UniProtKB - P61823 (RNAS1_BOVIN)
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- BLAST>sp|P61823|RNAS1_BOVIN Ribonuclease pancreatic OS=Bos taurus OX=9913 GN=RNASE1 PE=1 SV=1 MALKSLVLLSLLVLVLLLVRVQPSLGKETAAAKFERQHMDSSTSAASSSNYCNQMMKSRN LTKDRCKPVNTFVHESLADVQAVCSQKNVACKNGQTNCYQSYSTMSITDCRETGSSKYPN CAYKTTQANKHIIVACEGNPYVPVHFDASV
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Ribonuclease pancreatic
RNASE1
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.3"Engineering ribonuclease A: production, purification and characterization of wild-type enzyme and mutants at Gln11."
Delcardayre S.B., Ribo M., Yokel E.M., Quirk D.J., Rutter W.J., Raines R.T.
Protein Eng. 8:261-273(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 23-150, FUNCTION.
Miscellaneous
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 33 | Substrate | 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 36 | Substrate | 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 38 | Proton acceptor | 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 92 | Substrate | 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 111 | Substrate | 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 145 | Proton donor | 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- endonuclease activity Source: GO_Central
- nucleic acid binding Source: InterPro
- ribonuclease A activity Source: UniProtKB-EC
- ribonuclease activity Source: GO_Central
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Endonuclease, Hydrolase, Nuclease |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.1.27.5 908 |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P61823 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:RNASE1 Synonyms:RNS1 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Bos taurus (Bovine) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9913 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
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<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Extracellular region or secreted
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Secreted<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 38 | H → A: Loss of activity. | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 145 | H → A: Loss of activity. | 1 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL6091 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 26 | 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 26 | |
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000030915 | 27 – 150 | Ribonuclease pancreaticAdd BLAST | 124 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 27 | N-linked (Glc) (glycation) lysine; in vitro | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 33 | N-linked (Glc) (glycation) lysine; in vitro | 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 52 ↔ 110 | 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>GlycosylationiCAR_000006 | 60 | N-linked (GlcNAc...) asparagine; partial1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 63 | N-linked (Glc) (glycation) lysine; in vitro | 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 66 ↔ 121 | 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 67 | N-linked (Glc) (glycation) lysine; in vitro | 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 84 ↔ 136 | 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 91 ↔ 98 | 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
|
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Disulfide bond, Glycation, GlycoproteinProteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P61823 |
PeptideAtlas More...PeptideAtlasi | P61823 |
PRoteomics IDEntifications database More...PRIDEi | P61823 |
PTM databases
CarbonylDB database of protein carbonylation sites More...CarbonylDBi | P61823 |
GlyConnect protein glycosylation platform More...GlyConnecti | 529 |
UniCarbKB; an annotated and curated database of glycan structures More...UniCarbKBi | P61823 |
Miscellaneous databases
CutDB - Proteolytic event database More...PMAP-CutDBi | P61823 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSBTAG00000008793 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.19"Cleavage of 3',5'-pyrophosphate-linked dinucleotides by ribonuclease A and angiogenin."
Jardine A.M., Leonidas D.D., Jenkins J.L., Park C., Raines R.T., Acharya K.R., Shapiro R.
