TRMT10C

Summary: tRNA binding is intrinsic to TRMT10C: its N-terminal region binds tRNA and the MRPP1-MRPP2 subcomplex retains tRNA through successive maturation steps.

Reason: tRNA binding is intrinsic to TRMT10C: its N-terminal region binds tRNA and the MRPP1-MRPP2 subcomplex retains tRNA through successive maturation steps. Supports both the methyltransferase and RNase P scaffold roles.

Summary: In vitro, MRPP1/2 binds and retains the tRNA product of 5' processing and of ELAC2 3' processing.

Reason: In vitro, MRPP1/2 binds and retains the tRNA product of 5' processing and of ELAC2 3' processing.

Summary: Silencing of MRPP1 inhibits 5' (and 3') processing of mitochondrial tRNAs from polycistronic transcripts; consistent with its role as an essential RNase P subunit.

Reason: Silencing of MRPP1 inhibits 5' (and 3') processing of mitochondrial tRNAs from polycistronic transcripts; consistent with its role as an essential RNase P subunit.

Summary: The MRPP1-MRPP2 subcomplex holds the processed tRNA and presents it to the CCA-adding enzyme TRNT1, which performs the catalysis.

Reason: The MRPP1-MRPP2 subcomplex holds the processed tRNA and presents it to the CCA-adding enzyme TRNT1, which performs the catalysis. This is a scaffold contribution to a downstream maturation step, not a core TRMT10C activity.

Summary: RNA binding, from mRNA interactome capture.

Reason: True of TRMT10C but uninformative, because GO:0000049 tRNA binding, accepted in this review on IBA and IDA rows, already entails it and names the functionally relevant substrate, mitochondrial pre-tRNA. GO:0000049 is a confirmed is_a child of GO:0003723.

Summary: RNA binding, from an mRNA-bound proteome screen.

Reason: True of TRMT10C but uninformative, on the same ground as the mRNA interactome capture row above - GO:0000049 tRNA binding is accepted here and entails it. Both GO:0003723 rows share one argument and so take one action.

Summary: Protein binding derived from the identification of mitochondrial RNase P components.

Reason: Protein binding derived from the identification of mitochondrial RNase P components. The informative statements are membership of the mitochondrial ribonuclease P complex (GO:0030678) and the tRNA methyltransferase complex (GO:0043527), both annotated. Protein binding is uninformative; removal does not imply the interaction is false.

Summary: Protein binding to HSD17B10 (MRPP2) reflects formation of the MRPP1-MRPP2 tRNA methyltransferase subcomplex, already captured by GO:0043527 and GO:0030678.

Reason: Protein binding to HSD17B10 (MRPP2) reflects formation of the MRPP1-MRPP2 tRNA methyltransferase subcomplex, already captured by GO:0043527 and GO:0030678. Protein binding is uninformative; removal does not imply the interaction is false.

Summary: Protein binding from the BioPlex 2.0 AP-MS screen.

Reason: Protein binding from the BioPlex 2.0 AP-MS screen. Protein binding is uninformative; removal does not imply the interaction is false.

Summary: Protein binding reflects MRPP1-MRPP2 complex formation and its interactions with ELAC2 and TRNT1 during tRNA maturation; complex membership is annotated separately.

Reason: Protein binding reflects MRPP1-MRPP2 complex formation and its interactions with ELAC2 and TRNT1 during tRNA maturation; complex membership is annotated separately. Protein binding is uninformative; removal does not imply the interaction is false.

Summary: Protein binding reflects MRPP1-MRPP2 and MRPP1-MRPP2-MRPP3 complex formation, which is captured by the complex membership annotations.

Reason: Protein binding reflects MRPP1-MRPP2 and MRPP1-MRPP2-MRPP3 complex formation, which is captured by the complex membership annotations. Protein binding is uninformative; removal does not imply the interaction is false.

Summary: Protein binding from the BioPlex 3.0 AP-MS screen.

Reason: Protein binding from the BioPlex 3.0 AP-MS screen. Protein binding is uninformative; removal does not imply the interaction is false.

