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O09053

- WRN_MOUSE

UniProt

O09053 - WRN_MOUSE

Protein

Werner syndrome ATP-dependent helicase homolog

Gene

Wrn

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    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 similarity.By similarity

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Cofactori

    Binds 2 magnesium ions per subunit. Has high activity with manganese and zinc ions (in vitro).

    Enzyme regulationi

    Zinc ions stimulate the exonuclease activity.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi76 – 761Magnesium 1; catalytic
    Metal bindingi76 – 761Magnesium 2; catalytic
    Metal bindingi78 – 781Magnesium 1; catalytic
    Sitei139 – 1391Interaction with DNABy similarity
    Metal bindingi210 – 2101Magnesium 1; catalytic
    Sitei1002 – 10021Interaction with DNABy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi535 – 5428ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. 3'-5' exonuclease activity Source: UniProtKB
    2. ATP binding Source: UniProtKB-KW
    3. ATP-dependent 3'-5' DNA helicase activity Source: InterPro
    4. bubble DNA binding Source: Ensembl
    5. four-way junction helicase activity Source: Ensembl
    6. G-quadruplex DNA binding Source: Ensembl
    7. magnesium ion binding Source: UniProtKB
    8. manganese ion binding Source: UniProtKB
    9. protein binding Source: UniProtKB
    10. Y-form DNA binding Source: Ensembl

    GO - Biological processi

    1. base-excision repair Source: Ensembl
    2. cellular response to gamma radiation Source: UniProtKB
    3. cellular response to starvation Source: MGI
    4. DNA metabolic process Source: UniProtKB
    5. DNA recombination Source: InterPro
    6. DNA replication Source: MGI
    7. DNA synthesis involved in DNA repair Source: Ensembl
    8. double-strand break repair Source: UniProtKB
    9. multicellular organismal aging Source: MGI
    10. nucleic acid phosphodiester bond hydrolysis Source: GOC
    11. nucleolus to nucleoplasm transport Source: MGI
    12. positive regulation of hydrolase activity Source: Ensembl
    13. regulation of apoptotic process Source: Ensembl
    14. regulation of growth rate Source: MGI
    15. replication fork processing Source: Ensembl
    16. replicative cell aging Source: MGI
    17. response to oxidative stress Source: Ensembl
    18. response to UV-C Source: Ensembl
    19. telomere maintenance Source: MGI

    Keywords - Molecular functioni

    Exonuclease, Helicase, Hydrolase, Nuclease

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    ATP-binding, DNA-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Werner syndrome ATP-dependent helicase homolog (EC:3.6.4.12)
    Alternative name(s):
    Exonuclease WRN (EC:3.1.-.-)
    Gene namesi
    Name:Wrn
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:109635. Wrn.

    Subcellular locationi

    Nucleus 1 Publication. Nucleusnucleolus By similarity. Nucleusnucleoplasm By similarity
    Note: Gamma-irradiation leads to its translocation from nucleoli to nucleoplasm and PML regulates the irradiation-induced WRN relocation.By similarity

    GO - Cellular componenti

    1. centrosome Source: Ensembl
    2. MutLalpha complex Source: Ensembl
    3. nucleolus Source: MGI
    4. nucleoplasm Source: MGI
    5. nucleus Source: MGI

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi185 – 1851K → A: Loss of exonuclease activity. 1 Publication
    Mutagenesisi190 – 1901R → A: Strongly reduced exonuclease activity. 1 Publication
    Mutagenesisi206 – 2061Y → F: Loss of exonuclease activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14011401Werner syndrome ATP-dependent helicase homologPRO_0000205046Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei419 – 4191PhosphoserineBy similarity
    Modified residuei433 – 4331PhosphoserineBy similarity
    Modified residuei1098 – 10981PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated by PRKDC.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiO09053.
    PRIDEiO09053.

    PTM databases

    PhosphoSiteiO09053.

    Expressioni

    Tissue specificityi

    Expressed ubiquitously in most organs at a low level, highly expressed in testis, ovary and spleen.2 Publications

    Gene expression databases

    ArrayExpressiO09053.
    BgeeiO09053.
    CleanExiMM_WRN.
    GenevestigatoriO09053.

    Interactioni

    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. Interacts with PCNA; EXO1 and SUPV3L1 By similarity. Interacts with PML By similarity.By similarity

    Protein-protein interaction databases

    DIPiDIP-27642N.

