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Protein

Werner syndrome ATP-dependent helicase

Gene

WRN

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

Multifunctional enzyme that has both magnesium and ATP-dependent DNA-helicase activity and 3'->5' exonuclease activity towards double-stranded DNA with a 5'-overhang. Has no nuclease activity towards single-stranded DNA or blunt-ended double-stranded DNA. Binds preferentially to DNA substrates containing alternate secondary structures, such as replication forks and Holliday junctions. May play an important role in the dissociation of joint DNA molecules that can arise as products of homologous recombination, at stalled replication forks or during DNA repair. Alleviates stalling of DNA polymerases at the site of DNA lesions. Important for genomic integrity. Plays a role in the formation of DNA replication focal centers; stably associates with foci elements generating binding sites for RP-A (By similarity). Plays a role in double-strand break repair after gamma-irradiation.By similarity6 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

<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

Mg2+1 Publication, Mn2+1 Publication, Zn2+1 PublicationNote: Binds 2 magnesium ions per subunit. Has high activity with manganese and zinc ions (in vitro).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi82Magnesium 1; catalyticCombined sources1 Publication1
Metal bindingi82Magnesium 2; catalyticCombined sources1 Publication1
Metal bindingi84Magnesium 1; catalyticCombined sources1 Publication1
Metal bindingi216Magnesium 1; catalyticCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi571 – 578ATPPROSITE-ProRule annotation8

<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

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 functionDNA-binding, Exonuclease, Helicase, Hydrolase, Multifunctional enzyme, Nuclease
Biological processDNA damage, DNA repair
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
3.6.4.12 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-3108214 SUMOylation of DNA damage response and repair proteins
R-HSA-5685938 HDR through Single Strand Annealing (SSA)
R-HSA-5685942 HDR through Homologous Recombination (HRR)
R-HSA-5693554 Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA)
R-HSA-5693568 Resolution of D-loop Structures through Holliday Junction Intermediates
R-HSA-5693579 Homologous DNA Pairing and Strand Exchange
R-HSA-5693607 Processing of DNA double-strand break ends
R-HSA-5693616 Presynaptic phase of homologous DNA pairing and strand exchange
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-69473 G2/M DNA damage checkpoint

SIGNOR Signaling Network Open Resource

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SIGNORi
Q14191

<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:
Werner syndrome ATP-dependent helicase (EC:3.6.4.121 Publication)
Alternative name(s):
DNA helicase, RecQ-like type 3
Short name:
RecQ3
Exonuclease WRN (EC:3.1.-.-)
RecQ protein-like 2
<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:WRN
Synonyms:RECQ3, RECQL2
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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 8

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000165392.9

Human Gene Nomenclature Database

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HGNCi
HGNC:12791 WRN

Online Mendelian Inheritance in Man (OMIM)

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MIMi
604611 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q14191

<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

<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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Werner syndrome (WRN)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare autosomal recessive progeroid syndrome characterized by the premature onset of multiple age-related disorders, including atherosclerosis, cancer, non-insulin-dependent diabetes mellitus, ocular cataracts and osteoporosis. The major cause of death, at a median age of 47, is myocardial infarction.
See also OMIM:277700
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 variantiVAR_026588125K → N in WRN. 1 PublicationCorresponds to variant dbSNP:rs387906337EnsemblClinVar.1
Natural variantiVAR_026589135K → E in WRN. 1 PublicationCorresponds to variant dbSNP:rs267607008EnsemblClinVar.1
Colorectal cancer (CRC)2 Publications
The disease may be caused by mutations affecting the gene represented in this entry.
Disease descriptionA complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history.
See also OMIM:114500