Summary: Nucleus is propagated from the nuclear TRMT10 paralogs: the source node PTN000339531 lies above the TRMT10A/TRMT10C split and its human donor is TRMT10A (Q8TBZ6).

Reason: Nucleus is propagated from the nuclear TRMT10 paralogs: the source node PTN000339531 lies above the TRMT10A/TRMT10C split and its human donor is TRMT10A (Q8TBZ6). TRMT10C is a mitochondrial matrix protein that functions in mitochondrial RNase P and tRNA methylation, and is not active in the nucleus.

Summary: Nucleoplasm is propagated from the nuclear TRMT10 paralogs.

Reason: Nucleoplasm is propagated from the nuclear TRMT10 paralogs. TRMT10C is a mitochondrial matrix protein and is not active in the nucleoplasm.

Summary: Mitochondrion, from the MitoCoP high-confidence mitochondrial proteome.

Reason: Mitochondrion, from the MitoCoP high-confidence mitochondrial proteome. TRMT10C (MRPP1) is a mitochondrial matrix protein acting on mitochondrial pre-tRNAs; mitochondrial localization is well established.

Summary: Mitochondrion; IBA consistent with experimental data.

Reason: Mitochondrion; IBA consistent with experimental data. TRMT10C (MRPP1) is a mitochondrial matrix protein acting on mitochondrial pre-tRNAs; mitochondrial localization is well established.

Summary: Mitochondrion from Human Protein Atlas immunolocalization is consistent with the established function.

Reason: Mitochondrion from Human Protein Atlas immunolocalization is consistent with the established function. TRMT10C (MRPP1) is a mitochondrial matrix protein acting on mitochondrial pre-tRNAs; mitochondrial localization is well established.

Summary: TRMT10C (MRPP1) is a mitochondrial matrix protein acting on mitochondrial pre-tRNAs; mitochondrial localization is well established.

Reason: TRMT10C (MRPP1) is a mitochondrial matrix protein acting on mitochondrial pre-tRNAs; mitochondrial localization is well established.

Summary: TRMT10C (MRPP1) is a mitochondrial matrix protein acting on mitochondrial pre-tRNAs; mitochondrial localization is well established.

Reason: TRMT10C (MRPP1) is a mitochondrial matrix protein acting on mitochondrial pre-tRNAs; mitochondrial localization is well established.

Summary: TRMT10C (MRPP1) is a mitochondrial matrix protein acting on mitochondrial pre-tRNAs; mitochondrial localization is well established.

Reason: TRMT10C (MRPP1) is a mitochondrial matrix protein acting on mitochondrial pre-tRNAs; mitochondrial localization is well established.

Summary: Mitochondrial function of TRMT10C is shown by impaired mt-RNA processing in patient cells and rescue by wild-type TRMT10C.

Reason: Mitochondrial function of TRMT10C is shown by impaired mt-RNA processing in patient cells and rescue by wild-type TRMT10C. TRMT10C (MRPP1) is a mitochondrial matrix protein acting on mitochondrial pre-tRNAs; mitochondrial localization is well established.

Summary: TRMT10C (MRPP1) is a mitochondrial matrix protein acting on mitochondrial pre-tRNAs; mitochondrial localization is well established.

Reason: TRMT10C (MRPP1) is a mitochondrial matrix protein acting on mitochondrial pre-tRNAs; mitochondrial localization is well established.

Summary: Mitochondrial matrix is the compartment where mitochondrial transcripts are processed by RNase P.

Reason: Mitochondrial matrix is the compartment where mitochondrial transcripts are processed by RNase P.

Summary: Mitochondrial matrix (Reactome, m1G9 methylation reaction).

Reason: Mitochondrial matrix (Reactome, m1G9 methylation reaction).

Summary: Mitochondrial matrix (Reactome, m1A9 methylation reaction).

Reason: Mitochondrial matrix (Reactome, m1A9 methylation reaction).

Summary: TRMT10C installs a single m1A in the mitochondrial MT-ND5 mRNA.

Reason: TRMT10C installs a single m1A in the mitochondrial MT-ND5 mRNA. This is mRNA modification (GO:0016556) rather than mRNA processing, and is a minor secondary activity relative to tRNA position-9 methylation.

