RNASE1 Gene

HGNC Family	Ribonucleases, RNase A (RNASE)
Name	ribonuclease, RNase A family, 1 (pancreatic)
Description	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]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nHuman pancreatic ribonuclease 1 (RNase1), a prominent member of the RNase A superfamily, is widely expressed – for example, by endothelial and epithelial cells – and exhibits exceptionally high catalytic activity against single‐ and double‐stranded RNA as well as RNA–DNA hybrids. Detailed biochemical and structural studies have revealed that its solution conformation is finely tuned by factors such as glycosylation and dynamic side‐chain rearrangements, which in turn modulate its interactions with endogenous inhibitors (including the cytosolic ribonuclease inhibitor) and influence substrate recognition. In addition, certain family members have been shown to display immunomodulatory properties by activating antigen‐presenting cells, while engineered variants with altered charge and nuclear localization signals demonstrate the potential for targeted intracellular RNA degradation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nSecreted RNase1 plays a critical role in extracellular RNA clearance and vascular homeostasis. It degrades extracellular RNA – a procoagulatory and permeability‐enhancing factor – thereby contributing to the protection of vessels and tissues during inflammatory states. Moreover, by selectively cleaving RNA substrates outside the cell, RNase1 not only helps generate discrete RNA fragments (such as tRNA halves and Y RNA fragments) that may participate in intercellular signaling, but it also holds promise as a biomarker for diseases (e.g., pancreatic cancer when differential glycosylation is considered) as well as in modulating tumor microenvironments, as suggested by its involvement in the enrichment of cancer stem-like cells."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "17"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nEfforts to harness RNase1’s potent catalytic activity have led to the generation of engineered variants with modified cellular uptake and subcellular trafficking. For example, the construction of cytotoxic forms endowed with extended nuclear localization signals (which promote selective nuclear import and subsequent RNA degradation) underscores its therapeutic potential. In parallel, investigations into domain swapping and oligomerization have provided insights into residue‐specific determinants that govern dimer formation and stability, further informing strategies to modulate its activity and specificity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "18", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Julien B P Landré, Peter W Hewett, Jean-Marc Olivot, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Human endothelial cells selectively express large amounts of pancreatic-type ribonuclease (RNase 1)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Biochem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/jcb.10234"}], "href": "https://doi.org/10.1002/jcb.10234"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12210760"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12210760"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Deepak Gaur, Divya Seth, Janendra K Batra "}, {"type": "b", "children": [{"type": "t", "text": "Glycine 38 is crucial for the ribonucleolytic activity of human pancreatic ribonuclease on double-stranded RNA."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/s0006-291x(02)02216-7"}], "href": "https://doi.org/10.1016/s0006-291x(02"}, {"type": "t", "text": "02216-7) PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12237131"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12237131"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "De Yang, Qian Chen, Helene F Rosenberg, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Human ribonuclease A superfamily members, eosinophil-derived neurotoxin and pancreatic ribonuclease, induce dendritic cell maturation and activation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Immunol (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.4049/jimmunol.173.10.6134"}], "href": "https://doi.org/10.4049/jimmunol.173.10.6134"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15528350"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15528350"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "M Rodríguez, A Benito, P Tubert, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A cytotoxic ribonuclease variant with a discontinuous nuclear localization signal constituted by basic residues scattered over three areas of the molecule."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Mol Biol (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.jmb.2006.05.048"}], "href": "https://doi.org/10.1016/j.jmb.2006.05.048"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16780873"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16780873"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "R Jeremy Johnson, Jason G McCoy, Craig A Bingman, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Inhibition of human pancreatic ribonuclease by the human ribonuclease inhibitor protein."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Mol Biol (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.jmb.2007.02.005"}], "href": "https://doi.org/10.1016/j.jmb.2007.02.005"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17350650"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17350650"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "R Jeremy Johnson, Tzu-Yuan Chao, Luke D Lavis, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cytotoxic ribonucleases: the dichotomy of Coulombic forces."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochemistry (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/bi700857u"}], "href": "https://doi.org/10.1021/bi700857u"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17705507"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17705507"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Misuzu Ueki, Reiko Iida, Junko Fujihara, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Development of genotyping methods for single nucleotide polymorphism in the human pancreatic ribonuclease gene (RNASE1) and their application to population studies."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Genet (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s10528-007-9138-2"}], "href": "https://doi.org/10.1007/s10528-007-9138-2"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18219569"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18219569"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "K E Kövér, M Bruix, J Santoro, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The solution structure and dynamics of human pancreatic ribonuclease determined by NMR spectroscopy provide insight into its remarkable biological activities and inhibition."