termini, not acidic Glu N-termini; this IBA transfer over-extends the family substrate range to a specificity not supported for NAA10. Supporting Evidence: file:human/NAA10/NAA10-uniprot.txt Acetylates amino termini that are devoid of initiator methionine |
| GO:0004596 protein-N-terminal amino-acid acetyltransferase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic annotation of the parent N-terminal acetyltransferase MF, consistent with NAA10's experimentally established EC 2.3.1.255 activity. Reason: Matches the core catalytic function of NAA10 and is corroborated by direct experimental (IDA/EXP) annotations. Supporting Evidence: file:human/NAA10/NAA10-uniprot.txt Catalytic subunit of N-terminal acetyltransferase complexes which display alpha (N-terminal) acetyltransferase activity |
| GO:0005634 nucleus | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Electronic annotation of nuclear localization, consistent with experimentally documented nuclear pool of NAA10. Reason: Nuclear localization is documented but the core co-translational Nt-acetylation function acts on cytoplasmic ribosomes; nuclear pool is retained as non-core. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv NAA10 located_in GO:0005634 nucleus cellular_component EXP PMID:12464182 |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic annotation of cytoplasmic localization, the principal site of NatA co-translational action. Reason: Cytoplasm is where ribosome-associated NatA acetylates nascent chains; strongly supported by experimental annotations. Supporting Evidence: file:human/NAA10/NAA10-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm |
| GO:0008999 protein-N-terminal-alanine acetyltransferase activity | IEA GO_REF:0000116 | ACCEPT | Summary: RHEA-derived electronic annotation of N-terminal alanine acetylation, a documented NatA specificity of NAA10. Reason: N-terminal Ala acetylation is experimentally established for NAA10. Supporting Evidence: file:human/NAA10/NAA10-uniprot.txt N-terminal L-alanyl-[protein] + acetyl-CoA = N-terminal N(alpha)-acetyl-L-alanyl-[protein] + CoA + H(+) |
| GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: Generic acyltransferase MF from InterPro domain transfer; correct but far less informative than the specific N-terminal acetyltransferase terms. Reason: This high-level acyltransferase term adds no information beyond the specific Nt-acetyltransferase activity; uninformative. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups molecular_function IEA |
| GO:0031415 NatA complex | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic annotation of NatA complex membership; NAA10 is the defining catalytic subunit of NatA. Reason: Core complex membership, strongly supported by structural and IPI data. Supporting Evidence: file:human/NAA10/NAA10-uniprot.txt Component of the N-terminal acetyltransferase A complex (also called the NatA complex) composed of NAA10 and NAA15 |
| GO:1990189 protein N-terminal-serine acetyltransferase activity | IEA GO_REF:0000116 | ACCEPT | Summary: RHEA-derived electronic annotation duplicating the core N-terminal Ser acetylation activity. Reason: Core activity, redundant with the EXP/IBA Ser annotations. Supporting Evidence: file:human/NAA10/NAA10-uniprot.txt N-terminal L-seryl-[protein] + acetyl-CoA = N-terminal N(alpha)-acetyl-L-seryl-[protein] + CoA + H(+) |
| GO:0005515 protein binding | IPI PMID:15496142 Identification and characterization of the human ARD1-NATH p... | KEEP AS NON CORE | Summary: IntAct interaction with NAA15 (Q9BXJ9), the auxiliary NatA subunit. The bare protein binding term is uninformative but records the functionally central NAA10-NAA15 interaction. Reason: Records the real NAA10-NAA15 complex interaction; the informative MF (NatA complex membership / Nt-acetyltransferase activity) is captured elsewhere, so this generic term is kept non-core. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005515 protein binding molecular_function IPI PMID:15496142 UniProtKB:Q9BXJ9 |