    Structurei

    Secondary structure

    1
    1401
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi45 – 506
    Helixi53 – 6614
    Beta strandi72 – 787
    Beta strandi93 – 975
    Beta strandi99 – 1068
    Helixi108 – 1103
    Helixi116 – 1227
    Beta strandi127 – 1337
    Helixi134 – 14512
    Beta strandi151 – 1544
    Helixi155 – 1628
    Helixi171 – 1799
    Helixi187 – 1904
    Beta strandi196 – 1983
    Helixi201 – 22222

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2E6LX-ray2.20A31-238[»]
    2E6MX-ray2.00A31-238[»]
    ProteinModelPortaliO09053.
    SMRiO09053. Positions 37-225, 488-1200.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO09053.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini51 – 2231733'-5' exonucleaseAdd
    BLAST
    Domaini522 – 688167Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini713 – 866154Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini1115 – 119480HRDCPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 271271Interaction with WRNIP1Add
    BLAST
    Regioni952 – 9587Interaction with DNABy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi632 – 6354DEAH box

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1387 – 13904Poly-Ser

    Sequence similaritiesi

    Belongs to the helicase family. RecQ subfamily.Curated
    Contains 1 3'-5' exonuclease domain.Curated
    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
    Contains 1 HRDC domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0514.
    GeneTreeiENSGT00550000074520.
    HOGENOMiHOG000146447.
    HOVERGENiHBG000325.
    InParanoidiQ80YP9.
    KOiK10900.
    OMAiGIEGDQW.
    OrthoDBiEOG7J70F2.
    TreeFamiTF312852.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    1.10.150.80. 1 hit.
    3.30.420.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR002562. 3'-5'_exonuclease_dom.
    IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR004589. DNA_helicase_ATP-dep_RecQ.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR029491. Helicase_HTH.
    IPR010997. HRDC-like.
    IPR002121. HRDC_dom.
    IPR027417. P-loop_NTPase.
    IPR012337. RNaseH-like_dom.
    IPR018982. RQC_domain.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF01612. DNA_pol_A_exo1. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF00570. HRDC. 1 hit.
    PF14493. HTH_40. 1 hit.
    PF09382. RQC. 1 hit.
    [Graphical view]
    SMARTiSM00474. 35EXOc. 1 hit.
    SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    SM00341. HRDC. 1 hit.
    SM00956. RQC. 1 hit.
    [Graphical view]
    SUPFAMiSSF47819. SSF47819. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF53098. SSF53098. 1 hit.
    TIGRFAMsiTIGR00614. recQ_fam. 1 hit.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS50967. HRDC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O09053-1 [UniParc]FASTAAdd to Basket