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Mol Biol (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.jmb.2008.04.042"}], "href": "https://doi.org/10.1016/j.jmb.2008.04.042"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18495155"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18495155"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Giuseppe D'Alessio "}, {"type": "b", "children": [{"type": "t", "text": "It takes two to flirt with a dimeric RNase."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biopolymers (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/bip.21145"}], "href": "https://doi.org/10.1002/bip.21145"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19156888"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19156888"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Silvia Fischer, Miwako Nishio, Sara Dadkhahi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Expression and localisation of vascular ribonucleases in endothelial cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Thromb Haemost (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1160/TH10-06-0345"}], "href": "https://doi.org/10.1160/TH10-06-0345"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21103661"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21103661"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Md Tabish Rehman, Punyatirtha Dey, Md Imtaiyaz Hassan, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Functional role of glutamine 28 and arginine 39 in double stranded RNA cleavage by human pancreatic ribonuclease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS One (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pone.0017159"}], "href": "https://doi.org/10.1371/journal.pone.0017159"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21408145"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21408145"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Daisuke Nakata "}, {"type": "b", "children": [{"type": "t", "text": "Increased N-glycosylation of Asn⁸⁸ in serum pancreatic ribonuclease 1 is a novel diagnostic marker for pancreatic cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/srep06715"}], "href": "https://doi.org/10.1038/srep06715"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25336120"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25336120"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Sydney P Thomas, Eunji Kim, Jin-Soo Kim, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Knockout of the Ribonuclease Inhibitor Gene Leaves Human Cells Vulnerable to Secretory Ribonucleases."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochemistry (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/acs.biochem.6b01003"}], "href": "https://doi.org/10.1021/acs.biochem.6b01003"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27806571"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27806571"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Valerie T Ressler, Ronald T Raines "}, {"type": "b", "children": [{"type": "t", "text": "Consequences of the Endogenous N-Glycosylation of Human Ribonuclease 1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochemistry (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/acs.biochem.8b01246"}], "href": "https://doi.org/10.1021/acs.biochem.8b01246"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30633504"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30633504"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Katrin Bedenbender, Nicoletta Scheller, Silvia Fischer, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Inflammation-mediated deacetylation of the ribonuclease 1 promoter "}, {"type": "a", "children": [{"type": "t", "text": "i"}], "href": "i"}, {"type": "t", "text": "via"}, {"type": "a", "children": [{"type": "t", "text": "/i"}], "href": "/i"}, {"type": "t", "text": " histone deacetylase 2 in endothelial cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FASEB J (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1096/fj.201900451R"}], "href": "https://doi.org/10.1096/fj.201900451R"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31039328"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31039328"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Gal Nechooshtan, Dinar Yunusov, Kenneth Chang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Processing by RNase 1 forms tRNA halves and distinct Y RNA fragments in the extracellular environment."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nucleic Acids Res (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/nar/gkaa526"}], "href": "https://doi.org/10.1093/nar/gkaa526"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32609822"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32609822"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Heng-Huan Lee, Ying-Nai Wang, Wen-Hao Yang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Human ribonuclease 1 serves as a secretory ligand of ephrin A4 receptor and induces breast tumor initiation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41467-021-23075-2"}], "href": "https://doi.org/10.1038/s41467-021-23075-2"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33986289"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33986289"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Pere Tubert, Montserrat Rodríguez, Marc Ribó, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The nuclear transport capacity of a human-pancreatic ribonuclease variant is critical for its cytotoxicity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Invest New Drugs (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s10637-010-9426-2"}], "href": "https://doi.org/10.1007/s10637-010-9426-2"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20352290"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20352290"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Pere Tubert, Douglas V Laurents, Marc Ribó, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Interactions crucial for three-dimensional domain swapping in the HP-RNase variant PM8."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biophys J (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bpj.2011.06.013"}], "href": "https://doi.org/10.1016/j.bpj.2011.06.013"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21767499"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21767499"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Andrea Pica, Antonello Merlino, Alexander K Buell, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Three-dimensional domain swapping and supramolecular protein assembly: insights from the X-ray structure of a dimeric swapped variant of human pancreatic RNase."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Acta Crystallogr D Biol Crystallogr (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1107/S0907444913020507"}], "href": "https://doi.org/10.1107/S0907444913020507"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24100329"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24100329"}]}]}]}
Synonyms	RIB1, RNS1, RAC1
Proteins	RNAS1_HUMAN
NCBI Gene ID	6035
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