| GO:0005515 protein binding | IPI PMID:16507339 Cloning and characterization of hNAT5/hSAN: an evolutionaril... | KEEP AS NON CORE | Summary: IntAct interaction with NAA50 (Q9GZZ1), the NatE catalytic subunit that associates with NatA. Generic protein binding term. Reason: Real NAA50 interaction underlying NatE complex formation; informative function captured by complex annotations, so kept non-core. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005515 protein binding molecular_function IPI PMID:16507339 UniProtKB:Q9GZZ1 |
| GO:0005515 protein binding | IPI PMID:19480662 A novel human NatA Nalpha-terminal acetyltransferase complex... | KEEP AS NON CORE | Summary: IntAct interactions including NAA15 (Q9BXJ9), NAA50 (Q9GZZ1) and NAA16 (Q6N069), all NatA-related subunits/paralogs. Generic term. Reason: Real interactions with NatA partners; uninformative as a bare MF, kept non-core. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005515 protein binding molecular_function IPI PMID:19480662 UniProtKB:Q6N069 |
| GO:0005515 protein binding | IPI PMID:21295525 N-Ξ±-acetyltransferase 10 protein suppresses cancer cell meta... | KEEP AS NON CORE | Summary: High-throughput interactome interactions (e.g. O55043, Q14155, Q15052). Bare protein binding term, uninformative for core function. Reason: Real but high-throughput interactions not central to the catalytic role; kept non-core. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005515 protein binding molecular_function IPI PMID:21295525 UniProtKB:O55043 |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: Proteome-scale yeast two-hybrid interactome capturing many NAA10 interactions. Bare protein binding term. Reason: High-throughput interactome data; uninformative as a core MF. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005515 protein binding molecular_function IPI PMID:25416956 UniProtKB:O43829 |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | KEEP AS NON CORE | Summary: IntAct interaction with NAA15 (Q9BXJ9). Generic protein binding term. Reason: Records the central NAA10-NAA15 interaction; informative function captured elsewhere. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005515 protein binding molecular_function IPI PMID:28514442 UniProtKB:Q9BXJ9 |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | KEEP AS NON CORE | Summary: IntAct interactions (Q13137, Q92845) from a high-throughput study. Bare protein binding term. Reason: High-throughput interactions; uninformative as a core MF. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005515 protein binding molecular_function IPI PMID:31515488 UniProtKB:Q13137 |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: Large high-throughput interactome screen capturing numerous NAA10 interactions. Bare protein binding term. Reason: High-throughput interactome data; uninformative as core MF. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005515 protein binding molecular_function IPI PMID:32296183 UniProtKB:O43829 |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | KEEP AS NON CORE | Summary: Neurodegeneration interactome screen capturing interactions (e.g. APP P05067, RAC1 P63000). Bare protein binding term. Reason: High-throughput interactions not central to the catalytic function. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005515 protein binding molecular_function IPI PMID:32814053 UniProtKB:P05067 |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: BioPlex affinity-purification interactome capturing NatA-related partners (NAA15 Q9BXJ9, NAA50 Q9GZZ1, NAA16 Q6N069). Bare protein binding term. Reason: Records real NatA-partner interactions; informative function captured by complex annotations. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005515 protein binding molecular_function IPI PMID:33961781 UniProtKB:Q9BXJ9 |
| GO:0005515 protein binding | IPI PMID:35156780 CFTR interactome mapping using the mammalian membrane two-hy... | KEEP AS NON CORE | Summary: IntAct interaction with HTT (P13569, huntingtin). Bare protein binding term. Reason: High-throughput interaction; uninformative as core MF. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005515 protein binding molecular_function IPI PMID:35156780 UniProtKB:P13569 |
| GO:0005515 protein binding | IPI PMID:36012204 Differential CFTR-Interactome Proximity Labeling Procedures ... | KEEP AS NON CORE | Summary: IntAct interaction with HTT (P13569, huntingtin). Bare protein binding term. Reason: High-throughput interaction; uninformative as core MF. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005515 protein binding molecular_function IPI PMID:36012204 UniProtKB:P13569 |
