rrp36

UniProt ID: Q9P6P2
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Review Status: COMPLETE
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Gene Description

Rrp36 is a conserved nucleolar ribosome-biogenesis factor associated with the 90S preribosome. It supports early processing of the small-subunit rRNA precursor and production of the 40S ribosomal subunit. Comparative experiments in budding yeast and human cells establish a conserved requirement for early pre-rRNA cleavages, while fission yeast localization and curated phylogenetic evidence support the corresponding role of Rrp36. An intrinsic RNA-cleaving activity has not been established.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0000462 maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
IBA
GO_REF:0000033
ACCEPT
Summary: maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) is supported.
Reason: The target has the specific RRP36 family domain and a nucleolar localization in the fission yeast screen. Budding yeast purification and depletion experiments establish 90S/pre-40S association and early SSU-rRNA maturation, and human depletion supports conservation across eukaryotes. This agrees with the curated ancestral assertion and justifies transfer to the fission yeast ortholog.
Supporting Evidence:
PMID:20038530
We show that the Rrp36p protein is nucleolar and interacts with 90S and pre-40S preribosomal particles. Its depletion affects early cleavages of the 35S pre-rRNA and results in a rapid decrease in mature 18S rRNA levels.
PMID:16823372
Next, we determined the localization of 4,431 proteins, corresponding to approximately 90% of the fission yeast proteome, by tagging each ORF with the yellow fluorescent protein.
GO:0003674 molecular_function
ND
GO_REF:0000015
ACCEPT
Summary: molecular_function is supported.
Reason: Rrp36 participates in preribosome assembly and processing, but the reviewed experiments do not establish an intrinsic enzymatic or specific binding activity. Retain the ND molecular-function root instead of inventing an rRNA nuclease activity.
Supporting Evidence:
PMID:20038530
We show that the Rrp36p protein is nucleolar and interacts with 90S and pre-40S preribosomal particles. Its depletion affects early cleavages of the 35S pre-rRNA and results in a rapid decrease in mature 18S rRNA levels.
GO:0005634 nucleus
HDA
PMID:16823372
ORFeome cloning and global analysis of protein localization ...
ACCEPT
Summary: nucleus is supported.
Reason: The target has the specific RRP36 family domain and a nucleolar localization in the fission yeast screen. Budding yeast purification and depletion experiments establish 90S/pre-40S association and early SSU-rRNA maturation, and human depletion supports conservation across eukaryotes. This agrees with the curated ancestral assertion and justifies transfer to the fission yeast ortholog.
Supporting Evidence:
PMID:20038530
We show that the Rrp36p protein is nucleolar and interacts with 90S and pre-40S preribosomal particles. Its depletion affects early cleavages of the 35S pre-rRNA and results in a rapid decrease in mature 18S rRNA levels.
PMID:16823372
Next, we determined the localization of 4,431 proteins, corresponding to approximately 90% of the fission yeast proteome, by tagging each ORF with the yellow fluorescent protein.
GO:0005730 nucleolus
HDA
PMID:16823372
ORFeome cloning and global analysis of protein localization ...
ACCEPT
Summary: nucleolus is supported.
Reason: The target has the specific RRP36 family domain and a nucleolar localization in the fission yeast screen. Budding yeast purification and depletion experiments establish 90S/pre-40S association and early SSU-rRNA maturation, and human depletion supports conservation across eukaryotes. This agrees with the curated ancestral assertion and justifies transfer to the fission yeast ortholog.
Supporting Evidence:
PMID:20038530
We show that the Rrp36p protein is nucleolar and interacts with 90S and pre-40S preribosomal particles. Its depletion affects early cleavages of the 35S pre-rRNA and results in a rapid decrease in mature 18S rRNA levels.
PMID:16823372
Next, we determined the localization of 4,431 proteins, corresponding to approximately 90% of the fission yeast proteome, by tagging each ORF with the yellow fluorescent protein.
GO:0005730 nucleolus
IBA
GO_REF:0000033
ACCEPT
Summary: nucleolus is supported.
Reason: The target has the specific RRP36 family domain and a nucleolar localization in the fission yeast screen. Budding yeast purification and depletion experiments establish 90S/pre-40S association and early SSU-rRNA maturation, and human depletion supports conservation across eukaryotes. This agrees with the curated ancestral assertion and justifies transfer to the fission yeast ortholog.
Supporting Evidence:
PMID:20038530
We show that the Rrp36p protein is nucleolar and interacts with 90S and pre-40S preribosomal particles. Its depletion affects early cleavages of the 35S pre-rRNA and results in a rapid decrease in mature 18S rRNA levels.
PMID:16823372
Next, we determined the localization of 4,431 proteins, corresponding to approximately 90% of the fission yeast proteome, by tagging each ORF with the yellow fluorescent protein.
GO:0005730 nucleolus
IEA
GO_REF:0000044
ACCEPT
Summary: nucleolus is supported.
Reason: The target has the specific RRP36 family domain and a nucleolar localization in the fission yeast screen. Budding yeast purification and depletion experiments establish 90S/pre-40S association and early SSU-rRNA maturation, and human depletion supports conservation across eukaryotes. This agrees with the curated ancestral assertion and justifies transfer to the fission yeast ortholog.
Supporting Evidence:
PMID:20038530
We show that the Rrp36p protein is nucleolar and interacts with 90S and pre-40S preribosomal particles. Its depletion affects early cleavages of the 35S pre-rRNA and results in a rapid decrease in mature 18S rRNA levels.
PMID:16823372
Next, we determined the localization of 4,431 proteins, corresponding to approximately 90% of the fission yeast proteome, by tagging each ORF with the yellow fluorescent protein.
GO:0030686 90S preribosome
IBA
GO_REF:0000033
ACCEPT
Summary: 90S preribosome is supported.
Reason: The target has the specific RRP36 family domain and a nucleolar localization in the fission yeast screen. Budding yeast purification and depletion experiments establish 90S/pre-40S association and early SSU-rRNA maturation, and human depletion supports conservation across eukaryotes. This agrees with the curated ancestral assertion and justifies transfer to the fission yeast ortholog.
Supporting Evidence:
PMID:20038530
We show that the Rrp36p protein is nucleolar and interacts with 90S and pre-40S preribosomal particles. Its depletion affects early cleavages of the 35S pre-rRNA and results in a rapid decrease in mature 18S rRNA levels.
PMID:16823372
Next, we determined the localization of 4,431 proteins, corresponding to approximately 90% of the fission yeast proteome, by tagging each ORF with the yellow fluorescent protein.