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>Mutagenesisi84E → A: Abolishes exonuclease activity. 2 Publications1
Mutagenesisi88L → A: No effect on exonuclease activity. 1
Mutagenesisi145W → A: Reduces exonuclease activity. 1 Publication1
Mutagenesisi212Y → F: Strongly reduces exonuclease activity. 1 Publication1
Mutagenesisi987R → A: Reduces affinity for DNA about 8-fold. Loss of DNA binding; when associated with A-993. 1 Publication1
Mutagenesisi989S → A: Reduces affinity for DNA about 4-fold. 1 Publication1
Mutagenesisi993R → A: Reduces affinity for DNA about 20-fold. Loss of DNA binding; when associated with A-987. 1 Publication1
Mutagenesisi993R → E: Loss of DNA binding. 1 Publication1
Mutagenesisi1037F → A: Reduces affinity for DNA about 8-fold. 1 Publication1
Mutagenesisi1038M → A: Reduces affinity for DNA about 4-fold. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

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DisGeNETi
7486

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
WRN

MalaCards human disease database

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MalaCardsi
WRN
MIMi114500 phenotype
277700 phenotype

Open Targets

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OpenTargetsi
ENSG00000165392

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
902 Werner syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA367

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2146312

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
WRN

Domain mapping of disease mutations (DMDM)

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DMDMi
322510082

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<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_00002050452 – 1432Werner syndrome ATP-dependent helicaseAdd BLAST1431

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki154Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki241Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki252Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei426PhosphoserineCombined sources1
Modified residuei440PhosphoserineCombined sources1
Modified residuei453PhosphoserineCombined sources1
Modified residuei467PhosphoserineCombined sources1
Modified residuei478PhosphoserineCombined sources1
Modified residuei1133PhosphoserineCombined sources1
Modified residuei1400PhosphoserineCombined sources1

<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

Phosphorylated by PRKDC.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q14191

MaxQB - The MaxQuant DataBase

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MaxQBi
Q14191

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

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PaxDbi
Q14191

PeptideAtlas

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PeptideAtlasi
Q14191

PRoteomics IDEntifications database

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PRIDEi
Q14191

ProteomicsDB human proteome resource

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ProteomicsDBi
59913

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q14191

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

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PhosphoSitePlusi
Q14191

<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

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Bgeei
ENSG00000165392 Expressed in 199 organ(s), highest expression level in sperm

CleanEx database of gene expression profiles

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CleanExi
HS_WRN

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q14191 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA028661

<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, and homooligomer. May exist as homodimer, homotrimer, homotetramer and/or homohexamer. Homotetramer, or homohexamer, when bound to DNA. Interacts via its N-terminal domain with WRNIP1 (By similarity). Interacts with EXO1, PCNA and SUPV3L1. Interacts with PML (isoform PML-4).By similarity6 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>Sitei145Interaction with DNACurated1
Sitei1037Interaction with DNA1

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
113323, 57 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q14191

Database of interacting proteins

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DIPi
DIP-31380N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
Q14191

Protein interaction database and analysis system

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IntActi
Q14191, 29 interactors

Molecular INTeraction database

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MINTi
Q14191

STRING: functional protein association networks

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STRINGi
9606.ENSP00000298139

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q14191

<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

11432
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Database of protein disorder

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DisProti
DP00443

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q14191

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

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SMRi
Q14191

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q14191

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini60 – 2283'-5' exonucleaseAdd BLAST169
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati424 – 45011 PublicationAdd BLAST27
Repeati451 – 47721 PublicationAdd BLAST27
Domaini558 – 724Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST167
Domaini749 – 899Helicase C-terminalPROSITE-ProRule annotationAdd BLAST151
Domaini1150 – 1229HRDCPROSITE-ProRule annotationAdd BLAST80

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>Regioni2 – 277Interaction with WRNIP1By similarityAdd BLAST276
Regioni424 – 4772 X 27 AA tandem repeats of H-L-S-P-N-D-N-E-N-D-T-S-Y-V-I-E-S-D-E-D-L-E-M-E-M-L-KAdd BLAST54
Regioni987 – 993Interaction with DNA1 Publication7

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi668 – 671DEAH box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi507 – 510Poly-Glu4