| GO:0005515 protein binding | IPI PMID:36442525 ARD1 stabilizes NRF2 through direct interaction and promotes... | KEEP AS NON CORE | Summary: IntAct interaction with a high-throughput partner (Q16236). Bare protein binding term. Reason: High-throughput interaction; uninformative as core MF. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005515 protein binding molecular_function IPI PMID:36442525 UniProtKB:Q16236 |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | KEEP AS NON CORE | Summary: Multimodal cell-maps interactome capturing NatA-related partners (NAA15 Q9BXJ9, NAA50 Q9GZZ1, NAA16 Q6N069). Bare protein binding term. Reason: Records real NatA-partner interactions; informative function captured elsewhere. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005515 protein binding molecular_function IPI PMID:40205054 UniProtKB:Q9BXJ9 |
| GO:0008080 N-acetyltransferase activity | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Generic N-acetyltransferase MF from ortholog transfer; correct but less specific than the N-terminal acetyltransferase terms. Reason: Higher-level than the specific Nt-acetyltransferase activity; adds no information beyond the precise terms. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0008080 N-acetyltransferase activity molecular_function IEA GO_REF:0000107 |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: Direct immunofluorescence (HPA) cytosolic localization, consistent with ribosome-associated NatA function in the cytoplasm. Reason: Cytosol is the principal site of co-translational Nt-acetylation. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005829 cytosol cellular_component IDA GO_REF:0000052 HPA |
| GO:0005634 nucleus | EXP PMID:12464182 Regulation and destabilization of HIF-1alpha by ARD1-mediate... | KEEP AS NON CORE | Summary: Experimental nuclear localization of NAA10, where a free pool acts on substrates such as HIF1A. Reason: Documented nuclear pool; non-core relative to cytoplasmic co-translational NatA function. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005634 nucleus cellular_component EXP PMID:12464182 |
| GO:0005737 cytoplasm | EXP PMID:12464182 Regulation and destabilization of HIF-1alpha by ARD1-mediate... | ACCEPT | Summary: Experimental cytoplasmic localization, the principal site of NatA action. Reason: Core localization for co-translational Nt-acetylation. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005737 cytoplasm cellular_component EXP PMID:12464182 |
| GO:0008999 protein-N-terminal-alanine acetyltransferase activity | EXP PMID:15496142 Identification and characterization of the human ARD1-NATH p... | ACCEPT | Summary: Experimental demonstration of N-terminal alanine acetylation by NatA, a core specificity of NAA10. Reason: Direct experimental evidence for a core NatA substrate specificity. Supporting Evidence: file:human/NAA10/NAA10-uniprot.txt N-terminal L-alanyl-[protein] + acetyl-CoA = N-terminal N(alpha)-acetyl-L-alanyl-[protein] + CoA + H(+) |
| GO:0008999 protein-N-terminal-alanine acetyltransferase activity | EXP PMID:19420222 Proteomics analyses reveal the evolutionary conservation and... | ACCEPT | Summary: Experimental N-terminal alanine acetylation (acetylation of termini devoid of initiator Met), a core NatA activity. Reason: Direct experimental evidence for core NatA specificity. Supporting Evidence: file:human/NAA10/NAA10-uniprot.txt Acetylates amino termini that are devoid of initiator methionine |
| GO:0008999 protein-N-terminal-alanine acetyltransferase activity | EXP PMID:25489052 Biochemical and cellular analysis of Ogden syndrome reveals ... | ACCEPT | Summary: Experimental N-terminal alanine acetylation by NatA, core specificity. Reason: Direct experimental evidence for core NatA specificity. Supporting Evidence: file:human/NAA10/NAA10-uniprot.txt N-terminal L-alanyl-[protein] + acetyl-CoA = N-terminal N(alpha)-acetyl-L-alanyl-[protein] + CoA + H(+) |