Biochemistry 40:10262-10272(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| Fbxo2 | Q80UW2 | 2 | EBI-908364,EBI-2314714 | From Mus musculus. |
| PDI1 | P17967 | 2 | EBI-908364,EBI-13012 | From Saccharomyces cerevisiae (strain ATCC 204508 / S288c). |
| RNH1 | P13489 | 3 | EBI-908364,EBI-1237106 | From Homo sapiens. |
Protein-protein interaction databases
Database of interacting proteins More...DIPi | DIP-36384N |
Protein interaction database and analysis system More...IntActi | P61823, 8 interactors |
Molecular INTeraction database More...MINTi | P61823 |
STRING: functional protein association networks More...STRINGi | 9913.ENSBTAP00000011586 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P61823 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 30 – 38 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 43 – 45 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 48 – 50 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 51 – 58 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 59 – 62 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 63 – 65 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 68 – 73 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 77 – 81 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 82 – 85 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 86 – 89 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 92 – 94 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 98 – 100 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 105 – 112 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 118 – 120 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 123 – 130 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 132 – 137 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 138 – 141 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 142 – 149 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P61823 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P61823 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P61823 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 67 – 71 | Substrate binding | 5 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
SignalPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IYEN Eukaryota ENOG41113F1 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00900000140967 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000276883 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG008396 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P61823 |
KEGG Orthology (KO) More...KOi | K01168 |
Identification of Orthologs from Complete Genome Data More...OMAi | ACKNGQT |
Database of Orthologous Groups More...OrthoDBi | EOG091G15X3 |
TreeFam database of animal gene trees More...TreeFami | TF333393 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.10.130.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001427 RNaseA IPR036816 RNaseA-like_dom_sf IPR023411 RNaseA_AS IPR023412 RNaseA_domain |
The PANTHER Classification System More...PANTHERi | PTHR11437 PTHR11437, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00074 RnaseA, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00794 RIBONUCLEASE |
