Affinage

TMA16

Translation machinery-associated protein 16 · UniProt Q96EY4

Length
203 aa
Mass
23.9 kDa
Annotated
2026-06-10
4 papers in source corpus 1 papers cited in narrative 1 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 2/2 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

TMA16 is a factor associated with the human pre-60S ribosomal particle, positioned between the 5S RNA and the P0 stalk during the late nuclear maturation steps of large ribosomal subunit assembly (PMID:32669547). Cryo-EM analysis of pre-60S particles isolated through the nuclear export factor NMD3 places TMA16 at this site in assembly intermediates captured immediately before and after nuclear export, linking it to the stages of 60S maturation that bridge the nucleus and cytoplasm (PMID:32669547). Beyond this structural localization (PMID:32669547), no further mechanistic detail, biochemical activity, or interaction network for TMA16 has been characterized in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 1 step
  1. 2020 High

    Whether TMA16 participates in human ribosome biogenesis and where it acts on the maturing subunit was unknown; visualizing it within export-stage pre-60S particles established it as a late large-subunit assembly factor positioned at the 5S RNA/P0 stalk interface.

    Evidence Cryo-EM structural analysis of human pre-60S ribosomal particles isolated via the nuclear export factor NMD3

    PMID:32669547

    Open questions at the time
    • No biochemical activity or function assigned to TMA16 within the particle
    • Mechanism of recruitment and release relative to nuclear export is not defined
    • Effect of TMA16 depletion on 60S maturation or cell growth not tested

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unknown what molecular activity TMA16 contributes to pre-60S maturation and how its association is coordinated with the 5S RNP and stalk assembly.
  • No functional or loss-of-function characterization in the available corpus
  • No defined binding partners beyond structural proximity to 5S RNA and P0 stalk

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Localization
GO:0005634 nucleus 1
Pathway
R-HSA-8953854 Metabolism of RNA 1
Complex memberships
pre-60S ribosomal particle

Evidence

Reading pass · 1 per-paper finding extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2020 TMA16 is localized between the 5S RNA and the P0 stalk in human pre-60S ribosomal particles, as determined by cryo-EM structural snapshots of particles isolated through the nuclear export factor NMD3, representing assembly stages immediately before and after nuclear export. Cryo-EM structural analysis of human pre-60S ribosomal particles isolated via NMD3 Nature communications High 32669547

Source papers

Stage 0 corpus · 4 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2020 Structural snapshots of human pre-60S ribosomal particles before and after nuclear export. Nature communications 64 32669547
2017 P-body proteins regulate transcriptional rewiring to promote DNA replication stress resistance. Nature communications 33 28916784
2015 Genome-wide association study for the interaction between BMR and BMI in obese Korean women including overweight. Nutrition research and practice 24 26865924
2025 Characterization of methylation profile in biofluid cell-free DNA and identification of differentially methylated genes for phenotypic representations in Parkinson's disease. Clinical neurology and neurosurgery 1 40527220

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