| GO:1990189 protein N-terminal-serine acetyltransferase activity | EXP PMID:15496142 Identification and characterization of the human ARD1-NATH p... | ACCEPT | Summary: Experimental N-terminal serine acetylation, a core NatA specificity of NAA10. Reason: Direct experimental evidence; this is the prototypical NatA substrate. Supporting Evidence: file:human/NAA10/NAA10-uniprot.txt N-terminal L-seryl-[protein] + acetyl-CoA = N-terminal N(alpha)-acetyl-L-seryl-[protein] + CoA + H(+) |
| GO:1990189 protein N-terminal-serine acetyltransferase activity | EXP PMID:19420222 Proteomics analyses reveal the evolutionary conservation and... | ACCEPT | Summary: Experimental N-terminal serine acetylation by NatA. Reason: Direct experimental evidence for core specificity. Supporting Evidence: file:human/NAA10/NAA10-uniprot.txt N-terminal L-seryl-[protein] + acetyl-CoA = N-terminal N(alpha)-acetyl-L-seryl-[protein] + CoA + H(+) |
| GO:1990189 protein N-terminal-serine acetyltransferase activity | EXP PMID:25489052 Biochemical and cellular analysis of Ogden syndrome reveals ... | ACCEPT | Summary: Experimental N-terminal serine acetylation by NatA. Reason: Direct experimental evidence for core specificity. Supporting Evidence: file:human/NAA10/NAA10-uniprot.txt N-terminal L-seryl-[protein] + acetyl-CoA = N-terminal N(alpha)-acetyl-L-seryl-[protein] + CoA + H(+) |
| GO:1990189 protein N-terminal-serine acetyltransferase activity | EXP PMID:29754825 Structure of Human NatA and Its Regulation by the Huntingtin... | ACCEPT | Summary: Experimental N-terminal serine acetylation by NatA, from structural/ kinetic characterization of the human NatA/NatE complex. Reason: Direct experimental evidence for core specificity. Supporting Evidence: file:human/NAA10/NAA10-uniprot.txt N-terminal L-seryl-[protein] + acetyl-CoA = N-terminal N(alpha)-acetyl-L-seryl-[protein] + CoA + H(+) |
| GO:0051604 protein maturation | IDA PMID:15496142 Identification and characterization of the human ARD1-NATH p... | KEEP AS NON CORE | Summary: N-terminal acetylation is part of co-translational protein maturation; a plausible biological-process outcome of NatA activity. Reason: Maturation is a broad downstream process of Nt-acetylation; the core is the catalytic MF. Retained as non-core BP. Supporting Evidence: file:human/NAA10/NAA10-uniprot.txt Catalytic subunit of N-terminal acetyltransferase complexes which display alpha (N-terminal) acetyltransferase activity |
| GO:0051604 protein maturation | IDA PMID:19480662 A novel human NatA Nalpha-terminal acetyltransferase complex... | KEEP AS NON CORE | Summary: N-terminal acetylation as part of protein maturation; broad BP outcome of NatA activity. Reason: Downstream process of the catalytic MF; kept non-core. Supporting Evidence: file:human/NAA10/NAA10-uniprot.txt Catalytic subunit of N-terminal acetyltransferase complexes which display alpha (N-terminal) acetyltransferase activity |
| GO:1904592 positive regulation of protein refolding | IDA PMID:27708256 ARD1-mediated Hsp70 acetylation balances stress-induced prot... | KEEP AS NON CORE | Summary: NAA10 (ARD1) acetylates Hsp70 (HSPA1A/B at Lys-77), enhancing chaperone activity and balancing stress-induced protein refolding versus degradation. This is a context-dependent moonlighting (internal lysine acetylation) role, distinct from co-translational Nt-acetylation. Reason: Supported by direct experimental evidence but represents a specialized moonlighting (lysine-acetylation) function, not the core Nt-acetyltransferase activity. Supporting Evidence: PMID:27708256 ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation |
| GO:0005737 cytoplasm | IDA PMID:15496142 Identification and characterization of the human ARD1-NATH p... | ACCEPT | Summary: Direct cytoplasmic localization (ComplexPortal NatA), the principal site of co-translational acetylation. Reason: Core localization for NatA function. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005737 cytoplasm cellular_component IDA PMID:15496142 Homo sapiens ComplexPortal |
| GO:0031415 NatA complex | IPI PMID:15496142 Identification and characterization of the human ARD1-NATH p... | ACCEPT | Summary: Direct evidence that NAA10 is part of the NatA complex (with NAA15). Reason: Core complex membership, directly demonstrated. Supporting Evidence: file:human/NAA10/NAA10-uniprot.txt Component of the N-terminal acetyltransferase A complex (also called the NatA complex) composed of NAA10 and NAA15 |
