Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Werner syndrome ATP-dependent helicase homolog

Gene

Wrn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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).By similarity2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.1 Publication

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

Enzyme regulationi

Zinc ions stimulate the exonuclease activity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi76Magnesium 1; catalyticCombined sources1 Publication1
Metal bindingi76Magnesium 2; catalyticCombined sources1 Publication1
Metal bindingi78Magnesium 1; catalyticCombined sources1 Publication1
Metal bindingi210Magnesium 1; catalyticCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi535 – 542ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

  • base-excision repair Source: MGI
  • brain development Source: Ensembl
  • cell aging Source: MGI
  • cellular response to DNA damage stimulus Source: MGI
  • cellular response to gamma radiation Source: UniProtKB
  • cellular response to starvation Source: MGI
  • DNA duplex unwinding Source: GO_Central
  • DNA metabolic process Source: UniProtKB
  • DNA replication Source: MGI
  • DNA synthesis involved in DNA repair Source: MGI
  • double-strand break repair Source: UniProtKB
  • multicellular organism aging Source: MGI
  • nucleolus to nucleoplasm transport Source: MGI
  • positive regulation of hydrolase activity Source: MGI
  • regulation of apoptotic process Source: MGI
  • regulation of growth rate Source: MGI
  • replication fork processing Source: MGI
  • replicative cell aging Source: MGI
  • response to oxidative stress Source: MGI
  • response to UV-C Source: MGI
  • telomere maintenance Source: MGI
  • telomere maintenance via recombination Source: GO_Central
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

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Werner syndrome ATP-dependent helicase homolog (EC:3.6.4.121 Publication)
Alternative name(s):
Exonuclease WRN (EC:3.1.-.-)
Gene namesi
Name:Wrn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:109635. Wrn.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: MGI
  • cytoplasm Source: GO_Central
  • MutLalpha complex Source: Ensembl
  • neuron projection Source: Ensembl
  • nuclear chromosome, telomeric region Source: GO_Central
  • nucleolus Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi185K → A: Loss of exonuclease activity. 1 Publication1
Mutagenesisi190R → A: Strongly reduced exonuclease activity. 1 Publication1
Mutagenesisi206Y → F: Loss of exonuclease activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002050461 – 1401Werner syndrome ATP-dependent helicase homologAdd BLAST1401

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei419PhosphoserineBy similarity1
Modified residuei433PhosphoserineBy similarity1
Modified residuei444PhosphoserineBy similarity1
Modified residuei1098PhosphoserineBy similarity1
Modified residuei1364PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated by PRKDC.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO09053.
PaxDbiO09053.
PeptideAtlasiO09053.
PRIDEiO09053.

PTM databases

iPTMnetiO09053.
PhosphoSitePlusiO09053.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSMUSG00000031583.
CleanExiMM_WRN.
GenevisibleiO09053. MM.

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei139Interaction with DNABy similarity1
Sitei1002Interaction with DNABy similarity1

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-27642N.
STRINGi10090.ENSMUSP00000033990.

Structurei

Secondary structure

11401
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi45 – 50Combined sources6
Helixi53 – 66Combined sources14
Beta strandi72 – 78Combined sources7
Beta strandi93 – 97Combined sources5
Beta strandi99 – 106Combined sources8
Helixi108 – 110Combined sources3
Helixi116 – 122Combined sources7
Beta strandi127 – 133Combined sources7
Helixi134 – 145Combined sources12
Beta strandi151 – 154Combined sources4
Helixi155 – 162Combined sources8
Helixi171 – 179Combined sources9
Helixi187 – 190Combined sources4
Beta strandi196 – 198Combined sources3
Helixi201 – 222Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E6LX-ray2.20A31-238[»]
2E6MX-ray2.00A31-238[»]
ProteinModelPortaliO09053.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO09053.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini51 – 2233'-5' exonucleaseAdd BLAST173
Domaini522 – 688Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST167
Domaini713 – 866Helicase C-terminalPROSITE-ProRule annotationAdd BLAST154
Domaini1115 – 1194HRDCPROSITE-ProRule annotationAdd BLAST80

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 271Interaction with WRNIP11 PublicationAdd BLAST271
Regioni952 – 958Interaction with DNABy similarity7

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi632 – 635DEAH box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1387 – 1390Poly-Ser4