ProDom; a protein domain database More...ProDomi | View protein in ProDom or Entries sharing at least one domain PD000535 RNaseA, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00092 RNAse_Pc, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF54076 SSF54076, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00127 RNASE_PANCREATIC, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
10 20 30 40 50
MALKSLVLLS LLVLVLLLVR VQPSLGKETA AAKFERQHMD SSTSAASSSN
60 70 80 90 100
YCNQMMKSRN LTKDRCKPVN TFVHESLADV QAVCSQKNVA CKNGQTNCYQ
110 120 130 140 150
SYSTMSITDC RETGSSKYPN CAYKTTQANK HIIVACEGNP YVPVHFDASV
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X07283 Genomic DNA Translation: CAA30263.1 BC149529 mRNA Translation: AAI49530.1 BC149636 mRNA Translation: AAI49637.1 S80747 mRNA Translation: AAB35594.1 S81740 Genomic DNA Translation: AAB36134.1 |
Protein sequence database of the Protein Information Resource More...PIRi | S00897 NRBO |
NCBI Reference Sequences More...RefSeqi | NP_001014408.2, NM_001014386.4 XP_005211519.1, XM_005211462.2 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Bt.4630 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENSBTAT00000011586; ENSBTAP00000011586; ENSBTAG00000008793 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 282340 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | bta:282340 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P61823 | Ribonuclease A C2 | 215 | |||
| UPI0000110AED | 128 | ||||
| UPI0000112D34 | 113 | ||||
| UPI0000112D39 | 112 | ||||
| UPI0000112D2D | 118 |
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P61823 | Ribonuclease A C2 | 215 | |||
| UPI0000110AED | 128 | ||||
| UPI0000112D34 | 113 | ||||
| UPI0000112D39 | 112 | ||||
| UPI0000112D2D | 118 |
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P61823 | Ribonuclease A C2 | 215 | |||
| UPI0003C11D0F | 264 | ||||
| Ribonuclease pancreatic B | 128 | ||||
| UPI000719FDDC | 228 | ||||
| UPI0003ACB335 | 228 | ||||
| +14 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| Worthington enzyme manual |
| Functional Glycomics Gateway - Glycan Binding RNase A |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X07283 Genomic DNA Translation: CAA30263.1 BC149529 mRNA Translation: AAI49530.1 BC149636 mRNA Translation: AAI49637.1 S80747 mRNA Translation: AAB35594.1 S81740 Genomic DNA Translation: AAB36134.1 |
Protein sequence database of the Protein Information Resource More...PIRi | S00897 NRBO |
NCBI Reference Sequences More...RefSeqi | NP_001014408.2, NM_001014386.4 XP_005211519.1, XM_005211462.2 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Bt.4630 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1A2W | X-ray | 2.10 | A/B | 27-150 | [»] | |
| 1A5P | X-ray | 1.60 | A | 27-150 | [»] | |
| 1A5Q | X-ray | 2.30 | A | 27-150 | [»] | |
| 1AFK | X-ray | 1.70 | A/B | 27-150 | [»] | |
| 1AFL | X-ray | 1.70 | A/B | 27-150 | [»] | |
| 1AFU | X-ray | 2.00 | A/B | 27-150 | [»] | |
| 1AQP | X-ray | 2.00 | A | 27-150 | [»] | |
| 1B6V | X-ray | 2.00 | A/B | 27-150 | [»] | |
| 1BEL | X-ray | 1.60 | A | 27-150 | [»] | |
| 1BZQ | X-ray | 2.80 | A/B/C/D | 27-150 | [»] | |
| 1C0B | X-ray | 1.90 | A | 23-150 | [»] | |
| 1C0C | X-ray | 2.00 | A | 23-150 | [»] | |
| 1C8W | X-ray | 1.80 | A | 27-150 | [»] | |
| 1C9V | X-ray | 1.70 | A | 27-150 | [»] | |
| 1C9X | X-ray | 1.80 | A | 27-150 | [»] | |
| 1CJQ | X-ray | 3.00 | A | 27-41 | [»] | |