    « Hide

    METTSLQRKF PEWMSMQSQR CATEEKACVQ KSVLEDNLPF LEFPGSIVYS     50
    YEASDCSFLS EDISMRLSDG DVVGFDMEWP PIYKPGKRSR VAVIQLCVSE 100
    SKCYLFHISS MSVFPQGLKM LLENKSIKKA GVGIEGDQWK LLRDFDVKLE 150
    SFVELTDVAN EKLKCAETWS LNGLVKHVLG KQLLKDKSIR CSNWSNFPLT 200
    EDQKLYAATD AYAGLIIYQK LGNLGDTAQV FALNKAEENL PLEMKKQLNS 250
    ISEEMRDLAN RFPVTCRNLE TLQRVPVILK SISENLCSLR KVICGPTNTE 300
    TRLKPGSSFN LLSSEDSAAA GEKEKQIGKH STFAKIKEEP WDPELDSLVK 350
    QEEVDVFRNQ VKQEKGESEN EIEDNLLRED MERTCVIPSI SENELQDLEQ 400
    QAKEEKYNDV SHQLSEHLSP NDDENDSSYI IESDEDLEME MLKSLENLNS 450
    DVVEPTHSTW LEMGTNGRLP PEEEDGHGNE AIKEEQEEED HLLPEPNAKQ 500
    INCLKTYFGH SSFKPVQWKV IHSVLEERRD NVVVMATGYG KSLCFQYPPV 550
    YTGKIGIVIS PLISLMEDQV LQLELSNVPA CLLGSAQSKN ILGDVKLGKY 600
    RVIYITPEFC SGNLDLLQQL DSSIGITLIA VDEAHCISEW GHDFRSSFRM 650
    LGSLKTALPL VPVIALSATA SSSIREDIIS CLNLKDPQIT CTGFDRPNLY 700
    LEVGRKTGNI LQDLKPFLVR KASSAWEFEG PTIIYCPSRK MTEQVTAELG 750
    KLNLACRTYH AGMKISERKD VHHRFLRDEI QCVVATVAFG MGINKADIRK 800
    VIHYGAPKEM ESYYQEIGRA GRDGLQSSCH LLWAPADFNT SRNLLIEIHD 850
    EKFRLYKLKM MVKMEKYLHS SQCRRRIILS HFEDKCLQKA SLDIMGTEKC 900
    CDNCRPRLNH CLTANNSEDA SQDFGPQAFQ LLSAVDILQE KFGIGIPILF 950
    LRGSNSQRLP DKYRGHRLFG AGKEQAESWW KTLSHHLIAE GFLVEVPKEN 1000
    KYIKTCSLTK KGRKWLGEAS SQSPPSLLLQ ANEEMFPRKV LLPSSNPVSP 1050
    ETTQHSSNQN PAGLTTKQSN LERTHSYKVP EKVSSGTNIP KKSAVMPSPG 1100
    TSSSPLEPAI SAQELDARTG LYARLVEARQ KHANKMDVPP AILATNKVLL 1150
    DMAKMRPTTV ENMKQIDGVS EGKAALLAPL LEVIKHFCQV TSVQTDLLSS 1200
    AKPHKEQEKS QEMEKKDCSL PQSVAVTYTL FQEKKMPLHS IAENRLLPLT 1250
    AAGMHLAQAV KAGYPLDMER AGLTPETWKI IMDVIRNPPI NSDMYKVKLI 1300
    RMLVPENLDT YLIHMAIEIL QSGSDSRTQP PCDSSRKRRF PSSAESCESC 1350
    KESKEAVTET KASSSESKRK LPEWFAKGNV PSADTGSSSS MAKTKKKGLF 1400
    S 1401
    Length:1,401
    Mass (Da):157,204
    Last modified:July 27, 2011 - v3
    Checksum:i66DF2252B17C24C3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti101 – 1011S → N in BAA20269. (PubMed:9143515)Curated
    Sequence conflicti101 – 1011S → N in BAA20270. (PubMed:9143515)Curated
    Sequence conflicti101 – 1011S → N in AAC72359. 1 PublicationCurated
    Sequence conflicti101 – 1011S → N in AAF64490. (PubMed:10757812)Curated
    Sequence conflicti228 – 2281A → V in BAA20269. (PubMed:9143515)Curated
    Sequence conflicti228 – 2281A → V in BAA20270. (PubMed:9143515)Curated
    Sequence conflicti228 – 2281A → V in AAC72359. 1 PublicationCurated
    Sequence conflicti228 – 2281A → V in AAF64490. (PubMed:10757812)Curated
    Sequence conflicti250 – 2501S → L in BAA20269. (PubMed:9143515)Curated
    Sequence conflicti250 – 2501S → L in BAA20270. (PubMed:9143515)Curated
    Sequence conflicti250 – 2501S → L in AAC72359. 1 PublicationCurated
    Sequence conflicti250 – 2501S → L in AAF64490. (PubMed:10757812)Curated
    Sequence conflicti452 – 4521V → M in BAA20269. (PubMed:9143515)Curated
    Sequence conflicti452 – 4521V → M in BAA20270. (PubMed:9143515)Curated
    Sequence conflicti452 – 4521V → M in AAC72359. 1 PublicationCurated
    Sequence conflicti452 – 4521V → M in AAF64490. (PubMed:10757812)Curated
    Sequence conflicti459 – 4591T → K in BAA20269. (PubMed:9143515)Curated
    Sequence conflicti459 – 4591T → K in BAA20270. (PubMed:9143515)Curated
    Sequence conflicti459 – 4591T → K in AAC72359. 1 PublicationCurated
    Sequence conflicti459 – 4591T → K in AAF64490. (PubMed:10757812)Curated
    Sequence conflicti468 – 4681R → C in BAA20269. (PubMed:9143515)Curated
    Sequence conflicti468 – 4681R → C in BAA20270. (PubMed:9143515)Curated
    Sequence conflicti468 – 4681R → C in AAC72359. 1 PublicationCurated
    Sequence conflicti468 – 4681R → C in AAF64490. (PubMed:10757812)Curated
    Sequence conflicti619 – 6191Q → K in BAA20269. (PubMed:9143515)Curated
    Sequence conflicti619 – 6191Q → K in BAA20270. (PubMed:9143515)Curated
    Sequence conflicti619 – 6191Q → K in AAC72359. 1 PublicationCurated
    Sequence conflicti619 – 6191Q → K in AAF64490. (PubMed:10757812)Curated
    Sequence conflicti800 – 8001K → Q in BAA20270. (PubMed:9143515)Curated
    Sequence conflicti800 – 8001K → Q in BAA20269. (PubMed:9143515)Curated
    Sequence conflicti844 – 8441L → H in AAC72359. 1 PublicationCurated
    Sequence conflicti955 – 98834NSQRL…SHHLI → VSVSVIAPGTVSDSAFHCVA MALAFFRWLTSNPC in AAC72359. 1 PublicationCuratedAdd
    BLAST
    Sequence conflicti1021 – 10211S → L in BAA20269. (PubMed:9143515)Curated
    Sequence conflicti1021 – 10211S → L in BAA20270. (PubMed:9143515)Curated
    Sequence conflicti1021 – 10211S → L in AAF64490. (PubMed:10757812)Curated
    Sequence conflicti1145 – 11451T → A in BAA20270. (PubMed:9143515)Curated
    Sequence conflicti1145 – 11451T → A in BAA20269. (PubMed:9143515)Curated
    Sequence conflicti1181 – 11811L → V in BAA20270. (PubMed:9143515)Curated
    Sequence conflicti1181 – 11811L → V in BAA20269. (PubMed:9143515)Curated
    Sequence conflicti1182 – 11821E → G in BAA20269. (PubMed:9143515)Curated
    Sequence conflicti1182 – 11821E → G in BAA20270. (PubMed:9143515)Curated
    Sequence conflicti1182 – 11821E → G in AAF64490. (PubMed:10757812)Curated
    Sequence conflicti1252 – 12521A → V in BAA20269. (PubMed:9143515)Curated
    Sequence conflicti1252 – 12521A → V in BAA20270. (PubMed:9143515)Curated
    Sequence conflicti1252 – 12521A → V in AAF64490. (PubMed:10757812)Curated
    Sequence conflicti1308 – 13081L → I in BAA20269. (PubMed:9143515)Curated
    Sequence conflicti1308 – 13081L → I in BAA20270. (PubMed:9143515)Curated
    Sequence conflicti1308 – 13081L → I in AAF64490. (PubMed:10757812)Curated
    Sequence conflicti1356 – 13561A → V in BAA20269. (PubMed:9143515)Curated
    Sequence conflicti1356 – 13561A → V in BAA20270. (PubMed:9143515)Curated
    Sequence conflicti1356 – 13561A → V in AAF64490. (PubMed:10757812)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D86527 mRNA. Translation: BAA20270.1.
    D86526 mRNA. Translation: BAA20269.1.
    AF091215 mRNA. Translation: AAC78077.1.
    AF091216 Genomic DNA. Translation: AAC72359.1.
    AF241636 mRNA. Translation: AAF64490.1.
    AC153789 Genomic DNA. No translation available.
    AC115809 Genomic DNA. No translation available.
    BC050921 mRNA. Translation: AAH50921.1.
    BC060700 mRNA. Translation: AAH60700.1.
    CCDSiCCDS22229.1.
    PIRiT17452.
    T30247.
    RefSeqiNP_001116294.1. NM_001122822.1.
    NP_035851.3. NM_011721.4.
    XP_006509154.1. XM_006509091.1.
    XP_006509155.1. XM_006509092.1.
    UniGeneiMm.228805.

