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Protein / target

Ribonuclease 3

Encoded byDROSHAQ9NRR4Homo sapiensSwiss-Prot
UniProt: Q9NRR4Ensembl: ENSG00000113360HGNC: HGNC:17904NCBI Gene: 29102
Degrader-tractable
Druggability
Database Ubiquitination
1
Research papers

Protein at a glance

Biological role

Protein homodimerization

Strongest disease association

Neurodegenerative Diseases

Via encoding gene DROSHA · Pathway evidence · score 0.51

Research activity

Emerging research

1 papers · latest 2001

Derived from structured UniProt, Open Targets and literature data on this page.

Protein profile

UniProt 2026_02

Canonical identity and biological annotation from UniProt.

Function overview

Ribonuclease III double-stranded (ds) RNA-specific endoribonuclease that is involved in the initial step of microRNA (miRNA) biogenesis.

View complete UniProt function annotation

Ribonuclease III double-stranded (ds) RNA-specific endoribonuclease that is involved in the initial step of microRNA (miRNA) biogenesis. Component of the microprocessor complex that is required to process primary miRNA transcripts (pri-miRNAs) to release precursor miRNA (pre-miRNA) in the nucleus. Within the microprocessor complex, DROSHA cleaves the 3' and 5' strands of a stem-loop in pri-miRNAs (processing center 11 bp from the dsRNA-ssRNA junction) to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs. Involved also in pre-rRNA processing. Cleaves double-strand RNA and does not cleave single-strand RNA. Involved in the formation of GW bodies. Plays a role in growth homeostasis in response to autophagy in motor neurons (By similarity)

Subcellular location

NucleusNucleus, nucleolusCytoplasm
Domains and Gene Ontology detail (25)

Domains & features

RNase III 1RNase III 2DRBM

Gene Ontology

  • Ccytoplasm
  • Cglutamatergic synapse
  • Cmicroprocessor complex
  • Cnucleolus
  • Cnucleoplasm
  • Cnucleus
  • Cpostsynaptic density
  • FDEAD/H-box RNA helicase binding
  • Flipopolysaccharide binding
  • Fmetal ion binding
  • Fprimary miRNA binding
  • Fprotein homodimerization activity

1374 aa · 159 kDa · 4 isoforms

Translational evidence

Open Targets 26

Why this target matters therapeutically, strongest evidence first. Disease associations are gene-level (via the gene that encodes this protein) and open into the full confidence synthesis; the development universe, tractability and safety annotations are target-level, from Open Targets.

Strongest disease associations · via encoding gene DROSHA

Gene-level evidence surfaced through the gene DROSHA that encodes this protein — not a direct protein–disease relationship. Ranked by Forefront's causal-directness weighting, so genetically- and clinically-evidenced diseases lead over ones that merely share the literature.

Neurodegenerative Diseases
0.34Preliminary

Pathway evidence dominant · Open Targets 0.51 · no direct causal or clinical evidence

View evidence synthesis (1)
Neurodegenerative DiseasesPreliminary
0.34
agreement 0.16–0.52
Pathway98%Literature2%

Open Targets aggregate 0.51 · 2 independent evidence families · no direct causal or clinical evidence

The evidence agreement range shows how closely the independent evidence families agree — it is not a statistical confidence interval, and nothing here is fitted to outcome data. Derived from Open Targets evidence types under Forefront weighting; the per-type scores above show the calculation.

Show all associations
Neurodegenerative Diseases0.51

Tractability

Protein degraders — Emerging

Feasibility evidence (database ubiquitination and half-life data) — no clinical-stage drug of this modality recorded.

View underlying tractability evidence (2)
PR · Database UbiquitinationPR · Half-life Data

Raw Open Targets tractability assessment buckets, by modality.

Safety-related annotations

drug toxicityClinPGx

Terms indexed against this target in Open Targets' safety data, with their datasource. These are annotations, not causal claims: the direction of effect (whether activation or inhibition is implicated), species and evidence strength are not captured here, so an entry does not mean that modulating this target is known to cause that condition.

Research activity

1 papers · to 2001

Papers linked directly to this protein. This is the protein's own literature — descriptor-derived papers are kept separate below.

Most cited

RNA interference is mediated by 21- and 22-nucleotide RNAs.2,176 cites

Elbashir SM · Genes & development · 2001

Recent

RNA interference is mediated by 21- and 22-nucleotide RNAs.

Elbashir SM · Genes & development · 2001

Europe PMC papers linked directly to this protein.