| B | 50-150 | [»] | ||||
| 1CJR | X-ray | 2.30 | A | 27-41 | [»] | |
| B | 50-150 | [»] | ||||
| 1D5D | X-ray | 2.25 | A | 27-41 | [»] | |
| B | 50-150 | [»] | ||||
| 1D5E | X-ray | 2.25 | A | 27-41 | [»] | |
| B | 50-150 | [»] | ||||
| 1D5H | X-ray | 2.25 | A | 27-41 | [»] | |
| B | 50-150 | [»] | ||||
| 1DFJ | X-ray | 2.50 | E | 27-150 | [»] | |
| 1DY5 | X-ray | 0.87 | A/B | 27-150 | [»] | |
| 1EIC | X-ray | 1.40 | A | 27-150 | [»] | |
| 1EID | X-ray | 1.40 | A | 27-150 | [»] | |
| 1EIE | X-ray | 1.40 | A | 27-150 | [»] | |
| 1EOS | X-ray | 2.00 | A/B | 27-150 | [»] | |
| 1EOW | X-ray | 2.00 | A | 27-150 | [»] | |
| 1F0V | X-ray | 1.70 | A/B/C/D | 27-150 | [»] | |
| 1FEV | X-ray | 2.25 | A | 27-41 | [»] | |
| B | 50-150 | [»] | ||||
| 1FS3 | X-ray | 1.40 | A | 27-150 | [»] | |
| 1GV7 | X-ray | 2.10 | A | 84-99 | [»] | |
| 1IZP | X-ray | 1.50 | A | 27-150 | [»] | |
| 1IZQ | X-ray | 1.80 | A | 27-150 | [»] | |
| 1IZR | X-ray | 1.50 | A | 27-150 | [»] | |
| 1J7Z | X-ray | 2.25 | A | 27-41 | [»] | |
| B | 47-150 | [»] | ||||
| 1J80 | X-ray | 2.10 | A | 27-41 | [»] | |
| B | 47-150 | [»] | ||||
| 1J81 | X-ray | 2.20 | A | 27-41 | [»] | |
| B | 47-150 | [»] | ||||
| 1J82 | X-ray | 2.30 | A | 27-41 | [»] | |
| B | 47-150 | [»] | ||||
| 1JN4 | X-ray | 1.80 | A/B | 27-150 | [»] | |
| 1JS0 | X-ray | 2.20 | A/B/C | 27-150 | [»] | |
| 1JVT | X-ray | 2.05 | A/B | 27-150 | [»] | |
| 1JVU | X-ray | 1.78 | A/B | 27-150 | [»] | |
| 1JVV | X-ray | 2.20 | A/B | 27-150 | [»] | |
| 1KF2 | X-ray | 1.10 | A | 27-150 | [»] | |
| 1KF3 | X-ray | 1.05 | A | 27-150 | [»] | |
| 1KF4 | X-ray | 1.10 | A | 27-150 | [»] | |
| 1KF5 | X-ray | 1.15 | A | 27-150 | [»] | |
| 1KF7 | X-ray | 1.15 | A | 27-150 | [»] | |
| 1KF8 | X-ray | 1.15 | A | 27-150 | [»] | |
| 1KH8 | X-ray | 2.00 | A | 27-150 | [»] | |
| 1LSQ | X-ray | 1.90 | A/B | 27-150 | [»] | |
| 1O0F | X-ray | 1.50 | A/B | 27-150 | [»] | |
| 1O0H | X-ray | 1.20 | A/B | 27-150 | [»] | |
| 1O0M | X-ray | 1.50 | A/B | 27-150 | [»] | |
| 1O0N | X-ray | 1.50 | A/B | 27-150 | [»] | |
| 1O0O | X-ray | 1.20 | A/B | 27-150 | [»] | |
| 1QHC | X-ray | 1.70 | A/B | 27-150 | [»] | |
| 1RAR | X-ray | 1.90 | A | 28-150 | [»] | |
| 1RAS | X-ray | 1.70 | A | 28-150 | [»] | |
| 1RAT | X-ray | 1.50 | A | 27-150 | [»] | |
| 1RBB | X-ray | 2.50 | A/B | 27-150 | [»] | |
| 1RBC | X-ray | 2.00 | A | 47-150 | [»] | |
| S | 27-41 | [»] | ||||
| 1RBD | X-ray | 1.70 | A | 47-150 | [»] | |
| S | 27-41 | [»] | ||||
| 1RBE | X-ray | 1.75 | A | 47-150 | [»] | |
| S | 27-41 | [»] | ||||
| 1RBF | X-ray | 1.80 | A | 47-150 | [»] | |
| S | 27-41 | [»] | ||||
| 1RBG | X-ray | 1.80 | A | 47-150 | [»] | |
| S | 27-41 | [»] | ||||
| 1RBH | X-ray | 1.70 | A | 47-150 | [»] | |
| S | 27-41 | [»] | ||||
| 1RBI | X-ray | 1.80 | A | 47-150 | [»] | |
| S | 27-41 | [»] | ||||
| 1RBJ | X-ray | 2.70 | A | 27-150 | [»] | |
| 1RBN | X-ray | 2.10 | A | 27-150 | [»] | |
| 1RBW | X-ray | 1.69 | A | 27-150 | [»] | |
| 1RBX | X-ray | 1.69 | A | 27-150 | [»] | |
| 1RCA | X-ray | 1.90 | A | 27-150 | [»] | |
| 1RCN | X-ray | 2.32 | E | 27-150 | [»] | |
| 1RHA | X-ray | 1.80 | A | 27-150 | [»] | |
| 1RHB | X-ray | 1.50 | A | 27-150 | [»] | |
| 1RNC | X-ray | 1.50 | A | 27-150 | [»] | |
| 1RND | X-ray | 1.50 | A | 27-150 | [»] | |
| 1RNM | X-ray | 2.00 | E | 27-150 | [»] | |