    Genome annotation databases

    EnsembliENSMUST00000033990; ENSMUSP00000033990; ENSMUSG00000031583.
    ENSMUST00000033991; ENSMUSP00000033991; ENSMUSG00000031583.
    GeneIDi22427.
    KEGGimmu:22427.
    UCSCiuc009ljw.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D86527 mRNA. Translation: BAA20270.1 .
    D86526 mRNA. Translation: BAA20269.1 .
    AF091215 mRNA. Translation: AAC78077.1 .
    AF091216 Genomic DNA. Translation: AAC72359.1 .
    AF241636 mRNA. Translation: AAF64490.1 .
    AC153789 Genomic DNA. No translation available.
    AC115809 Genomic DNA. No translation available.
    BC050921 mRNA. Translation: AAH50921.1 .
    BC060700 mRNA. Translation: AAH60700.1 .
    CCDSi CCDS22229.1.
    PIRi T17452.
    T30247.
    RefSeqi NP_001116294.1. NM_001122822.1.
    NP_035851.3. NM_011721.4.
    XP_006509154.1. XM_006509091.1.
    XP_006509155.1. XM_006509092.1.
    UniGenei Mm.228805.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2E6L X-ray 2.20 A 31-238 [» ]
    2E6M X-ray 2.00 A 31-238 [» ]
    ProteinModelPortali O09053.
    SMRi O09053. Positions 37-225, 488-1200.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-27642N.