RNASE1 has 12,090 functional associations with biological entities spanning 9 categories (molecular profile, organism, chemical, disease, phenotype or trait, functional term, phrase or reference, structural feature, cell line, cell type or tissue, gene, protein or microRNA, sequence feature) extracted from 117 datasets.

Click the + buttons to view associations for RNASE1 from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

RNASE1 Gene

Functional Associations

Please acknowledge the Harmonizome in your publications by citing the following reference(s):

	Dataset	Summary
	Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of RNASE1 gene relative to other tissues from the Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles dataset.
	Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles	tissues with high or low expression of RNASE1 gene relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.
	Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles	tissue samples with high or low expression of RNASE1 gene relative to other tissue samples from the Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles dataset.
	Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by Microarray	tissue samples with high or low expression of RNASE1 gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by Microarray dataset.
	Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq	tissue samples with high or low expression of RNASE1 gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq dataset.
	Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of RNASE1 gene relative to other tissues from the Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles dataset.
	BioGPS Cell Line Gene Expression Profiles	cell lines with high or low expression of RNASE1 gene relative to other cell lines from the BioGPS Cell Line Gene Expression Profiles dataset.
	BioGPS Human Cell Type and Tissue Gene Expression Profiles	cell types and tissues with high or low expression of RNASE1 gene relative to other cell types and tissues from the BioGPS Human Cell Type and Tissue Gene Expression Profiles dataset.
	BioGPS Mouse Cell Type and Tissue Gene Expression Profiles	cell types and tissues with high or low expression of RNASE1 gene relative to other cell types and tissues from the BioGPS Mouse Cell Type and Tissue Gene Expression Profiles dataset.
	Carcinogenome Chemical Perturbation Carcinogenicity Signatures	small molecule perturbations changing expression of RNASE1 gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of RNASE1 gene relative to other cell lines from the CCLE Cell Line Gene CNV Profiles dataset.
	CCLE Cell Line Gene Expression Profiles	cell lines with high or low expression of RNASE1 gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with RNASE1 gene from the CellMarker Gene-Cell Type Associations dataset.
	ChEA Transcription Factor Binding Site Profiles	transcription factor binding site profiles with transcription factor binding evidence at the promoter of RNASE1 gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of RNASE1 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets dataset.
	ChEA Transcription Factor Targets 2022	transcription factors binding the promoter of RNASE1 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset.
	ClinVar Gene-Phenotype Associations 2025	phenotypes associated with RNASE1 gene from the curated ClinVar Gene-Phenotype Associations 2025 dataset.
	CM4AI KOLF21J CRISPRi Gene Perturbation Atlas	gene perturbations changing expression of RNASE1 gene from the CM4AI KOLF21J CRISPRi Gene Perturbation Atlas dataset.
	CM4AI U2OS Cell Map Protein Localization Assemblies	assemblies containing RNASE1 protein from integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.
	CMAP Signatures of Differentially Expressed Genes for Small Molecules	small molecule perturbations changing expression of RNASE1 gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing RNASE1 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing RNASE1 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores	cellular components co-occuring with RNASE1 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025	cellular components co-occuring with RNASE1 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.
	COSMIC Cell Line Gene CNV Profiles	cell lines with high or low copy number of RNASE1 gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with RNASE1 gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Disease Associations	diseases associated with RNASE1 gene/protein from the curated CTD Gene-Disease Associations dataset.
	DepMap CRISPR Gene Dependency	cell lines with fitness changed by RNASE1 gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DGIdb Drug Targets 2026	interacting drugs for RNASE1 protein from the DGIdb Drug Targets 2026 dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with RNASE1 gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores 2025	diseases co-occuring with RNASE1 gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.
	DisGeNET Gene-Disease Associations	diseases associated with RNASE1 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with RNASE1 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Phenoptype Associations dataset.
	DrugBank Drug Targets	interacting drugs for RNASE1 protein from the curated DrugBank Drug Targets dataset.
	ENCODE Histone Modification Site Profiles	histone modification site profiles with high histone modification abundance at RNASE1 gene from the ENCODE Histone Modification Site Profiles dataset.
	ENCODE Transcription Factor Binding Site Profiles	transcription factor binding site profiles with transcription factor binding evidence at the promoter of RNASE1 gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of RNASE1 gene in ChIP-seq datasets from the ENCODE Transcription Factor Targets dataset.
	ESCAPE Omics Signatures of Genes and Proteins for Stem Cells	PubMedIDs of publications reporting gene signatures containing RNASE1 from the ESCAPE Omics Signatures of Genes and Proteins for Stem Cells dataset.
	GAD Gene-Disease Associations	diseases associated with RNASE1 gene in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.
	GAD High Level Gene-Disease Associations	diseases associated with RNASE1 gene in GWAS and other genetic association datasets from the GAD High Level Gene-Disease Associations dataset.