Harmonizome 3.0

ribonuclease, RNase A family, 11 (non-active)

Predicted to enable endonuclease activity and nucleic acid binding activity. Predicted to be involved in defense response to Gram-positive bacterium. Predicted to be located in extracellular region. [provided by Alliance of Genome Resources, Mar 2025]

ribonuclease, RNase A family, 10 (non-active)

Predicted to enable nucleic acid binding activity. Predicted to be involved in several processes, including defense response to Gram-positive bacterium; positive regulation of flagellated sperm motility; and regulation of fertilization. Predicted to act upstream of or within epithelial cell morphogenesis; seminiferous tubule development; and single fertilization. Predicted to be located in extracellular region. [provided by Alliance of Genome Resources, Mar 2025]

ribonuclease, RNase A family, 13 (non-active)

Predicted to enable nucleic acid binding activity. Predicted to be involved in defense response to Gram-positive bacterium. Predicted to be located in extracellular region. [provided by Alliance of Genome Resources, Mar 2025]

ribonuclease, RNase A family, 12 (non-active)

Predicted to enable RNA nuclease activity. Predicted to be involved in defense response to Gram-positive bacterium. Predicted to be located in extracellular region. [provided by Alliance of Genome Resources, Mar 2025]

ribonuclease, RNase K

Enables RNA endonuclease activity. Involved in endosomal lumen acidification; proton transmembrane transport; and receptor-mediated endocytosis of virus by host cell. Part of membrane. [provided by Alliance of Genome Resources, Mar 2025]

ribonuclease, RNase A family, 1 (pancreatic)

This gene encodes a member of the pancreatic-type of secretory ribonucleases, a subset of the ribonuclease A superfamily. The encoded endonuclease cleaves internal phosphodiester RNA bonds on the 3'-side of pyrimidine bases. It prefers poly(C) as a substrate and hydrolyzes 2',3'-cyclic nucleotides, with a pH optimum near 8.0. The encoded protein is monomeric and more commonly acts to degrade ds-RNA over ss-RNA. Alternative splicing occurs at this locus and four transcript variants encoding the same protein have been identified. [provided by RefSeq, Jul 2008]

ribonuclease, RNase A family, 3

The protein encoded by this gene belongs to the pancreatic ribonuclease family, a subset of the ribonuclease A superfamily. The protein exhibits antimicrobial activity against pathogenic bacteria [provided by RefSeq, Oct 2014]

ribonuclease, RNase A family, 2 (liver, eosinophil-derived neurotoxin)

The protein encoded by this gene is a non-secretory ribonuclease that belongs to the pancreatic ribonuclease family, a subset of the ribonuclease A superfamily. The protein antimicrobial activity against viruses. [provided by RefSeq, Oct 2014]

ribonuclease, RNase A family, 7

The protein encoded by this gene belongs to the pancreatic ribonuclease family, a subset of the ribonuclease A superfamily. The protein has broad-spectrum antimicrobial activity against bacteria and fungi. [provided by RefSeq, Oct 2014]

ribonuclease, RNase A family, k6

The protein encoded by this gene is a member of the ribonuclease A superfamily and functions in the urinary tract. The protein has broad-spectrum antimicrobial activity against pathogenic bacteria. [provided by RefSeq, Nov 2014]

ribonuclease, RNase A family, 9 (non-active)

Predicted to enable nucleic acid binding activity. Predicted to be involved in defense response to Gram-positive bacterium. Predicted to act upstream of or within positive regulation of flagellated sperm motility involved in capacitation. Predicted to be located in extracellular region. [provided by Alliance of Genome Resources, Mar 2025]

ribonuclease, RNase A family, 8

The protein encoded by this gene belongs to the pancreatic ribonuclease family, a subset of the ribonuclease A superfamily. The protein is expressed prominently in the placenta and exhibits antimicrobial activity against pathogenic bacteria and fungi. [provided by RefSeq, Oct 2014]

