NAA30 PN Consistency Notes
- Generated: 2026-06-18
- Project: PROTEOSTASIS
- Scope: PN consistency rereview against local AIGR review and available deep-research artifacts
- UniProt: Q147X3
- AIGR review status: COMPLETE
- Review batch: proteostasis-batch-2026-06-07c
- Batch change status: added
Source Files Checked
Deep Research Files
- No
*-deep-research*.md file found in this gene directory.
AIGR Review Snapshot
- Description: NAA30 (N-alpha-acetyltransferase 30; also hMak3, NAT12) is the catalytic subunit of the human NatC N-terminal acetyltransferase complex (NatC = NAA30 + NAA35 + NAA38). It is a GNAT-fold acetyltransferase (MAK3 subfamily, EC 2.3.1.256) that co-translationally transfers an acetyl group from acetyl-CoA to the alpha-amino group of N-terminal methionine residues retained in front of bulky/hydrophobic residues (Met-Leu, Met-Ile, Met-Phe, Met-Trp, Met-Tyr). NatC associates with ribosomes and acts on nascent polypeptides; this N-terminal acetylation can shield proteins from N-degron-mediated ubiquitination and degradation. NAA30 activity is required for the lysosomal localization of the small GTPase ARL8B (a NatC substrate), and depletion of NatC subunits triggers p53-dependent apoptosis. NAA30 is predominantly cytoplasmic (ribosome-associated) with some reported nuclear localization.
- Existing/core annotation action counts: ACCEPT: 14; KEEP_AS_NON_CORE: 6; MARK_AS_OVER_ANNOTATED: 1; NEW: 1
PN Consistency Summary
- Consistency: Strong. Deep-research notes, review YAML and PN dossier all agree NAA30 is the catalytic subunit of NatC (=NAA30+NAA35+NAA38, hMak3/hMak10/hMak31), co-translational Nt-acetylation of retained Met before bulky/hydrophobic residues, ribosome-associated. PN-node mapping (NatC complex CC; Nt-acetylation BP) matches the review's MF/CC content. No contradictions.
- PN story / NEW pressure: PN projects the BP GO:0006474 (N-terminal protein amino acid acetylation) — verified real and non-obsolete via OLS; confirmed absent from NAA30 GOA (grep). The review captures the MF (GO:0004596, GO:0120518) and CC (GO:0031417) but has no BP for the acetylation process. GO:0006474 is the BP aspect, not a parent of the MF terms, so it is genuinely complementary. Conclusion: ADD GO:0006474 (involved_in) is defensible and would round out MF/BP/CC; not an over-reach for the catalytic subunit.
- Evidence alignment: Concordant. PN row carries no reference titles; review/notes anchor to PMID:19398576 (NatC characterization, hMak3 catalytic; IDA GO:0004596/GO:0031417) and PMID:37891180 (Nt-acetylation shields from degradation). Both VERIFIED in the YAML reference_review. No divergence.
- Verdict: Consistent and high-quality. Optional ADD of BP GO:0006474 to the review to mirror the PN projection. Recommended edits: Add existing/new BP annotation GO:0006474 (N-terminal protein amino acid acetylation, involved_in) to NAA30 review [YAML].
Full Consistency Review
- UniProt: Q147X3 · batch: proteostasis-batch-2026-06-07c · review status: COMPLETE
- PN placement:
Translation|Cytosolic translation|Nascent peptide husbandry|N-terminal acetylation of nascent peptide|NatC complex component ; PN-node mapping: subtype mapped→GO:0031417 NatC complex (ok_for_propagation); type mapped→GO:0006474 N-terminal protein amino acid acetylation (ok_for_propagation, new_to_goa)
- Consistency: Strong. Deep-research notes, review YAML and PN dossier all agree NAA30 is the catalytic subunit of NatC (=NAA30+NAA35+NAA38, hMak3/hMak10/hMak31), co-translational Nt-acetylation of retained Met before bulky/hydrophobic residues, ribosome-associated. PN-node mapping (NatC complex CC; Nt-acetylation BP) matches the review's MF/CC content. No contradictions.