| 1RNN | X-ray | 1.80 | E | 27-150 | [»] | |
| 1RNO | X-ray | 1.90 | A | 27-150 | [»] | |
| 1RNQ | X-ray | 2.00 | A | 27-150 | [»] | |
| 1RNU | X-ray | 1.60 | A | 27-150 | [»] | |
| 1RNV | X-ray | 1.60 | A | 27-150 | [»] | |
| 1RNW | X-ray | 1.80 | A | 27-150 | [»] | |
| 1RNX | X-ray | 1.90 | A | 27-150 | [»] | |
| 1RNY | X-ray | 2.00 | A | 27-150 | [»] | |
| 1RNZ | X-ray | 1.90 | A | 27-150 | [»] | |
| 1ROB | X-ray | 1.60 | A | 27-150 | [»] | |
| 1RPF | X-ray | 2.20 | A | 27-150 | [»] | |
| 1RPG | X-ray | 1.40 | A | 27-150 | [»] | |
| 1RPH | X-ray | 2.20 | A | 27-150 | [»] | |
| 1RSM | X-ray | 2.00 | A | 27-150 | [»] | |
| 1RTA | X-ray | 2.50 | E | 27-150 | [»] | |
| 1RTB | X-ray | 2.50 | A | 27-150 | [»] | |
| 1RUV | X-ray | 1.25 | A | 27-150 | [»] | |
| 1SRN | X-ray | 1.80 | A | 27-144 | [»] | |
| B | 137-150 | [»] | ||||
| 1SSA | X-ray | 2.00 | A | 27-144 | [»] | |
| B | 137-150 | [»] | ||||
| 1SSB | X-ray | 2.00 | A | 27-144 | [»] | |
| B | 137-150 | [»] | ||||
| 1SSC | X-ray | 2.00 | A | 27-138 | [»] | |
| B | 140-150 | [»] | ||||
| 1U1B | X-ray | 2.00 | A/B | 27-150 | [»] | |
| 1UN5 | X-ray | 2.60 | A | 64-74 | [»] | |
| 1W4O | X-ray | 1.60 | A/B | 27-150 | [»] | |
| 1W4P | X-ray | 1.69 | A/B | 27-150 | [»] | |
| 1W4Q | X-ray | 1.68 | A/B | 27-150 | [»] | |
| 1WBU | X-ray | 1.90 | A/B | 27-150 | [»] | |
| 1XPS | X-ray | 1.80 | A/B | 27-150 | [»] | |
| 1XPT | X-ray | 1.90 | A/B | 27-150 | [»] | |
| 1YMN | X-ray | 1.45 | A | 27-150 | [»] | |
| 1YMR | X-ray | 1.50 | A | 27-150 | [»] | |
| 1YMW | X-ray | 1.50 | A | 27-150 | [»] | |
| 1Z3L | X-ray | 1.80 | E | 47-150 | [»] | |
| S | 27-41 | [»] | ||||
| 1Z3M | X-ray | 2.00 | E | 47-150 | [»] | |
| S | 27-41 | [»] | ||||
| 1Z3P | X-ray | 2.00 | E | 47-150 | [»] | |
| S | 27-41 | [»] | ||||
| 1Z6D | X-ray | 1.54 | A/B | 27-150 | [»] | |
| 1Z6S | X-ray | 1.50 | A/B | 27-150 | [»] | |
| 2AAS | NMR | - | A | 27-150 | [»] | |
| 2APQ | X-ray | 1.80 | A | 27-150 | [»] | |
| 2APU | model | - | 0/1/2/3/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x/y/z | 27-150 | [»] | |
| 2BLP | X-ray | 1.40 | A | 27-150 | [»] | |
| 2BLZ | X-ray | 1.40 | A | 27-150 | [»] | |
| 2E33 | X-ray | 2.70 | B | 27-150 | [»] | |
| 2E3W | X-ray | 1.05 | A | 27-150 | [»] | |
| 2G4W | X-ray | 1.84 | A/B | 27-150 | [»] | |
| 2G4X | X-ray | 1.95 | A | 27-150 | [»] | |
| 2G8Q | X-ray | 1.50 | A/B | 27-150 | [»] | |
| 2G8R | X-ray | 1.70 | A/B | 27-150 | [»] | |
| 2NUI | X-ray | 1.10 | A | 27-150 | [»] | |
| 2OP2 | X-ray | 1.60 | A | 27-150 | [»] | |
| 2OQF | X-ray | 2.30 | A/B/C/D | 27-150 | [»] | |
| 2P42 | X-ray | 1.80 | A/C | 27-150 | [»] | |
| 2P43 | X-ray | 1.65 | A | 27-150 | [»] | |
| 2P44 | X-ray | 1.80 | A | 27-150 | [»] | |
| 2P45 | X-ray | 1.10 | A | 27-150 | [»] | |
| 2P46 | X-ray | 2.50 | A/C | 27-150 | [»] | |
| 2P47 | X-ray | 2.50 | A | 27-150 | [»] | |
| 2P48 | X-ray | 2.30 | A | 27-150 | [»] | |
| 2P49 | X-ray | 1.38 | A | 27-150 | [»] | |
| 2P4A | X-ray | 1.90 | A/C | 27-150 | [»] | |
| 2QCA | X-ray | 1.33 | A | 27-150 | [»] | |
| 2RAT | X-ray | 1.50 | A | 27-150 | [»] | |
| 2RLN | X-ray | 1.85 | E | 42-150 | [»] | |
| S | 27-41 | [»] | ||||
| 2RNS | X-ray | 1.60 | A | 27-150 | [»] | |
| 2W5G | X-ray | 1.70 | A/B | 27-150 | [»] | |
| 2W5I | X-ray | 2.40 | A/B | 27-150 | [»] | |
| 2W5K | X-ray | 1.70 | A/B | 27-150 | [»] | |
