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HUMAN:RNAS2
Contents
| Species (Taxon ID) | Homo sapiens (Human). (9606) | |
| Gene Name(s) | RNASE2 (synonyms: EDN, RNS2) | |
| Protein Name(s) | Non-secretory ribonuclease
Eosinophil-derived neurotoxin RNase UpI-2 Ribonuclease 2 RNase 2 Ribonuclease US | |
| External Links | ||
| UniProt | P10153 | |
| EMBL | M30510 M28129 M24157 X16546 AF294007 AF294008 AF294009 AF294010 AF294011 AF294012 AF294013 AF294014 AF294015 X55987 X55988 BC093678 BC093680 BC096059 | |
| CCDS | CCDS9561.1 | |
| PIR | A35328 | |
| RefSeq | NP_002925.1 | |
| UniGene | Hs.728 | |
| PDB | 1GQV 1HI2 1HI3 1HI4 1HI5 1K2A 2BEX 2BZZ 2C01 2C02 2C05 | |
| PDBsum | 1GQV 1HI2 1HI3 1HI4 1HI5 1K2A 2BEX 2BZZ 2C01 2C02 2C05 | |
| ProteinModelPortal | P10153 | |
| SMR | P10153 | |
| BioGrid | 111965 | |
| STRING | 9606.ENSP00000303276 | |
| BindingDB | P10153 | |
| ChEMBL | CHEMBL5120 | |
| PhosphoSite | P10153 | |
| UniCarbKB | P10153 | |
| DMDM | 133168 | |
| PaxDb | P10153 | |
| PeptideAtlas | P10153 | |
| PRIDE | P10153 | |
| Ensembl | ENST00000304625 | |
| GeneID | 6036 | |
| KEGG | hsa:6036 | |
| UCSC | uc001vyl.1 | |
| CTD | 6036 | |
| GeneCards | GC14P021423 | |
| HGNC | HGNC:10045 | |
| HPA | HPA044983 | |
| MIM | 131410 | |
| neXtProt | NX_P10153 | |
| PharmGKB | PA34413 | |
| eggNOG | NOG39501 | |
| HOGENOM | HOG000276882 | |
| HOVERGEN | HBG008396 | |
| InParanoid | P10153 | |
| KO | K01168 | |
| OMA | TWAQWFE | |
| OrthoDB | EOG7KDFCP | |
| PhylomeDB | P10153 | |
| TreeFam | TF333393 | |
| ChiTaRS | RNASE2 | |
| EvolutionaryTrace | P10153 | |
| GeneWiki | Eosinophil-derived_neurotoxin | |
| GenomeRNAi | 6036 | |
| NextBio | 23525 | |
| PRO | PR:P10153 | |
| Proteomes | UP000005640 | |
| Bgee | P10153 | |
| CleanEx | HS_RNASE2 | |
| ExpressionAtlas | P10153 | |
| Genevestigator | P10153 | |
| GO | GO:0005576 GO:0070062 GO:0005764 GO:0003676 GO:0004522 GO:0004540 GO:0006935 GO:0006401 GO:0090501 | |
| Gene3D | 3.10.130.10 | |
| InterPro | IPR001427 IPR023411 IPR023412 | |
| PANTHER | PTHR11437 | |
| Pfam | PF00074 | |
| PRINTS | PR00794 | |
| ProDom | PD000535 | |
| SMART | SM00092 | |
| SUPFAM | SSF54076 | |
| PROSITE | PS00127 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0004540 |
ribonuclease activity |
ECO:0000314 |
F |
Coordinates siRNA amplification and mRNA cleavage during RNAi |
complete | |||||
|
enables |
GO:0004540 |
ribonuclease activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0090501 |
RNA phosphodiester bond hydrolysis |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0051607 |
defense response to virus |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
NOT|involved_in |
GO:0043152 |
induction of bacterial agglutination |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
NOT|enables |
GO:0001530 |
lipopolysaccharide binding |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
NOT|involved_in |
GO:0050829 |
defense response to Gram-negative bacterium |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
NOT|involved_in |
GO:0050830 |
defense response to Gram-positive bacterium |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0070062 |
extracellular exosome |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006935 |
chemotaxis |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004540 |
ribonuclease activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
MGI:MGI:104984 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0003676 |
nucleic acid binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006401 |
RNA catabolic process |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005576 |
extracellular region |
PMID:2734298[7] |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
|
C |
Seeded From UniProt |
complete | |
|
enables |
GO:0004540 |
ribonuclease activity |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0043312 |
neutrophil degranulation |
Reactome:R-HSA-6798695 |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
P |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0035578 |
azurophil granule lumen |
Reactome:R-HSA-6798751 |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
C |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0006935 |
chemotaxis |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004518 |
nuclease activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016787 |
hydrolase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004519 |
endonuclease activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005764 |
lysosome |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016829 |
lyase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Tsai, HY et al. (2015) A ribonuclease coordinates siRNA amplification and mRNA cleavage during RNAi. Cell 160 407-19 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 Domachowske, JB et al. (1998) Evolution of antiviral activity in the ribonuclease A gene superfamily: evidence for a specific interaction between eosinophil-derived neurotoxin (EDN/RNase 2) and respiratory syncytial virus. Nucleic Acids Res. 26 5327-32 PubMed GONUTS page
- ↑ 3.0 3.1 3.2 3.3 Pulido, D et al. (2013) Towards the rational design of antimicrobial proteins: single point mutations can switch on bactericidal and agglutinating activities on the RNase A superfamily lineage. FEBS J. 280 5841-52 PubMed GONUTS page
- ↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
- ↑ Yang, D et al. (2003) Eosinophil-derived neurotoxin (EDN), an antimicrobial protein with chemotactic activities for dendritic cells. Blood 102 3396-403 PubMed GONUTS page
- ↑ Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ 7.0 7.1 7.2 Rosenberg, HF et al. (1989) Molecular cloning of the human eosinophil-derived neurotoxin: a member of the ribonuclease gene family. Proc. Natl. Acad. Sci. U.S.A. 86 4460-4 PubMed GONUTS page
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