Core Functions

Nucleolar 90S preribosome factor supporting early small-subunit rRNA maturation; function transferred from characterized RRP36 orthologs.

Supporting Evidence:
  • PMID:20038530
    We show that the Rrp36p protein is nucleolar and interacts with 90S and pre-40S preribosomal particles. Its depletion affects early cleavages of the 35S pre-rRNA and results in a rapid decrease in mature 18S rRNA levels.

References

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External Prediction Reviews

These computational predictions are reviewed separately from the GOA annotation set used for this review. The assessments below are from this project and do not constitute official GO annotations or endorsement by GO/UniProt. They are not included in the existing annotation review above.

ProtNLM2 External predictions

View prediction review YAML Β· rrp36-protnlm-predictions-review.yaml Β· Review status: COMPLETE

Rrp36 is a conserved 90S preribosome factor supporting small-subunit rRNA maturation. Both predictions are supported but less precise than the established process and complex assignments.

Source documents: genes/SCHPO/rrp36/rrp36-protnlm-source.xml Β· genes/SCHPO/rrp36/rrp36-uniprot.txt Β· genes/SCHPO/rrp36/rrp36-ai-review.yaml

Review score: 2 = concordant with evidence; 1 = uncertain; 0 = discordant with evidence. This is an assessment score, not a model probability.

GO:0006364 rRNA processing GO_BP
LSP β€” Less precise than existing annotation Review score: 2/2
Prediction method: ProtNLM2 Β· Version: pre-release post-processed-2026_02_28k.xml Β· file:SCHPO/rrp36/rrp36-protnlm-source.xml
Review rationale: The specific RRP36 domain and target nucleolar localization support the conserved preribosome role inferred by PAINT. Purification and depletion in budding yeast establish 90S/pre-40S association and early small-subunit rRNA maturation; human depletion supports conservation across eukaryotes. GOA already records maturation of SSU-rRNA from tricistronic rRNA transcript (GO:0000462). The broad rRNA-processing prediction is supported but loses small-subunit specificity; no intrinsic RNase chemistry is implied.
Supporting Evidence:
  • PMID:20038530: "We show that the Rrp36p protein is nucleolar and interacts with 90S and pre-40S preribosomal particles. Its depletion affects early cleavages of the 35S pre-rRNA and results in a rapid decrease in mature 18S rRNA levels."
  • file:SCHPO/rrp36/rrp36-uniprot.txt: "DR InterPro; IPR009292; RRP36."
GO:1990904 ribonucleoprotein complex GO_CC
LSP β€” Less precise than existing annotation Review score: 2/2
Prediction method: ProtNLM2 Β· Version: pre-release post-processed-2026_02_28k.xml Β· file:SCHPO/rrp36/rrp36-protnlm-source.xml
Review rationale: Rrp36 belongs to a specifically identified ribosome-biogenesis family; characterized ortholog copurification with RNA-containing 90S and pre-40S particles establishes the relevant complex type. Curated ancestral inference already places fission yeast Rrp36 in the 90S preribosome (GO:0030686), consistent with its nucleolar localization. A ribonucleoprotein complex is a broader description of that supported complex membership. The prediction is correct but less precise than the existing 90S assignment.
Supporting Evidence:
  • PMID:20038530: "We show that the Rrp36p protein is nucleolar and interacts with 90S and pre-40S preribosomal particles. Its depletion affects early cleavages of the 35S pre-rRNA and results in a rapid decrease in mature 18S rRNA levels."
  • file:SCHPO/rrp36/rrp36-uniprot.txt: "DR InterPro; IPR009292; RRP36."

Deep Research

Falcon

(rrp36-deep-research-falcon.md)

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πŸ“š Additional Documentation

Notes

(rrp36-notes.md)

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Protnlm Function Review

(rrp36-protnlm-function-review.md)

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πŸ“„ View Raw YAML

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