| 2W5L | X-ray | 1.70 | A/B | 27-150 | [»] | |
| 2W5M | X-ray | 1.80 | A/B | 27-150 | [»] | |
| 2XOG | X-ray | 1.72 | A/B | 27-150 | [»] | |
| 2XOI | X-ray | 1.72 | A/B | 27-150 | [»] | |
| 3A1R | neutron diffraction | 1.70 | A | 27-150 | [»] | |
| 3D6O | X-ray | 1.58 | A/B | 27-150 | [»] | |
| 3D6P | X-ray | 1.60 | A/B | 27-150 | [»] | |
| 3D6Q | X-ray | 1.60 | A/B | 27-150 | [»] | |
| 3D7B | X-ray | 1.60 | A/B | 27-150 | [»] | |
| 3D8Y | X-ray | 1.72 | A/B | 27-150 | [»] | |
| 3D8Z | X-ray | 1.98 | A/B | 27-150 | [»] | |
| 3DH5 | X-ray | 1.60 | A | 27-150 | [»] | |
| 3DH6 | X-ray | 1.60 | A | 27-150 | [»] | |
| 3DI7 | X-ray | 1.60 | A | 27-150 | [»] | |
| 3DI8 | X-ray | 1.60 | A | 27-150 | [»] | |
| 3DI9 | X-ray | 2.00 | A | 27-150 | [»] | |
| 3DIB | X-ray | 1.40 | A | 27-150 | [»] | |
| 3DIC | X-ray | 1.60 | A | 27-150 | [»] | |
| 3DXG | X-ray | 1.39 | A/B | 27-150 | [»] | |
| 3DXH | X-ray | 1.40 | A/B | 27-150 | [»] | |
| 3EUX | X-ray | 1.65 | A/B | 27-150 | [»] | |
| 3EUY | X-ray | 1.95 | A/B | 27-150 | [»] | |
| 3EUZ | X-ray | 1.84 | A/B | 27-150 | [»] | |
| 3EV0 | X-ray | 1.76 | A/B | 27-150 | [»] | |
| 3EV1 | X-ray | 2.00 | A/B | 27-150 | [»] | |
| 3EV2 | X-ray | 2.02 | A/B | 27-150 | [»] | |
| 3EV3 | X-ray | 1.68 | A/B | 27-150 | [»] | |
| 3EV4 | X-ray | 1.93 | A/B | 27-150 | [»] | |
| 3EV5 | X-ray | 1.68 | A/B | 27-150 | [»] | |
| 3EV6 | X-ray | 1.76 | A/B | 27-150 | [»] | |
| 3FKZ | X-ray | 1.99 | A/B | 27-150 | [»] | |
| 3FL0 | X-ray | 1.94 | A/B | 27-150 | [»] | |
| 3FL1 | X-ray | 1.90 | A/B | 27-150 | [»] | |
| 3FL3 | X-ray | 1.60 | A/B | 27-150 | [»] | |
| 3I67 | X-ray | 1.30 | A | 27-150 | [»] | |
| 3I6F | X-ray | 1.30 | A | 27-150 | [»] | |
| 3I6H | X-ray | 1.30 | A | 27-150 | [»] | |
| 3I6J | X-ray | 1.30 | A | 27-150 | [»] | |
| 3I7W | X-ray | 2.35 | A | 27-150 | [»] | |
| 3I7X | X-ray | 2.60 | A | 27-150 | [»] | |
| 3I7Y | X-ray | 2.40 | A | 27-150 | [»] | |
| 3JW1 | X-ray | 1.60 | A/B | 27-150 | [»] | |
| 3LXO | X-ray | 1.55 | A | 27-150 | [»] | |
| 3MWQ | X-ray | 1.68 | A | 26-150 | [»] | |
| 3MWR | X-ray | 1.85 | A | 27-150 | [»] | |
| 3MX8 | X-ray | 2.10 | A | 26-150 | [»] | |
| 3MZQ | X-ray | 1.50 | A | 23-150 | [»] | |
| 3MZR | X-ray | 1.50 | A | 23-150 | [»] | |
| 3OQY | X-ray | 1.49 | A/B | 47-150 | [»] | |
| a/b | 27-41 | [»] | ||||
| 3OQZ | X-ray | 2.50 | A/B | 47-150 | [»] | |
| a/b | 27-41 | [»] | ||||
| 3OR0 | X-ray | 2.30 | A/B | 47-150 | [»] | |
| a/b | 27-41 | [»] | ||||
| 3QL1 | X-ray | 1.29 | A | 27-150 | [»] | |
| 3QL2 | X-ray | 1.49 | A/B | 27-150 | [»] | |
| 3QSK | X-ray | 1.75 | A | 27-150 | [»] | |
| 3RAT | X-ray | 1.50 | A | 27-150 | [»] | |
| 3RH1 | X-ray | 2.10 | A | 27-150 | [»] | |
| 3RID | X-ray | 2.18 | A/B/C/D | 27-150 | [»] | |
| 3RN3 | X-ray | 1.45 | A | 27-150 | [»] | |
| 3RSD | X-ray | 1.60 | A | 27-150 | [»] | |
| 3RSK | X-ray | 2.00 | A | 27-150 | [»] | |
| 3RSP | X-ray | 1.70 | A | 27-150 | [»] | |
| 3SRN | X-ray | 2.00 | A | 27-139 | [»] | |
| B | 140-146 | [»] | ||||
| 4AO1 | X-ray | 1.58 | A | 27-150 | [»] | |
| 4G8V | X-ray | 1.70 | A/B | 27-150 | [»] | |
| 4G8Y | X-ray | 1.80 | A/B | 27-150 | [»] | |
| 4G90 | X-ray | 1.90 | A/B | 27-150 | [»] | |
| 4J5Z | X-ray | 1.80 | A | 27-150 | [»] | |
| 4J60 | X-ray | 1.69 | A | 27-150 | [»] | |
| 4J61 | X-ray | 1.69 | A | 27-150 | [»] | |