| GO:0031415 NatA complex | IPI PMID:19480662 A novel human NatA Nalpha-terminal acetyltransferase complex... | ACCEPT | Summary: Direct evidence for NatA complex membership. Reason: Core complex membership, directly demonstrated. Supporting Evidence: file:human/NAA10/NAA10-uniprot.txt Component of the N-terminal acetyltransferase A complex (also called the NatA complex) composed of NAA10 and NAA15 |
| GO:0004596 protein-N-terminal amino-acid acetyltransferase activity | IDA PMID:25489052 Biochemical and cellular analysis of Ogden syndrome reveals ... | ACCEPT | Summary: Direct experimental evidence for N-terminal amino-acid acetyltransferase activity, the core catalytic function. Reason: Core catalytic MF, directly demonstrated. Supporting Evidence: file:human/NAA10/NAA10-uniprot.txt Catalytic subunit of N-terminal acetyltransferase complexes which display alpha (N-terminal) acetyltransferase activity |
| GO:0005515 protein binding | IPI PMID:25489052 Biochemical and cellular analysis of Ogden syndrome reveals ... | KEEP AS NON CORE | Summary: IntAct interactions with NAA15 (Q9BXJ9) and NAA50 (Q9GZZ1), NatA/NatE subunits. Generic protein binding term. Reason: Records central NatA/NatE subunit interactions; informative function captured elsewhere. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005515 protein binding molecular_function IPI PMID:25489052 UniProtKB:Q9BXJ9 |
| GO:0005737 cytoplasm | IDA PMID:25489052 Biochemical and cellular analysis of Ogden syndrome reveals ... | ACCEPT | Summary: Direct cytoplasmic localization of NAA10. Reason: Core localization for NatA function. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005737 cytoplasm cellular_component IDA PMID:25489052 |
| GO:2000719 negative regulation of maintenance of mitotic sister chromatid cohesion, centromeric | IDA PMID:27422821 Opposing Functions of the N-terminal Acetyltransferases Naa5... | KEEP AS NON CORE | Summary: NAA10 reported as a negative regulator of sister chromatid cohesion during mitosis; a specialized context-dependent role. Reason: Documented experimentally but a specialized non-core function distinct from co-translational Nt-acetylation. Supporting Evidence: file:human/NAA10/NAA10-uniprot.txt Acts as a negative regulator of sister chromatid cohesion during mitosis |
| GO:0005515 protein binding | IPI PMID:27708256 ARD1-mediated Hsp70 acetylation balances stress-induced prot... | KEEP AS NON CORE | Summary: IntAct interaction with HSPA1A/HSPA1B (P0DMV8/P0DMV9), the Hsp70 substrate acetylated by NAA10. Generic protein binding term. Reason: Real interaction underlying the moonlighting Hsp70-acetylation role; uninformative as a bare MF. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005515 protein binding molecular_function IPI PMID:27708256 UniProtKB:P0DMV8 |
| GO:0005634 nucleus | IDA PMID:25732826 An organellar NΞ±-acetyltransferase, Naa60, acetylates cytoso... | KEEP AS NON CORE | Summary: Direct nuclear localization of NAA10. Reason: Documented nuclear pool; non-core relative to cytoplasmic NatA function. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005634 nucleus cellular_component IDA PMID:25732826 |
| GO:0005737 cytoplasm | IDA PMID:25732826 An organellar NΞ±-acetyltransferase, Naa60, acetylates cytoso... | ACCEPT | Summary: Direct cytoplasmic localization of NAA10. Reason: Core localization for NatA function. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005737 cytoplasm cellular_component IDA PMID:25732826 |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | MARK AS OVER ANNOTATED | Summary: Membrane localization from a high-throughput membrane proteome dataset; not consistent with NAA10's soluble cytoplasmic/ribosome-associated function. Reason: HDA membrane proteome hit; likely reflects co-purification rather than a genuine integral-membrane localization for this soluble enzyme. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0016020 membrane cellular_component HDA PMID:19946888 |