Proposed replacements: mRNA modification

Summary: Involvement in tRNA processing, with no compartment specified.

Reason: tRNA processing is correct but general; TRMT10C acts specifically in mitochondrial tRNA processing (GO:0090646).

Proposed replacements: mitochondrial tRNA processing

Summary: TRMT10C (MRPP1) is a subunit of mitochondrial RNase P together with HSD17B10 (MRPP2) and PRORP (MRPP3).

Reason: TRMT10C (MRPP1) is a subunit of mitochondrial RNase P together with HSD17B10 (MRPP2) and PRORP (MRPP3).

Summary: Mitochondrial RNase P is a proteinaceous complex reconstituted from three proteins, one of which is the TRMT10C methyltransferase.

Reason: Mitochondrial RNase P is a proteinaceous complex reconstituted from three proteins, one of which is the TRMT10C methyltransferase.

Summary: RNase P associates with mtDNA nucleoids, where RNA processing is initiated.

Reason: RNase P associates with mtDNA nucleoids, where RNA processing is initiated. Accurate but secondary to its matrix function.

Summary: Localisation to the mitochondrial nucleoid, from an electronic inference.

Reason: Nucleoid association, consistent with the experimental nucleoid proteomics.

Summary: TRMT10C is a component of the mitochondrial RNase Z complex (ELAC2/SDR5C1/TRMT10C) and the MRPP1-MRPP2 subcomplex enhances ELAC2-catalysed 3' processing.

Reason: TRMT10C is a component of the mitochondrial RNase Z complex (ELAC2/SDR5C1/TRMT10C) and the MRPP1-MRPP2 subcomplex enhances ELAC2-catalysed 3' processing.

Summary: The MRPP1 N-terminus mediates monomer-monomer self-interaction.

Reason: The MRPP1 N-terminus mediates monomer-monomer self-interaction. This is a structural property, not a separate function.

Summary: MRPP1 with MRPP2 forms the tRNA N1-methyltransferase complex.

Reason: MRPP1 with MRPP2 forms the tRNA N1-methyltransferase complex.

Summary: The MRPP1-MRPP2 subcomplex forms m1G9 in mitochondrial tRNAs, with TRMT10C as the catalytic SPOUT methyltransferase subunit.

Reason: The MRPP1-MRPP2 subcomplex forms m1G9 in mitochondrial tRNAs, with TRMT10C as the catalytic SPOUT methyltransferase subunit. Core MF.

Summary: Combined IEA consistent with experimental evidence for m1G9 formation.

Reason: Combined IEA consistent with experimental evidence for m1G9 formation.

Summary: Mitochondrial tRNA methylation at position 9 is a core process of TRMT10C.

Reason: Mitochondrial tRNA methylation at position 9 is a core process of TRMT10C.

Summary: Patient TRMT10C variants impair mitochondrial tRNA processing, rescued by wild-type TRMT10C.

Reason: Patient TRMT10C variants impair mitochondrial tRNA processing, rescued by wild-type TRMT10C.

Summary: Mitochondrial tRNA 5'-end processing is the core process of mitochondrial RNase P, of which TRMT10C is an essential subunit.

Reason: Mitochondrial tRNA 5'-end processing is the core process of mitochondrial RNase P, of which TRMT10C is an essential subunit.

Summary: MRPP1/2 is a required component of the RNase P reaction in vitro.

Reason: MRPP1/2 is a required component of the RNase P reaction in vitro.

Summary: The MRPP1-MRPP2-MRPP3 complex assembles on precursor tRNA for 5' cleavage.

Reason: The MRPP1-MRPP2-MRPP3 complex assembles on precursor tRNA for 5' cleavage.

Summary: Knockdown of MRPP1 impairs 5' processing of mitochondrial tRNAs.

Reason: Knockdown of MRPP1 impairs 5' processing of mitochondrial tRNAs.

Summary: The MRPP1-MRPP2 subcomplex forms m1A9 in mitochondrial tRNAs; TRMT10C is the catalytic subunit.