<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 helicase family. RecQ subfamily.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0351 Eukaryota
KOG4373 Eukaryota
COG0514 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000159168

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000146447

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG000325

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q14191

KEGG Orthology (KO)

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KOi
K10900

Identification of Orthologs from Complete Genome Data

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OMAi
HRFMRDE

Database of Orthologous Groups

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OrthoDBi
EOG091G0B07

Database for complete collections of gene phylogenies

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PhylomeDBi
Q14191

TreeFam database of animal gene trees

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TreeFami
TF312852

Family and domain databases

Conserved Domains Database

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CDDi
cd00079 HELICc, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.10.10, 1 hit
3.30.420.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR002562 3'-5'_exonuclease_dom
IPR011545 DEAD/DEAH_box_helicase_dom
IPR004589 DNA_helicase_ATP-dep_RecQ
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR029491 Helicase_HTH
IPR010997 HRDC-like_sf
IPR002121 HRDC_dom
IPR027417 P-loop_NTPase
IPR032284 RecQ_Zn-bd
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
IPR018982 RQC_domain
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf

Pfam protein domain database

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Pfami
View protein in Pfam
PF00270 DEAD, 1 hit
PF01612 DNA_pol_A_exo1, 1 hit
PF00271 Helicase_C, 1 hit
PF00570 HRDC, 1 hit
PF14493 HTH_40, 1 hit
PF16124 RecQ_Zn_bind, 1 hit
PF09382 RQC, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00474 35EXOc, 1 hit
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit
SM00341 HRDC, 1 hit
SM00956 RQC, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF46785 SSF46785, 1 hit
SSF47819 SSF47819, 1 hit
SSF52540 SSF52540, 1 hit
SSF53098 SSF53098, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00614 recQ_fam, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit
PS50967 HRDC, 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.

