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Protein

Deoxyribonuclease-1

Gene

DNASE1

Organism
Bos taurus (Bovine)
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

Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs (PubMed:4976790, PubMed:5166750, PubMed:3352748, PubMed:2395459). Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA (By similarity). Among other functions, seems to be involved in cell death by apoptosis (PubMed:2395459). Binds specifically to G-actin and blocks actin polymerization (PubMed:2395459). Together with DNASE1L3, plays a key role in degrading neutrophil extracellular traps (NETs) (By similarity). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (By similarity). Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation (By similarity).By similarity4 Publications

<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 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products.3 Publications EC:3.1.21.1

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+3 Publications, Mg2+3 PublicationsNote: Divalent metal cations. Prefers Ca2+ or Mg2+.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei35Involved in actin-binding1 Publication1
Sitei87Nitration by tetranitromethane destroys a Ca(2+) binding site and inactivates enzyme1
Sitei89Involved in actin-binding1 Publication1
<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 sitei1001 Publication1
Active sitei1562 Publications1

<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

  • actin binding Source: UniProtKB-KW
  • deoxyribonuclease activity Source: GO_Central
  • deoxyribonuclease I activity Source: GO_Central
  • DNA binding Source: GO_Central

GO - Biological processi

<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 functionActin-binding, Endonuclease, Hydrolase, Nuclease
Biological processApoptosis
LigandCalcium

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.21.1 908

<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:
Deoxyribonuclease-1 (EC:3.1.21.13 Publications)
Alternative name(s):
Deoxyribonuclease I
Short name:
DNase I
<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:DNASE1
Synonyms:DNL1
<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>OrganismiBos 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 identifieri9913 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
<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
  • UP000009136 <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 25

Organism-specific databases

Vertebrate Gene Nomenclature Database

More...
VGNCi
VGNC:28132 DNASE1

<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

Nucleus, 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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5712

<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 – 221 PublicationAdd BLAST22
<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_000000727523 – 282Deoxyribonuclease-1Add BLAST260

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi40N-linked (GlcNAc...) asparagine2 Publications1
<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 bondi123 ↔ 1261 Publication
Disulfide bondi195 ↔ 231Essential for enzymatic activity1 Publication

<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

The only differences between the A and B forms and the C and D forms are in the compositions of the carbohydrate bound to Asn-40.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

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

More...
PaxDbi
P00639

PRoteomics IDEntifications database

More...
PRIDEi
P00639

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSBTAG00000020107 Expressed in 9 organ(s), highest expression level in adult mammalian kidney

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P00639 baseline and differential

<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%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
ACTA1P681353EBI-8545986,EBI-367540From Oryctolagus cuniculus.

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-541N

Protein interaction database and analysis system

More...
IntActi
P00639, 2 interactors

Molecular INTeraction database

More...
MINTi
P00639

STRING: functional protein association networks

More...
STRINGi
9913.ENSBTAP00000054758

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P00639

<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

1282
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
1ATNX-ray2.80D23-282[»]
1DNKX-ray2.30A23-282[»]
2A3ZX-ray2.08B23-282[»]
2A40X-ray1.80B/E23-282[»]
2A41X-ray2.60B23-282[»]
2A42X-ray1.85B23-282[»]
2D1KX-ray2.50B23-282[»]
2DNJX-ray2.00A23-282[»]
3CJCX-ray3.90D23-282[»]
3DNIX-ray2.00A23-282[»]
3W3DX-ray1.80B23-282[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P00639

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

More...
SMRi
P00639

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
P00639

<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

<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 DNase I family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IFZB Eukaryota
ENOG410Z4MV LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000153734

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000059570

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG051368

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P00639

KEGG Orthology (KO)

More...
KOi
K11994

Database of Orthologous Groups

More...
OrthoDBi
1282784at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.60.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR018057 Deoxyribonuclease-1_AS
IPR016202 DNase_I
IPR033125 DNASE_I_2
IPR036691 Endo/exonu/phosph_ase_sf
IPR005135 Endo/exonuclease/phosphatase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03372 Exo_endo_phos, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000988 DNase_I_euk, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00130 DNASEI

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00476 DNaseIc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56219 SSF56219, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00919 DNASE_I_1, 1 hit
PS00918 DNASE_I_2, 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

