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O09053

- WRN_MOUSE

UniProt

O09053 - WRN_MOUSE

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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

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.2 Publications

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 DNA By similarity
Metal bindingi210 – 2101Magnesium 1; catalytic
Sitei1002 – 10021Interaction with DNA By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi535 – 5428ATP By similarity

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. G-quadruplex DNA binding Source: Ensembl
  5. Y-form DNA binding Source: Ensembl
  6. bubble DNA binding Source: Ensembl
  7. four-way junction helicase activity Source: Ensembl
  8. magnesium ion binding Source: UniProtKB
  9. manganese ion binding Source: UniProtKB
  10. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. DNA metabolic process Source: UniProtKB
  2. DNA recombination Source: InterPro
  3. DNA replication Source: MGI
  4. DNA synthesis involved in DNA repair Source: Ensembl
  5. base-excision repair Source: Ensembl
  6. cellular response to gamma radiation Source: UniProtKB
  7. cellular response to starvation Source: MGI
  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 UV-C Source: Ensembl
  18. response to oxidative stress Source: Ensembl
  19. telomere maintenance Source: MGI
Complete GO annotation...

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. 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.1 Publication

GO - Cellular componenti

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

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 homolog
PRO_0000205046Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei419 – 4191Phosphoserine By similarity
Modified residuei433 – 4331Phosphoserine By similarity
Modified residuei1098 – 10981Phosphoserine By 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.2 Publications

Protein-protein interaction databases

DIPiDIP-27642N.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiO09053.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini51 – 2231733'-5' exonuclease
Add
BLAST
Domaini522 – 688167Helicase ATP-binding
Add
BLAST
Domaini713 – 866154Helicase C-terminal
Add
BLAST
Domaini1115 – 119480HRDC
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 271271Interaction with WRNIP1
Add
BLAST
Regioni952 – 9587Interaction with DNA By 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

Contains 1 HRDC domain.

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

Sequence conflict

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

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...

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 131 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

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