Q14191-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSEKKLETTA QQRKCPEWMN VQNKRCAVEE RKACVRKSVF EDDLPFLEFT
60 70 80 90 100
GSIVYSYDAS DCSFLSEDIS MSLSDGDVVG FDMEWPPLYN RGKLGKVALI
110 120 130 140 150
QLCVSESKCY LFHVSSMSVF PQGLKMLLEN KAVKKAGVGI EGDQWKLLRD
160 170 180 190 200
FDIKLKNFVE LTDVANKKLK CTETWSLNSL VKHLLGKQLL KDKSIRCSNW
210 220 230 240 250
SKFPLTEDQK LYAATDAYAG FIIYRNLEIL DDTVQRFAIN KEEEILLSDM
260 270 280 290 300
NKQLTSISEE VMDLAKHLPH AFSKLENPRR VSILLKDISE NLYSLRRMII
310 320 330 340 350
GSTNIETELR PSNNLNLLSF EDSTTGGVQQ KQIREHEVLI HVEDETWDPT
360 370 380 390 400
LDHLAKHDGE DVLGNKVERK EDGFEDGVED NKLKENMERA CLMSLDITEH
410 420 430 440 450
ELQILEQQSQ EEYLSDIAYK STEHLSPNDN ENDTSYVIES DEDLEMEMLK
460 470 480 490 500
HLSPNDNEND TSYVIESDED LEMEMLKSLE NLNSGTVEPT HSKCLKMERN
510 520 530 540 550
LGLPTKEEEE DDENEANEGE EDDDKDFLWP APNEEQVTCL KMYFGHSSFK
560 570 580 590 600
PVQWKVIHSV LEERRDNVAV MATGYGKSLC FQYPPVYVGK IGLVISPLIS
610 620 630 640 650
LMEDQVLQLK MSNIPACFLG SAQSENVLTD IKLGKYRIVY VTPEYCSGNM
660 670 680 690 700
GLLQQLEADI GITLIAVDEA HCISEWGHDF RDSFRKLGSL KTALPMVPIV
710 720 730 740 750
ALTATASSSI REDIVRCLNL RNPQITCTGF DRPNLYLEVR RKTGNILQDL
760 770 780 790 800
QPFLVKTSSH WEFEGPTIIY CPSRKMTQQV TGELRKLNLS CGTYHAGMSF
810 820 830 840 850
STRKDIHHRF VRDEIQCVIA TIAFGMGINK ADIRQVIHYG APKDMESYYQ
860 870 880 890 900
EIGRAGRDGL QSSCHVLWAP ADINLNRHLL TEIRNEKFRL YKLKMMAKME
910 920 930 940 950
KYLHSSRCRR QIILSHFEDK QVQKASLGIM GTEKCCDNCR SRLDHCYSMD
960 970 980 990 1000
DSEDTSWDFG PQAFKLLSAV DILGEKFGIG LPILFLRGSN SQRLADQYRR
1010 1020 1030 1040 1050
HSLFGTGKDQ TESWWKAFSR QLITEGFLVE VSRYNKFMKI CALTKKGRNW
1060 1070 1080 1090 1100
LHKANTESQS LILQANEELC PKKLLLPSSK TVSSGTKEHC YNQVPVELST
1110 1120 1130 1140 1150
EKKSNLEKLY SYKPCDKISS GSNISKKSIM VQSPEKAYSS SQPVISAQEQ
1160 1170 1180 1190 1200
ETQIVLYGKL VEARQKHANK MDVPPAILAT NKILVDMAKM RPTTVENVKR
1210 1220 1230 1240 1250
IDGVSEGKAA MLAPLLEVIK HFCQTNSVQT DLFSSTKPQE EQKTSLVAKN
1260 1270 1280 1290 1300
KICTLSQSMA ITYSLFQEKK MPLKSIAESR ILPLMTIGMH LSQAVKAGCP
1310 1320 1330 1340 1350
LDLERAGLTP EVQKIIADVI RNPPVNSDMS KISLIRMLVP ENIDTYLIHM
1360 1370 1380 1390 1400
AIEILKHGPD SGLQPSCDVN KRRCFPGSEE ICSSSKRSKE EVGINTETSS
1410 1420 1430
AERKRRLPVW FAKGSDTSKK LMDKTKRGGL FS
Length:1,432
Mass (Da):162,461
Last modified:February 8, 2011 - v2
<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:i63F10D19E90AA461
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01745332K → R1 PublicationCorresponds to variant dbSNP:rs34477820EnsemblClinVar.1
Natural variantiVAR_03631892G → V in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_017454114V → I Polymorphism; no effect on exonuclease activity. 3 PublicationsCorresponds to variant dbSNP:rs2230009EnsemblClinVar.1
Natural variantiVAR_026588125K → N in WRN. 1 PublicationCorresponds to variant dbSNP:rs387906337EnsemblClinVar.1
Natural variantiVAR_026589135K → E in WRN. 1 PublicationCorresponds to variant dbSNP:rs267607008EnsemblClinVar.1
Natural variantiVAR_017455172T → P Polymorphism; no effect on exonuclease activity. 2 PublicationsCorresponds to variant dbSNP:rs367991517EnsemblClinVar.1
Natural variantiVAR_017456240N → K1 PublicationCorresponds to variant dbSNP:rs148229804EnsemblClinVar.1
Natural variantiVAR_006904324T → A1 PublicationCorresponds to variant dbSNP:rs1800390EnsemblClinVar.1
Natural variantiVAR_020450329Q → R. Corresponds to variant dbSNP:rs4987237Ensembl.1
Natural variantiVAR_018941343E → K1 PublicationCorresponds to variant dbSNP:rs11574222EnsemblClinVar.1
Natural variantiVAR_020451383L → F. Corresponds to variant dbSNP:rs4987238EnsemblClinVar.1
Natural variantiVAR_017457383L → W1 Publication1
Natural variantiVAR_006905387M → I4 PublicationsCorresponds to variant dbSNP:rs1800391EnsemblClinVar.1
Natural variantiVAR_018942533N → S1 PublicationCorresponds to variant dbSNP:rs11574240EnsemblClinVar.1
Natural variantiVAR_018943612S → C1 PublicationCorresponds to variant dbSNP:rs11574250EnsemblClinVar.1
Natural variantiVAR_018944708S → F1 PublicationCorresponds to variant dbSNP:rs11574289EnsemblClinVar.1
Natural variantiVAR_057124711R → W. Corresponds to variant dbSNP:rs34560788EnsemblClinVar.1
Natural variantiVAR_017458724Q → L1 Publication1
Natural variantiVAR_014913834R → C1 PublicationCorresponds to variant dbSNP:rs3087425EnsemblClinVar.1
Natural variantiVAR_018945912I → S1 PublicationCorresponds to variant dbSNP:rs11574323EnsemblClinVar.1
Natural variantiVAR_0079031074L → F5 PublicationsCorresponds to variant dbSNP:rs1801195EnsemblClinVar.1
Natural variantiVAR_0149141079S → L1 PublicationCorresponds to variant dbSNP:rs3087414EnsemblClinVar.1
Natural variantiVAR_0189461133S → A1 PublicationCorresponds to variant dbSNP:rs11574358Ensembl.1
Natural variantiVAR_0541621141S → L1 PublicationCorresponds to variant dbSNP:rs139323683EnsemblClinVar.1
Natural variantiVAR_0174591269K → E1 PublicationCorresponds to variant dbSNP:rs746648510Ensembl.1
Natural variantiVAR_0189471339V → I1 PublicationCorresponds to variant dbSNP:rs11574395EnsemblClinVar.1
Natural variantiVAR_0069061367C → R Polymorphism associated with a higher risk of myocardial infarction. 4 PublicationsCorresponds to variant dbSNP:rs1346044EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L76937 Genomic DNA Translation: AAC41981.1
AY818673 mRNA Translation: AAX21098.1
AF091214 mRNA Translation: AAC63361.1
AF181897, AF181896 Genomic DNA Translation: AAF06162.1
AY442327 Genomic DNA Translation: AAR05448.1
AC084736 Genomic DNA No translation available.

