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UniProtKB - P07998 (RNAS1_HUMAN)

Protein

Ribonuclease pancreatic

Gene

RNASE1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

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>

<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

Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA.1 Publication

<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. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates. EC:3.1.27.5

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei35SubstrateBy similarity1
Binding sitei38SubstrateBy similarity1
<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 sitei40Proton acceptor1
Binding sitei94SubstrateBy similarity1
Binding sitei113SubstrateBy similarity1
Active sitei147Proton donor1

<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

  • nucleic acid binding Source: InterPro
  • ribonuclease A activity Source: ProtInc
  • ribonuclease activity Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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 functionEndonuclease, Hydrolase, Nuclease

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.1.27.5 2681

<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
Recommended name:
Ribonuclease pancreatic (EC:3.1.27.5)
Alternative name(s):
HP-RNase
RIB-1
RNase UpI-1
Ribonuclease 1
Short name:
RNase 1
Ribonuclease A
Short name:
RNase A
<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:RIB1, 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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 14

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000129538.13

Human Gene Nomenclature Database

More...HGNCi		HGNC:10044 RNASE1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		180440 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P07998

<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 Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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 keyPosition(s)DescriptionActionsGraphical viewLength
<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>Mutagenesisi67R → D: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-95, A-116, D-117 and D-119. 1 Publication1
Mutagenesisi95N → D: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, A-116, D-117 and D-119. 1 Publication1
Mutagenesisi116 – 117NG → RS: No effect on inhibition by RNH1. 1 Publication2
Mutagenesisi116N → A: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, D-95, D-117 and D-119. 1 Publication1
Mutagenesisi117G → D: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, D-95, A-116 and D-119. 1 Publication1
Mutagenesisi119R → D: Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, D-95, A-116 and D-117. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		6035

Open Targets

More...OpenTargetsi		ENSG00000129538

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA34412

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL5425

Drug and drug target database

More...DrugBanki		DB03765 2'-cytidylic acid
DB03448 2'-Deoxyuridine 3'-Monophosphate
DB02363 2'-Monophosphoadenosine-5'-Diphosphate
DB03900 2-Methyl-2-Propanol
DB01842 3'-Phosphate-Adenosine-5'-Diphosphate
DB02714 3'-Uridinemonophosphate
DB08596 5'-deoxy-5'-piperidin-1-ylthymidine
DB02098 Adenosine-2'-5'-Diphosphate
DB01812 Adenosine-3'-5'-Diphosphate
DB04272 Citric Acid
DB02987 Cysteine-S-Acetamide
DB01961 Cytidine-3'-Monophosphate
DB01942 Formic Acid
DB00536 Guanidine
DB02325 Isopropyl Alcohol
DB00128 L-Aspartic Acid
DB04464 N-Formylmethionine
DB04514 Phosphoric Acid-2'-[2'-Deoxy-Uridine]Ester-5'-Guanosine Ester
DB03726 Purine Riboside-5'-Monophosphate
DB03186 U-Pi-a-Pi
DB02805 Uracil arabinose-3'-phosphate
DB03447 Uridylyl-2'-5'-Phospho-Adenosine

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		RNASE1

Domain mapping of disease mutations (DMDM)

More...DMDMi		1350818

<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 keyPosition(s)DescriptionActionsGraphical viewLength
<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 peptidei1 – 286 PublicationsAdd BLAST28
<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_000003092129 – 156Ribonuclease pancreaticAdd BLAST128

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bondi54 ↔ 112
<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>Glycosylationi62N-linked (GlcNAc...) asparagine; partial1 Publication1
Disulfide bondi68 ↔ 123
Disulfide bondi86 ↔ 138
Disulfide bondi93 ↔ 100
Glycosylationi104N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi116N-linked (GlcNAc...) asparagine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N-linked glycans are of complex type.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P07998

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P07998

PeptideAtlas

More...PeptideAtlasi		P07998

PRoteomics IDEntifications database

More...PRIDEi		P07998

ProteomicsDB human proteome resource

More...ProteomicsDBi		52059

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P07998

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P07998

<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

Pancreas and other tissues and body fluids (indicating it may have other physiological functions besides its role in digestion).