angiogenin, ribonuclease, RNase A family, 5

The protein encoded by this gene is a member of the RNase A superfamily though it has relatively weak ribonucleolytic activity. This protein is a potent mediator of new blood vessel formation and thus, in addition to the name RNase5, is commonly called angiogenin. This protein induces angiogenesis after binding to actin on the surface of endothelial cells. This protein also accumulates at the nucleolus where it stimulates ribosomal transcription. Under stress conditions this protein translocates to the cytosol where it hydrolyzes cellular tRNAs and influences protein synthesis. A signal peptide is cleaved from the precursor protein to produce a mature protein which contains a nuclear localization signal, a cell binding motif, and a catalytic domain. This protein has been shown to be both neurotrophic and neuroprotective and the mature protein has antimicrobial activity against some bacteria and fungi, including S. pneumoniae and C. albicans. Due to its effect on rRNA production and angiogenesis this gene plays important roles in cell growth and tumor progression. Mutations in this gene are associated with progression of amyotrophic lateral sclerosis (ALS). This gene and the neighboring RNase4 gene share promoters and 5' exons though each gene then splices to a distinct 3' exon containing the complete coding region of each gene. Alternative splicing results in multiple transcript variants encoding the same protein. [provided by RefSeq, Jul 2020]

ribonuclease, RNase A family, 2 (liver, eosinophil-derived neurotoxin) pseudogene

ribonuclease, RNase A family, 4

The protein encoded by this gene belongs to the pancreatic ribonuclease family. It plays an important role in mRNA cleavage and has marked specificity towards the 3' side of uridine nucleotides. Alternative splicing results in four transcript variants encoding the same protein. This gene and the gene that encodes angiogenin share promoters and 5' exons. Each gene splices to a unique downstream exon that contains its complete coding region. [provided by RefSeq, Aug 2013]

protein only RNase P catalytic subunit

Enables ribonuclease P activity. Involved in mitochondrial tRNA 5'-end processing. Located in mitochondrion and nucleoplasm. Part of mitochondrial ribonuclease P complex. Implicated in combined oxidative phosphorylation deficiency 54. [provided by Alliance of Genome Resources, Mar 2025]

telomerase RNA component interacting RNase

Enables 3'-5' exonuclease activity and 5'-3' exonuclease activity. Involved in rRNA catabolic process. [provided by Alliance of Genome Resources, Mar 2025]

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Rof/RNase P-like protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the cytoplasmic exosome (rnase complex) cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the exosome (rnase complex) cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the nuclear exosome (rnase complex) cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the cytoplasmic exosome (rnase complex) cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the exosome (rnase complex) cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From CORUM Protein Complexes

proteins in the Rnase/Mrp complex protein complex from the CORUM Protein Complexes dataset.

From GeneRIF Biological Term Annotations

genes co-occuring with the biological term rnase in literature-supported statements describing functions of genes from the GeneRIF Biological Term Annotations dataset.

From GO Cellular Component Annotations 2015

proteins localized to the cytoplasmic exosome (rnase complex) cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the exosome (rnase complex) cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the nuclear exosome (rnase complex) cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the RNase L inhibitor RLI, possible metal-binding domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Mut7-C RNAse domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Ribosomal protein L9/RNase H1, N-terminal protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the RNAse P, Rpr2/Rpp21 subunit protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the RNase P subunit p30 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the PNPase/RNase PH domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Exonuclease, RNase T/DNA polymerase III protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From GO Biological Process Annotations 2023

genes participating in the nuclear-transcribed mRNA catabolic process, RNase MRP-dependent biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the nucleolar exosome (RNase complex) cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the nucleolar exosome (RNase complex) cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Nuclear exosome (RNase complex) cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Exosome (RNase complex) cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Cytoplasmic exosome (RNase complex) cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Nucleolar exosome (RNase complex) cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Cytoplasmic exosome (RNase complex) cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Exosome (RNase complex) cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Nuclear exosome (RNase complex) cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From CM4AI U2OS Cell Map Protein Localization Assemblies

proteins comprising RNAse mitochondrial RNA processing (MRP) complex assembly using integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.