P00639-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRGTRLMGLL LALAGLLQLG LSLKIAAFNI RTFGETKMSN ATLASYIVRI
60 70 80 90 100
VRRYDIVLIQ EVRDSHLVAV GKLLDYLNQD DPNTYHYVVS EPLGRNSYKE
110 120 130 140 150
RYLFLFRPNK VSVLDTYQYD DGCESCGNDS FSREPAVVKF SSHSTKVKEF
160 170 180 190 200
AIVALHSAPS DAVAEINSLY DVYLDVQQKW HLNDVMLMGD FNADCSYVTS
210 220 230 240 250
SQWSSIRLRT SSTFQWLIPD SADTTATSTN CAYDRIVVAG SLLQSSVVPG
260 270 280
SAAPFDFQAA YGLSNEMALA ISDHYPVEVT LT
Length:282
Mass (Da):31,346
Last modified:December 15, 1998 - v3
<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:i43904EF0D5F2E0E2
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
G3MYW9G3MYW9_BOVIN
Deoxyribonuclease
DNASE1
316Annotation score:

Annotation score:2 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 conflicti217L → V in AAM93248 (PubMed:14680812).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti143H → P in allele C/D. 2 Publications1

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
AJ001538 mRNA Translation: CAA04819.1
AF528509 Genomic DNA Translation: AAM93248.1
BC142349 mRNA Translation: AAI42350.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JC6532 NDBOA

NCBI Reference Sequences

More...
RefSeqi
NP_776959.1, NM_174534.2
XP_010817356.1, XM_010819054.2
XP_015315660.1, XM_015460174.1
XP_015315661.1, XM_015460175.1
XP_015315662.1, XM_015460176.1
XP_015315663.1, XM_015460177.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Bt.12952

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSBTAT00000026784; ENSBTAP00000026784; ENSBTAG00000020107

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
282217

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bta:282217

Keywords - Coding sequence diversityi

Polymorphism

<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

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001538 mRNA Translation: CAA04819.1
AF528509 Genomic DNA Translation: AAM93248.1
BC142349 mRNA Translation: AAI42350.1
PIRiJC6532 NDBOA
RefSeqiNP_776959.1, NM_174534.2
XP_010817356.1, XM_010819054.2
XP_015315660.1, XM_015460174.1
XP_015315661.1, XM_015460175.1
XP_015315662.1, XM_015460176.1
XP_015315663.1, XM_015460177.1
UniGeneiBt.12952

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ATNX-ray2.80D23-282[»]
1DNKX-ray2.30A23-282[»]
2A3ZX-ray2.08B23-282[»]
2A40X-ray1.80B/E23-282[»]
2A41X-ray2.60B23-282[»]
2A42X-ray1.85B23-282[»]
2D1KX-ray2.50B23-282[»]
2DNJX-ray2.00A23-282[»]
3CJCX-ray3.90D23-282[»]
3DNIX-ray2.00A23-282[»]
3W3DX-ray1.80B23-282[»]
ProteinModelPortaliP00639
SMRiP00639
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-541N
IntActiP00639, 2 interactors
MINTiP00639
STRINGi9913.ENSBTAP00000054758

Chemistry databases

BindingDBiP00639
ChEMBLiCHEMBL5712

Proteomic databases

PaxDbiP00639
PRIDEiP00639

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000026784; ENSBTAP00000026784; ENSBTAG00000020107
GeneIDi282217
KEGGibta:282217

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1773
VGNCiVGNC:28132 DNASE1

Phylogenomic databases

eggNOGiENOG410IFZB Eukaryota
ENOG410Z4MV LUCA
GeneTreeiENSGT00940000153734
HOGENOMiHOG000059570
HOVERGENiHBG051368
InParanoidiP00639
KOiK11994
OrthoDBi1282784at2759

Enzyme and pathway databases

BRENDAi3.1.21.1 908

Miscellaneous databases

EvolutionaryTraceiP00639

Protein Ontology

More...
PROi
PR:P00639

Gene expression databases

BgeeiENSBTAG00000020107 Expressed in 9 organ(s), highest expression level in adult mammalian kidney
ExpressionAtlasiP00639 baseline and differential

Family and domain databases

Gene3Di3.60.10.10, 1 hit
InterProiView protein in InterPro
IPR018057 Deoxyribonuclease-1_AS
IPR016202 DNase_I
IPR033125 DNASE_I_2
IPR036691 Endo/exonu/phosph_ase_sf
IPR005135 Endo/exonuclease/phosphatase
PfamiView protein in Pfam
PF03372 Exo_endo_phos, 1 hit
PIRSFiPIRSF000988 DNase_I_euk, 1 hit
PRINTSiPR00130 DNASEI
SMARTiView protein in SMART
SM00476 DNaseIc, 1 hit
SUPFAMiSSF56219 SSF56219, 1 hit
PROSITEiView protein in PROSITE
PS00919 DNASE_I_1, 1 hit
PS00918 DNASE_I_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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<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 nameiDNAS1_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>AccessioniPrimary (citable) accession number: P00639
Secondary accession number(s): A5PK44, Q8MJ27
<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: July 21, 1986
Last sequence update: December 15, 1998
Last modified: January 16, 2019
This is version 172 of the entry and version 3 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

<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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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