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000129538 Expressed in 226 organ(s), highest expression level in right testis

CleanEx database of gene expression profiles

More...CleanExi		HS_RNASE1

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P07998 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P07998 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA001140

<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

Monomer. Interacts with and forms tight 1:1 complexes with RNH1. Dimerization of two such complexes may occur. Interaction with RNH1 inhibits this protein.1 Publication

<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

WithEntry#Exp.IntActNotes
RNH1P134896EBI-2823523,EBI-1237106

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		111964, 5 interactors

Protein interaction database and analysis system

More...IntActi		P07998, 7 interactors

Molecular INTeraction database

More...MINTi		P07998

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000344193

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P07998

<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

1156
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DZAX-ray1.65A/B28-156[»]
1E21X-ray1.90A29-156[»]
1H8XX-ray2.00A/B29-156[»]
1Z7XX-ray1.95X/Z29-156[»]
2E0JX-ray1.60A/B29-156[»]
2E0LX-ray1.60A/B29-156[»]
2E0MX-ray1.70A/B29-156[»]
2E0OX-ray2.00A/B29-156[»]
2K11NMR-A29-155[»]
2Q4GX-ray1.95X/Z29-156[»]
3F8GX-ray2.60A/B29-153[»]
4KXHX-ray2.70A/B/C/D29-156[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P07998

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P07998

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		P07998

<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 keyPosition(s)DescriptionActionsGraphical viewLength
<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>Regioni69 – 73Substrate bindingBy similarity5

<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

Belongs to the pancreatic ribonuclease family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG410IYEN Eukaryota
ENOG41113F1 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000160869

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG008396

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P07998

KEGG Orthology (KO)

More...KOi		K01168

Identification of Orthologs from Complete Genome Data

More...OMAi		SNSTYCN

Database of Orthologous Groups

More...OrthoDBi		1549558at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P07998

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>Sequence (1+)i

<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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P07998-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MALEKSLVRL LLLVLILLVL GWVQPSLGKE SRAKKFQRQH MDSDSSPSSS 
        60         70         80         90        100
STYCNQMMRR RNMTQGRCKP VNTFVHEPLV DVQNVCFQEK VTCKNGQGNC 
       110        120        130        140        150
YKSNSSMHIT DCRLTNGSRY PNCAYRTSPK ERHIIVACEG SPYVPVHFDA 

SVEDST
Length:156
Mass (Da):17,644
Last modified:February 1, 1996 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF63B17B8B55115F9
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V357G3V357_HUMAN
Ribonuclease pancreatic
RNASE1
116Annotation score:

Annotation score:1 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti2A → G in CAA55817 (PubMed:8588814).Curated1
Sequence conflicti4Missing in AAB35096 (PubMed:7649283).Curated1
Sequence conflicti9 – 11RLL → VLP in AAB35096 (PubMed:7649283).Curated3
Sequence conflicti16 – 22ILLVLGW → VLLLVR in AAB35096 (PubMed:7649283).Curated7
Sequence conflicti67R → L in CAG29314 (Ref. 4) Curated1
Sequence conflicti151S → T in CAA55817 (PubMed:8588814).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
D26129 mRNA Translation: BAA05124.1
DQ494867 Genomic DNA Translation: ABF00144.1
AK312100 mRNA Translation: BAG35036.1
CR450318 mRNA Translation: CAG29314.1
CH471078 Genomic DNA Translation: EAW66437.1
CH471078 Genomic DNA Translation: EAW66438.1
BC005324 mRNA Translation: AAH05324.1
BC022882 mRNA Translation: AAH22882.1
X79235 Genomic DNA Translation: CAA55817.1
S79281 mRNA Translation: AAB35096.1
X62946 Genomic DNA Translation: CAA44718.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS9559.1

Protein sequence database of the Protein Information Resource

More...PIRi		I53530
S45003 NRHU1

NCBI Reference Sequences

More...RefSeqi		NP_002924.1, NM_002933.4
NP_937875.1, NM_198232.2
NP_937877.1, NM_198234.2
NP_937878.1, NM_198235.2

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.78224

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000340900; ENSP00000344193; ENSG00000129538
ENST00000397967; ENSP00000381057; ENSG00000129538
ENST00000397970; ENSP00000381060; ENSG00000129538
ENST00000412779; ENSP00000399493; ENSG00000129538

Database of genes from NCBI RefSeq genomes

More...GeneIDi		6035

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:6035

<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

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26129 mRNA Translation: BAA05124.1
DQ494867 Genomic DNA Translation: ABF00144.1
AK312100 mRNA Translation: BAG35036.1
CR450318 mRNA Translation: CAG29314.1
CH471078 Genomic DNA Translation: EAW66437.1
CH471078 Genomic DNA Translation: EAW66438.1
BC005324 mRNA Translation: AAH05324.1
BC022882 mRNA Translation: AAH22882.1
X79235 Genomic DNA Translation: CAA55817.1
S79281 mRNA Translation: AAB35096.1
X62946 Genomic DNA Translation: CAA44718.1
CCDSiCCDS9559.1
PIRiI53530
S45003 NRHU1
RefSeqiNP_002924.1, NM_002933.4
NP_937875.1, NM_198232.2
NP_937877.1, NM_198234.2
NP_937878.1, NM_198235.2
UniGeneiHs.78224