The Consensus CDS (CCDS) project

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CCDSi
CCDS6082.1

NCBI Reference Sequences

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RefSeqi
NP_000544.2, NM_000553.4

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.632050

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000298139; ENSP00000298139; ENSG00000165392

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
7486

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:7486

UCSC genome browser

More...
UCSCi
uc003xio.5 human

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

WRN

WRN mutation db (Warner disease)

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L76937 Genomic DNA Translation: AAC41981.1
AY818673 mRNA Translation: AAX21098.1
AF091214 mRNA Translation: AAC63361.1
AF181897, AF181896 Genomic DNA Translation: AAF06162.1
AY442327 Genomic DNA Translation: AAR05448.1
AC084736 Genomic DNA No translation available.
CCDSiCCDS6082.1
RefSeqiNP_000544.2, NM_000553.4
UniGeneiHs.632050

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AXLNMR-A949-1092[»]
2DGZNMR-A1140-1239[»]
2E1EX-ray2.30A1142-1242[»]
2E1FX-ray2.00A1142-1242[»]
2FBTX-ray2.05A38-236[»]
2FBVX-ray2.40A38-236[»]
2FBXX-ray2.20A38-236[»]
2FBYX-ray2.00A38-236[»]
2FC0X-ray2.00A38-236[»]
3AAFX-ray1.90A/B949-1079[»]
DisProtiDP00443
ProteinModelPortaliQ14191
SMRiQ14191
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113323, 57 interactors
CORUMiQ14191
DIPiDIP-31380N
ELMiQ14191
IntActiQ14191, 29 interactors
MINTiQ14191
STRINGi9606.ENSP00000298139

Chemistry databases

BindingDBiQ14191
ChEMBLiCHEMBL2146312

PTM databases

iPTMnetiQ14191
PhosphoSitePlusiQ14191

Polymorphism and mutation databases

BioMutaiWRN
DMDMi322510082

Proteomic databases

EPDiQ14191
MaxQBiQ14191
PaxDbiQ14191
PeptideAtlasiQ14191
PRIDEiQ14191
ProteomicsDBi59913