| 4J62 | X-ray | 2.04 | A | 27-150 | [»] | |
| 4J63 | X-ray | 2.04 | A | 27-150 | [»] | |
| 4J64 | X-ray | 1.78 | A | 27-150 | [»] | |
| 4J65 | X-ray | 1.96 | A | 27-150 | [»] | |
| 4J66 | X-ray | 2.04 | A | 27-150 | [»] | |
| 4J67 | X-ray | 1.86 | A | 27-150 | [»] | |
| 4J68 | X-ray | 1.78 | A | 27-150 | [»] | |
| 4J69 | X-ray | 1.89 | A | 27-150 | [»] | |
| 4J6A | X-ray | 2.04 | A | 27-150 | [»] | |
| 4K7L | X-ray | 1.38 | A | 27-41 | [»] | |
| B | 47-150 | [»] | ||||
| 4K7M | X-ray | 1.80 | A | 27-150 | [»] | |
| 4L55 | X-ray | 1.65 | A/B | 27-150 | [»] | |
| 4MXF | X-ray | 2.25 | A/B | 27-150 | [»] | |
| 4O36 | X-ray | 1.22 | A | 27-41 | [»] | |
| B | 47-150 | [»] | ||||
| 4O37 | X-ray | 1.40 | A | 27-41 | [»] | |
| B | 47-150 | [»] | ||||
| 4OKF | X-ray | 1.54 | A | 27-41 | [»] | |
| B | 47-150 | [»] | ||||
| 4OOH | X-ray | 1.89 | A | 27-150 | [»] | |
| 4OT4 | X-ray | 1.85 | A/B | 27-150 | [»] | |
| 4PEQ | X-ray | 2.21 | A/C | 27-150 | [»] | |
| 4POU | X-ray | 1.75 | A | 27-150 | [»] | |
| 4QH3 | X-ray | 2.00 | A/B | 27-150 | [»] | |
| 4RAT | X-ray | 1.50 | A | 27-150 | [»] | |
| 4RSD | X-ray | 1.60 | A | 27-150 | [»] | |
| 4RSK | X-ray | 2.10 | A | 27-150 | [»] | |
| 4RTE | X-ray | 1.95 | A | 27-150 | [»] | |
| 4S0Q | X-ray | 2.09 | A/B | 27-150 | [»] | |
| 4S18 | X-ray | 2.27 | A/B | 27-150 | [»] | |
| 4SRN | X-ray | 2.00 | A | 27-139 | [»] | |
| B | 140-150 | [»] | ||||
| 4WYN | X-ray | 1.80 | A/B | 27-150 | [»] | |
| 4WYP | X-ray | 1.50 | A/B | 27-150 | [»] | |
| 4WYZ | X-ray | 1.45 | A/B | 27-150 | [»] | |
| 4YGW | X-ray | 2.18 | B | 48-150 | [»] | |
| b | 27-41 | [»] | ||||
| 4ZZ4 | neutron diffraction | 1.80 | A | 27-150 | [»] | |
| 5D6U | X-ray | 1.52 | A | 27-150 | [»] | |
| 5D97 | neutron diffraction | 1.80 | A | 27-150 | [»] | |
| 5E5E | X-ray | 1.98 | A/B | 27-150 | [»] | |
| 5E5F | X-ray | 1.68 | A/B | 27-150 | [»] | |
| 5ET4 | X-ray | 2.10 | A/B/C/D | 27-150 | [»] | |
| 5JLG | X-ray | 1.79 | A/B | 27-150 | [»] | |
| 5JMG | X-ray | 1.85 | A/B | 27-150 | [»] | |
| 5JML | X-ray | 2.29 | A/B | 27-150 | [»] | |
| 5NA9 | X-ray | 2.07 | A | 27-150 | [»] | |
| 5NJ7 | X-ray | 2.15 | A/B | 27-150 | [»] | |
| 5OBC | X-ray | 2.07 | A/B | 27-150 | [»] | |
| 5OBD | X-ray | 1.98 | A/B | 27-150 | [»] | |
| 5OBE | X-ray | 1.82 | A/B | 27-150 | [»] | |
| 5RAT | X-ray | 1.50 | A | 27-150 | [»] | |
| 5RSA | X-ray | 2.00 | A | 27-150 | [»] | |
| 6ETK | X-ray | 0.85 | A | 27-150 | [»] | |
| 6ETL | X-ray | 0.85 | A | 27-150 | [»] | |
| 6ETM | X-ray | 0.92 | A | 27-150 | [»] | |
| 6ETN | X-ray | 0.92 | A | 27-150 | [»] | |
| 6ETO | X-ray | 1.02 | A | 27-150 | [»] | |
| 6ETP | X-ray | 1.02 | A | 27-150 | [»] | |
| 6ETQ | X-ray | 1.08 | A | 27-150 | [»] | |
| 6ETR | X-ray | 1.17 | A | 27-150 | [»] | |
| 6F60 | X-ray | 1.14 | A/B | 27-150 | [»] | |
| 6RAT | X-ray | 1.50 | A | 27-150 | [»] | |
| 6RSA | X-ray | 2.00 | A | 27-150 | [»] | |
| 7RAT | X-ray | 1.50 | A | 27-150 | [»] | |
| 7RSA | X-ray | 1.26 | A | 27-150 | [»] | |
| 8RAT | X-ray | 1.50 | A | 27-150 | [»] | |
| 8RSA | X-ray | 1.80 | A/B | 27-150 | [»] | |
| 9RAT | X-ray | 1.50 | A | 27-150 | [»] | |
| 9RSA | X-ray | 1.80 | A/B | 27-150 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P61823 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P61823 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