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DZAX-ray1.65A/B28-156[»]
1E21X-ray1.90A29-156[»]
1H8XX-ray2.00A/B29-156[»]
1Z7XX-ray1.95X/Z29-156[»]
2E0JX-ray1.60A/B29-156[»]
2E0LX-ray1.60A/B29-156[»]
2E0MX-ray1.70A/B29-156[»]
2E0OX-ray2.00A/B29-156[»]
2K11NMR-A29-155[»]
2Q4GX-ray1.95X/Z29-156[»]
3F8GX-ray2.60A/B29-153[»]
4KXHX-ray2.70A/B/C/D29-156[»]
ProteinModelPortaliP07998
SMRiP07998
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111964, 5 interactors
IntActiP07998, 7 interactors
MINTiP07998
STRINGi9606.ENSP00000344193

Chemistry databases

BindingDBiP07998
ChEMBLiCHEMBL5425
DrugBankiDB03765 2'-cytidylic acid
DB03448 2'-Deoxyuridine 3'-Monophosphate
DB02363 2'-Monophosphoadenosine-5'-Diphosphate
DB03900 2-Methyl-2-Propanol
DB01842 3'-Phosphate-Adenosine-5'-Diphosphate
DB02714 3'-Uridinemonophosphate
DB08596 5'-deoxy-5'-piperidin-1-ylthymidine
DB02098 Adenosine-2'-5'-Diphosphate
DB01812 Adenosine-3'-5'-Diphosphate
DB04272 Citric Acid
DB02987 Cysteine-S-Acetamide
DB01961 Cytidine-3'-Monophosphate
DB01942 Formic Acid
DB00536 Guanidine
DB02325 Isopropyl Alcohol
DB00128 L-Aspartic Acid
DB04464 N-Formylmethionine
DB04514 Phosphoric Acid-2'-[2'-Deoxy-Uridine]Ester-5'-Guanosine Ester
DB03726 Purine Riboside-5'-Monophosphate
DB03186 U-Pi-a-Pi
DB02805 Uracil arabinose-3'-phosphate
DB03447 Uridylyl-2'-5'-Phospho-Adenosine

PTM databases

iPTMnetiP07998
PhosphoSitePlusiP07998

Polymorphism and mutation databases

BioMutaiRNASE1
DMDMi1350818

Proteomic databases

jPOSTiP07998
PaxDbiP07998
PeptideAtlasiP07998
PRIDEiP07998
ProteomicsDBi52059

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000340900; ENSP00000344193; ENSG00000129538
ENST00000397967; ENSP00000381057; ENSG00000129538
ENST00000397970; ENSP00000381060; ENSG00000129538
ENST00000412779; ENSP00000399493; ENSG00000129538
GeneIDi6035
KEGGihsa:6035

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		6035
DisGeNETi6035
EuPathDBiHostDB:ENSG00000129538.13

GeneCards: human genes, protein and diseases

More...GeneCardsi		RNASE1
HGNCiHGNC:10044 RNASE1
HPAiHPA001140
MIMi180440 gene
neXtProtiNX_P07998
OpenTargetsiENSG00000129538
PharmGKBiPA34412

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG410IYEN Eukaryota
ENOG41113F1 LUCA
GeneTreeiENSGT00940000160869
HOVERGENiHBG008396
InParanoidiP07998
KOiK01168
OMAiSNSTYCN
OrthoDBi1549558at2759
PhylomeDBiP07998
TreeFamiTF333393

Enzyme and pathway databases

BRENDAi3.1.27.5 2681

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		RNASE1 human
EvolutionaryTraceiP07998

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		RNASE1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		6035

Protein Ontology

More...PROi		PR:P07998

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000129538 Expressed in 226 organ(s), highest expression level in right testis
CleanExiHS_RNASE1
ExpressionAtlasiP07998 baseline and differential
GenevisibleiP07998 HS

Family and domain databases

Gene3Di3.10.130.10, 1 hit
InterProiView protein in InterPro
IPR001427 RNaseA
IPR036816 RNaseA-like_dom_sf
IPR023411 RNaseA_AS
IPR023412 RNaseA_domain
PANTHERiPTHR11437 PTHR11437, 1 hit
PfamiView protein in Pfam
PF00074 RnaseA, 1 hit
PRINTSiPR00794 RIBONUCLEASE
ProDomiView protein in ProDom or Entries sharing at least one domain
PD000535 RNaseA, 1 hit
SMARTiView protein in SMART
SM00092 RNAse_Pc, 1 hit
SUPFAMiSSF54076 SSF54076, 1 hit
PROSITEiView 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 nameiRNAS1_HUMAN
<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>AccessioniPrimary (citable) accession number: P07998
Secondary accession number(s): B2R589
, D3DS06, Q16830, Q16869, Q1KHR2, Q6ICS5, Q9UCB4, Q9UCB5
<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 historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 1, 1996
Last modified: January 16, 2019
This is version 191 of the entry and version 4 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
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