    PTM databases

    PhosphoSitei O09053.

    Proteomic databases

    PaxDbi O09053.
    PRIDEi O09053.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033990 ; ENSMUSP00000033990 ; ENSMUSG00000031583 .
    ENSMUST00000033991 ; ENSMUSP00000033991 ; ENSMUSG00000031583 .
    GeneIDi 22427.
    KEGGi mmu:22427.
    UCSCi uc009ljw.1. mouse.

    Organism-specific databases

    CTDi 7486.
    MGIi MGI:109635. Wrn.

    Phylogenomic databases

    eggNOGi COG0514.
    GeneTreei ENSGT00550000074520.
    HOGENOMi HOG000146447.
    HOVERGENi HBG000325.
    InParanoidi Q80YP9.
    KOi K10900.
    OMAi GIEGDQW.
    OrthoDBi EOG7J70F2.
    TreeFami TF312852.

    Miscellaneous databases

    EvolutionaryTracei O09053.
    NextBioi 302865.
    PROi O09053.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O09053.
    Bgeei O09053.
    CleanExi MM_WRN.
    Genevestigatori O09053.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    1.10.150.80. 1 hit.
    3.30.420.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProi IPR002562. 3'-5'_exonuclease_dom.
    IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR004589. DNA_helicase_ATP-dep_RecQ.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR029491. Helicase_HTH.
    IPR010997. HRDC-like.
    IPR002121. HRDC_dom.
    IPR027417. P-loop_NTPase.
    IPR012337. RNaseH-like_dom.
    IPR018982. RQC_domain.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami 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.
    PF09382. RQC. 1 hit.
    [Graphical view ]
    SMARTi SM00474. 35EXOc. 1 hit.
    SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    SM00341. HRDC. 1 hit.
    SM00956. RQC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47819. SSF47819. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF53098. SSF53098. 1 hit.
    TIGRFAMsi TIGR00614. recQ_fam. 1 hit.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS50967. HRDC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of a mouse homologue of the human Werner syndrome gene and assignment to 8A4 by fluorescence in situ hybridization."
      Imamura O., Ichikawa K., Yamabe Y., Goto M., Sugawara M., Furuichi Y.
      Genomics 41:298-300(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Strain: BALB/c.
      Tissue: Spleen and Testis.
    2. "Genomic structure of the human Werner's gene and cloning of its mouse homolog."
      Paeper B.W., Gayle M., Brady W., Swartz A., Gillett L.A., Alisch R.S., Mulligan J., Galas D., Fu Y.-H.
      Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: Lymph node and Spleen.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6.
      Tissue: Brain.
    6. "Nucleolar localization of the Werner syndrome protein in human cells."
      Marciniak R.A., Lombard D.B., Johnson F.B., Guarente L.
      Proc. Natl. Acad. Sci. U.S.A. 95:6887-6892(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "A novel protein interacts with the Werner's syndrome gene product physically and functionally."
      Kawabe Y., Branzei D., Hayashi T., Suzuki H., Masuko T., Onoda F., Heo S.-J., Ikeda H., Shimamoto A., Furuichi Y., Seki M., Enomoto T.
      J. Biol. Chem. 276:20364-20369(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WRNIP1.
    8. "Probing the roles of active site residues in the 3'-5' exonuclease of the Werner syndrome protein."
      Choi J.M., Kang S.Y., Bae W.J., Jin K.S., Ree M., Cho Y.
      J. Biol. Chem. 282:9941-9951(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 31-238 IN COMPLEX WITH ZINC IONS AND SULFATE, SUBUNIT, FUNCTION, EXONUCLEASE ACTIVITY, ENZYME REGULATION, CIRCULAR DICHROISM, MUTAGENESIS OF LYS-185; ARG-190 AND TYR-206.

    Entry informationi

    Entry nameiWRN_MOUSE
    AccessioniPrimary (citable) accession number: O09053
    Secondary accession number(s): O09050
    , Q80YP9, Q9JKD4, Q9Z241, Q9Z242
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 132 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3