| GO:0004596 protein-N-terminal amino-acid acetyltransferase activity | IDA PMID:19480662 A novel human NatA Nalpha-terminal acetyltransferase complex... | ACCEPT | Summary: Direct evidence that NAA10 contributes the catalytic N-terminal acetyltransferase activity to the NatA complex. Reason: Core catalytic MF; the contributes_to qualifier correctly reflects that catalysis occurs in the NAA10-NAA15 complex. Supporting Evidence: file:human/NAA10/NAA10-uniprot.txt Catalytic subunit of N-terminal acetyltransferase complexes which display alpha (N-terminal) acetyltransferase activity |
| GO:0031415 NatA complex | IDA PMID:19480662 A novel human NatA Nalpha-terminal acetyltransferase complex... | ACCEPT | Summary: Direct evidence for NatA complex membership. Reason: Core complex membership. Supporting Evidence: file:human/NAA10/NAA10-uniprot.txt Component of the N-terminal acetyltransferase A complex (also called the NatA complex) composed of NAA10 and NAA15 |
| GO:0043022 ribosome binding | IDA PMID:19480662 A novel human NatA Nalpha-terminal acetyltransferase complex... | ACCEPT | Summary: NAA10/NatA binds the ribosome, enabling co-translational acetylation of nascent chains. Ribosome anchoring is largely conferred by NAA15. Reason: Ribosome binding is a documented and functionally important MF for the co-translational action of NatA. Supporting Evidence: file:human/NAA10/NAA10-uniprot.txt Interacts with the ribosome |
| GO:0005634 nucleus | IDA PMID:15496142 Identification and characterization of the human ARD1-NATH p... | KEEP AS NON CORE | Summary: Direct nuclear localization of NAA10. Reason: Documented nuclear pool; non-core relative to cytoplasmic NatA function. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005634 nucleus cellular_component IDA PMID:15496142 |
| GO:0016407 acetyltransferase activity | IDA PMID:15496142 Identification and characterization of the human ARD1-NATH p... | MARK AS OVER ANNOTATED | Summary: Generic acetyltransferase MF; correct but less informative than the specific N-terminal acetyltransferase terms. Reason: High-level term superseded by the specific Nt-acetyltransferase annotations. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0016407 acetyltransferase activity molecular_function IDA PMID:15496142 |
| GO:0043022 ribosome binding | IDA PMID:15496142 Identification and characterization of the human ARD1-NATH p... | ACCEPT | Summary: NAA10/NatA binds the ribosome, enabling co-translational Nt-acetylation. Reason: Functionally important MF for co-translational action of NatA. Supporting Evidence: file:human/NAA10/NAA10-uniprot.txt Interacts with the ribosome |
| GO:0005634 nucleus | TAS PMID:7981673 Isolation of new genes in distal Xq28: transcriptional map a... | KEEP AS NON CORE | Summary: Early traceable-author statement placing the protein in the nucleus. Reason: Consistent with the documented nuclear pool; non-core relative to cytoplasmic NatA function. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0005634 nucleus cellular_component TAS PMID:7981673 |
| GO:0008080 N-acetyltransferase activity | TAS PMID:7981673 Isolation of new genes in distal Xq28: transcriptional map a... | MARK AS OVER ANNOTATED | Summary: Early traceable-author statement of N-acetyltransferase activity; generic relative to the specific Nt-acetyltransferase terms. Reason: Generic term superseded by specific Nt-acetyltransferase annotations. Supporting Evidence: file:human/NAA10/NAA10-goa.tsv GO:0008080 N-acetyltransferase activity molecular_function TAS PMID:7981673 |
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Download this section (compressed HTML)Q: To what extent is the internal (lysine) acetyltransferase activity of free NAA10 a genuine physiological function versus an in vitro property of the NAA15-unbound enzyme?
Q: How do Ogden syndrome variants (e.g. Ser37Pro) differentially impair NatA catalysis, NAA15 binding, and ribosome association?
Experiment: N-terminal acetylome (N-terminal COFRADIC / SILAC) profiling in NAA10 patient-variant versus wild-type cells to quantify substrate-specific loss of Nt-acetylation.
Experiment: Reconstitution of NatA with and without NAA15/HYPK/NAA50 to dissect how each auxiliary factor modulates NAA10 catalytic specificity and ribosome binding.
Experiment: Targeted proteomics to test whether reported lysine-acetylation substrates (HIF1A, HSPA1A, TSC2) are modified by free NAA10 in vivo under physiological conditions.
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