Reason: The MRPP1-MRPP2 subcomplex forms m1A9 in mitochondrial tRNAs; TRMT10C is the catalytic subunit. Core MF.

Summary: Combined IEA consistent with experimental evidence for m1A9 formation.

Reason: Combined IEA consistent with experimental evidence for m1A9 formation.

Summary: Membership of a catalytic complex, without naming which complex.

Reason: True of TRMT10C but uninformative, because more specific complex terms kept in this review already entail it - GO:0030678 mitochondrial ribonuclease P complex and GO:0043527 tRNA methyltransferase complex, both accepted and in core_functions, and GO:1902555 endoribonuclease complex, kept as non-core. All three are confirmed descendants of GO:1902494 in the QuickGO is_a/part_of closure.

Summary: Membership of an endoribonuclease complex, shown directly.

Reason: TRMT10C is part of the mitochondrial RNase Z complex with ELAC2 and SDR5C1, which is an endoribonuclease complex; the catalytic endonuclease is ELAC2.

Summary: MRPP1/2 significantly enhances ELAC2-catalysed 3' processing of most mitochondrial tRNAs.

Reason: MRPP1/2 significantly enhances ELAC2-catalysed 3' processing of most mitochondrial tRNAs.

Summary: Proposed annotation not in GOA. TRMT10C is one of the three proteins whose combination reconstitutes mitochondrial RNase P activity, and the one that binds the pre-tRNA and holds it for cleavage; PRORP carries the metallonuclease moiety.

Reason: The qualifier is contributes_to and not enables because TRMT10C does not do the chemistry - reconstitution requires all three subunits, and the nuclease activity is PRORP's - while TRMT10C is not merely present either: it binds the pre-tRNA and positions it, so in_complex GO:0030678 alone would understate it. GO:0004526 is absent from TRMT10C-goa.tsv, which carries the complex membership (GO:0030678, part_of) but no RNase P molecular function. This is how GO annotates the paralogous case. The nuclear RNase P holoenzyme's catalytic moiety is the RPPH1 RNA rather than any protein, and QuickGO splits GO:0004526 by qualifier accordingly: RPPH1 carries enables - as do ten further RNAcentral ncRNA ids, itemised in the notes, which are not themselves RPPH1 entries and three of which are lnc-* entries named against CCNB1IP1 and PDGFC, so those ten read as electronic propagation rather than as curated nuclear holoenzyme subunits. Two facts that could look like further marks against the ten are class-level and so differentiate nothing - all fourteen ncRNA enables rows are IEA, RPPH1's four included, and none of the fourteen is recorded as a member of the nucleolar complex - while the holoenzyme's ten protein subunits - POP1, POP4, POP5, POP7, RPP14, RPP21, RPP25, RPP30, RPP38 and RPP40 - carry contributes_to, every one by IDA. That is the comparator set CLAUDE.md asks for: ten gene products standing in this row's role, all carrying this row's term with this row's qualifier. The qualifier split follows the evidence code rather than being absolute - POP5, RPP30 and RPP40 each also carry an enables row, by IEA or TAS - but every IDA row on a nuclear protein subunit is contributes_to, and PRORP is the only protein in either complex carrying enables by direct assay, because in the mitochondrial complex the catalyst is a protein. So the experimental curation lines up behind contributes_to for the subunits and only the electronic and author-statement rows do not. The two mitochondrial accessory subunits are the outliers rather than the convention: neither TRMT10C nor HSD17B10 carries GO:0004526 in GOA. HSD17B10's review does make a recorded choice here, and a different one: its third core function models the same moonlighting subunit role as GO:0000049 tRNA binding with in_complex GO:0030678, and its proposed_new_terms is an explicit empty list. That review carries 101 reviewed rows and three authored core functions, so its status: INITIALIZED is stale metadata rather than a signal that nobody has looked. Under the nuclear comparator above it warrants the same contributes_to proposal; flagged rather than changed here, since HSD17B10 is outside this slice. The gap between the two reviews is narrower than a bare GO:0004526 comparison suggests: both carry GO:0000049 and GO:0030678, and this row is the one addition.