Database of interacting proteins More...DIPi | DIP-36384N |
Protein interaction database and analysis system More...IntActi | P61823, 8 interactors |
Molecular INTeraction database More...MINTi | P61823 |
STRING: functional protein association networks More...STRINGi | 9913.ENSBTAP00000011586 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P61823 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL6091 |
PTM databases
CarbonylDB database of protein carbonylation sites More...CarbonylDBi | P61823 |
GlyConnect protein glycosylation platform More...GlyConnecti | 529 |
UniCarbKB; an annotated and curated database of glycan structures More...UniCarbKBi | P61823 |
Proteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P61823 |
PeptideAtlas More...PeptideAtlasi | P61823 |
PRoteomics IDEntifications database More...PRIDEi | P61823 |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENSBTAT00000011586; ENSBTAP00000011586; ENSBTAG00000008793 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 282340 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | bta:282340 |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 6035 |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IYEN Eukaryota ENOG41113F1 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00900000140967 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000276883 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG008396 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P61823 |
KEGG Orthology (KO) More...KOi | K01168 |
Identification of Orthologs from Complete Genome Data More...OMAi | ACKNGQT |
Database of Orthologous Groups More...OrthoDBi | EOG091G15X3 |
TreeFam database of animal gene trees More...TreeFami | TF333393 |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.1.27.5 908 |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P61823 |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P61823 |
CutDB - Proteolytic event database More...PMAP-CutDBi | P61823 |
Protein Ontology More...PROi | PR:P61823 |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSBTAG00000008793 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.10.130.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001427 RNaseA IPR036816 RNaseA-like_dom_sf IPR023411 RNaseA_AS IPR023412 RNaseA_domain |
The PANTHER Classification System More...PANTHERi | PTHR11437 PTHR11437, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00074 RnaseA, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00794 RIBONUCLEASE |
ProDom; a protein domain database More...ProDomi | View protein in ProDom or Entries sharing at least one domain PD000535 RNaseA, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00092 RNAse_Pc, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF54076 SSF54076, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00127 RNASE_PANCREATIC, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | RNAS1_BOVIN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P61823Primary (citable) accession number: P61823 Secondary accession number(s): A6QPW8, P00656, Q9TSF2 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
| Last sequence update: | June 7, 2004 | |
| Last modified: | July 18, 2018 | |
| This is version 140 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