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000298139; ENSP00000298139; ENSG00000165392
GeneIDi7486
KEGGihsa:7486
UCSCiuc003xio.5 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7486
DisGeNETi7486
EuPathDBiHostDB:ENSG00000165392.9

GeneCards: human genes, protein and diseases

More...
GeneCardsi
WRN
GeneReviewsiWRN

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0007441
HGNCiHGNC:12791 WRN
HPAiHPA028661
MalaCardsiWRN
MIMi114500 phenotype
277700 phenotype
604611 gene
neXtProtiNX_Q14191
OpenTargetsiENSG00000165392
Orphaneti902 Werner syndrome
PharmGKBiPA367

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0351 Eukaryota
KOG4373 Eukaryota
COG0514 LUCA
GeneTreeiENSGT00940000159168
HOGENOMiHOG000146447
HOVERGENiHBG000325
InParanoidiQ14191
KOiK10900
OMAiHRFMRDE
OrthoDBiEOG091G0B07
PhylomeDBiQ14191
TreeFamiTF312852

Enzyme and pathway databases

BRENDAi3.6.4.12 2681
ReactomeiR-HSA-3108214 SUMOylation of DNA damage response and repair proteins
R-HSA-5685938 HDR through Single Strand Annealing (SSA)
R-HSA-5685942 HDR through Homologous Recombination (HRR)
R-HSA-5693554 Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA)
R-HSA-5693568 Resolution of D-loop Structures through Holliday Junction Intermediates
R-HSA-5693579 Homologous DNA Pairing and Strand Exchange
R-HSA-5693607 Processing of DNA double-strand break ends
R-HSA-5693616 Presynaptic phase of homologous DNA pairing and strand exchange
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-69473 G2/M DNA damage checkpoint
SIGNORiQ14191

Miscellaneous databases

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

More...
ChiTaRSi
WRN human
EvolutionaryTraceiQ14191

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Werner_syndrome_ATP-dependent_helicase

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

More...
GenomeRNAii
7486

Protein Ontology

More...
PROi
PR:Q14191

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000165392 Expressed in 199 organ(s), highest expression level in sperm
CleanExiHS_WRN
GenevisibleiQ14191 HS

Family and domain databases

CDDicd00079 HELICc, 1 hit
Gene3Di1.10.10.10, 1 hit
3.30.420.10, 1 hit
InterProiView protein in InterPro
IPR002562 3'-5'_exonuclease_dom
IPR011545 DEAD/DEAH_box_helicase_dom
IPR004589 DNA_helicase_ATP-dep_RecQ
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR029491 Helicase_HTH
IPR010997 HRDC-like_sf
IPR002121 HRDC_dom
IPR027417 P-loop_NTPase
IPR032284 RecQ_Zn-bd
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
IPR018982 RQC_domain
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF00270 DEAD, 1 hit
PF01612 DNA_pol_A_exo1, 1 hit
PF00271 Helicase_C, 1 hit
PF00570 HRDC, 1 hit
PF14493 HTH_40, 1 hit
PF16124 RecQ_Zn_bind, 1 hit
PF09382 RQC, 1 hit
SMARTiView protein in SMART
SM00474 35EXOc, 1 hit
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit
SM00341 HRDC, 1 hit
SM00956 RQC, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
SSF47819 SSF47819, 1 hit
SSF52540 SSF52540, 1 hit
SSF53098 SSF53098, 1 hit
TIGRFAMsiTIGR00614 recQ_fam, 1 hit
PROSITEiView protein in PROSITE
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit
PS50967 HRDC, 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 nameiWRN_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: Q14191
Secondary accession number(s): A1KYY9
<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: December 15, 1998
Last sequence update: February 8, 2011
Last modified: December 5, 2018
This is version 211 of the entry and version 2 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. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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