- PN story / NEW pressure: PN projects the BP GO:0006474 (N-terminal protein amino acid acetylation) — verified real and non-obsolete via OLS; confirmed absent from NAA30 GOA (grep). The review captures the MF (GO:0004596, GO:0120518) and CC (GO:0031417) but has no BP for the acetylation process. GO:0006474 is the BP aspect, not a parent of the MF terms, so it is genuinely complementary. Conclusion: ADD GO:0006474 (involved_in) is defensible and would round out MF/BP/CC; not an over-reach for the catalytic subunit.
- Mapping strategy: Sound for the catalytic subunit. Subtype→NatC complex (exact CC) and type→Nt-acetylation BP are both appropriate and not too broad (NAA30 directly performs the catalysis). No change to node mapping warranted.
- Evidence alignment: Concordant. PN row carries no reference titles; review/notes anchor to PMID:19398576 (NatC characterization, hMak3 catalytic; IDA GO:0004596/GO:0031417) and PMID:37891180 (Nt-acetylation shields from degradation). Both VERIFIED in the YAML reference_review. No divergence.
- Verdict: Consistent and high-quality. Optional ADD of BP GO:0006474 to the review to mirror the PN projection. Recommended edits: Add existing/new BP annotation GO:0006474 (N-terminal protein amino acid acetylation, involved_in) to NAA30 review [YAML].
- 2026-06-18 follow-up: Implemented the YAML edit: added GO:0006474 N-terminal protein amino acid acetylation as a NEW BP recommendation and added it to the catalytic NatC core function.
PN Dossier Context
- review_batch: proteostasis-batch-2026-06-07c
- review_yaml: genes/human/NAA30/NAA30-ai-review.yaml
- PN workbook rows: 1
PN row 1: Translation | Cytosolic translation | Nascent peptide husbandry | N-terminal acetylation of nascent peptide | NatC complex component
- UniProt: Q147X3
- In branches: TR
- PN-node mapping records (path + ancestors):
- [subtype] Translation|Cytosolic translation|Nascent peptide husbandry|N-terminal acetylation of nascent peptide|NatC complex component
status=mapped scope=ok_for_propagation_to_go GO=[GO:0031417 NatC complex]
rationale: Exact cellular-component match: members are subunits of the NatC N-terminal acetyltransferase complex. Complements the parent BP mapping with the complex-membership CC term.
- [type] Translation|Cytosolic translation|Nascent peptide husbandry|N-terminal acetylation of nascent peptide
status=mapped scope=ok_for_propagation_to_go GO=[GO:0006474 N-terminal protein amino acid acetylation]
rationale: This PN type denotes N-terminal acetyltransferase machinery acting on nascent peptides. The GO N-terminal acetylation process is the direct target.
- [group] Translation|Cytosolic translation|Nascent peptide husbandry
status=no_mapping scope= GO=[]
rationale: Reviewed as a broad PN category rather than a single GO class. The member genes span multiple activities, complexes, or contexts, so direct propagation from this node would overstate the shared biology.
- [class] Translation|Cytosolic translation
status=context_only scope=too_broad_to_propagate GO=[GO:0002181 cytoplasmic translation]
rationale: The PN class Cytosolic translation is centered on the cytoplasmic translation apparatus and process, but it also houses supporting machinery such as ribosome biogenesis factors. The GO process term is a useful high-level label for the class, but propagating it to all members would over-annotate genes whose PN placement is through assembly or maturation context rather than core cytoplasmic translation.
- [branch] Translation
status=context_only scope=too_broad_to_propagate GO=[GO:0006412 translation]
rationale: The PN Translation branch is organized around the translation apparatus and immediately associated cotranslational quality-control systems. GO translation is the closest high-level process label, but the PN branch also contains adjacent machinery such as ribosome biogenesis and nascent-chain handling. Keeping this relationship is useful for interpretation, but it is too broad to project safely onto every member.
Projected GO annotations (1)
- GO:0006474 N-terminal protein amino acid acetylation | scope=ok_for_propagation_to_go | goa_status=new_to_goa | from=Translation|Cytosolic translation|Nascent peptide husbandry|N-terminal acetylation of nascent peptide
Note
This file is generated from the current PROTEOSTASIS phase-1 dossier and local gene-review artifacts. Edit the source review, PN mapping, or dossier rather than this generated note when correcting the underlying curation.