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

eggNOGiKOG0351. Eukaryota.
KOG4373. Eukaryota.
COG0514. LUCA.
GeneTreeiENSGT00550000074520.
HOGENOMiHOG000146447.
HOVERGENiHBG000325.
InParanoidiO09053.
KOiK10900.
OMAiYLIHMAI.
OrthoDBiEOG091G0B07.
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. DEAD/DEAH_box_helicase_dom.
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.
IPR032284. RecQ_Zn-bd.
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.
PF16124. RecQ_Zn_bind. 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]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF47819. 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

        10         20         30         40         50
METTSLQRKF PEWMSMQSQR CATEEKACVQ KSVLEDNLPF LEFPGSIVYS
60 70 80 90 100
YEASDCSFLS EDISMRLSDG DVVGFDMEWP PIYKPGKRSR VAVIQLCVSE
110 120 130 140 150
SKCYLFHISS MSVFPQGLKM LLENKSIKKA GVGIEGDQWK LLRDFDVKLE
160 170 180 190 200
SFVELTDVAN EKLKCAETWS LNGLVKHVLG KQLLKDKSIR CSNWSNFPLT
210 220 230 240 250
EDQKLYAATD AYAGLIIYQK LGNLGDTAQV FALNKAEENL PLEMKKQLNS
260 270 280 290 300
ISEEMRDLAN RFPVTCRNLE TLQRVPVILK SISENLCSLR KVICGPTNTE
310 320 330 340 350
TRLKPGSSFN LLSSEDSAAA GEKEKQIGKH STFAKIKEEP WDPELDSLVK
360 370 380 390 400
QEEVDVFRNQ VKQEKGESEN EIEDNLLRED MERTCVIPSI SENELQDLEQ
410 420 430 440 450
QAKEEKYNDV SHQLSEHLSP NDDENDSSYI IESDEDLEME MLKSLENLNS
460 470 480 490 500
DVVEPTHSTW LEMGTNGRLP PEEEDGHGNE AIKEEQEEED HLLPEPNAKQ
510 520 530 540 550
INCLKTYFGH SSFKPVQWKV IHSVLEERRD NVVVMATGYG KSLCFQYPPV
560 570 580 590 600
YTGKIGIVIS PLISLMEDQV LQLELSNVPA CLLGSAQSKN ILGDVKLGKY
610 620 630 640 650
RVIYITPEFC SGNLDLLQQL DSSIGITLIA VDEAHCISEW GHDFRSSFRM
660 670 680 690 700
LGSLKTALPL VPVIALSATA SSSIREDIIS CLNLKDPQIT CTGFDRPNLY
710 720 730 740 750
LEVGRKTGNI LQDLKPFLVR KASSAWEFEG PTIIYCPSRK MTEQVTAELG
760 770 780 790 800
KLNLACRTYH AGMKISERKD VHHRFLRDEI QCVVATVAFG MGINKADIRK
810 820 830 840 850
VIHYGAPKEM ESYYQEIGRA GRDGLQSSCH LLWAPADFNT SRNLLIEIHD
860 870 880 890 900
EKFRLYKLKM MVKMEKYLHS SQCRRRIILS HFEDKCLQKA SLDIMGTEKC
910 920 930 940 950
CDNCRPRLNH CLTANNSEDA SQDFGPQAFQ LLSAVDILQE KFGIGIPILF
960 970 980 990 1000
LRGSNSQRLP DKYRGHRLFG AGKEQAESWW KTLSHHLIAE GFLVEVPKEN
1010 1020 1030 1040 1050
KYIKTCSLTK KGRKWLGEAS SQSPPSLLLQ ANEEMFPRKV LLPSSNPVSP
1060 1070 1080 1090 1100
ETTQHSSNQN PAGLTTKQSN LERTHSYKVP EKVSSGTNIP KKSAVMPSPG
1110 1120 1130 1140 1150
TSSSPLEPAI SAQELDARTG LYARLVEARQ KHANKMDVPP AILATNKVLL
1160 1170 1180 1190 1200
DMAKMRPTTV ENMKQIDGVS EGKAALLAPL LEVIKHFCQV TSVQTDLLSS
1210 1220 1230 1240 1250
AKPHKEQEKS QEMEKKDCSL PQSVAVTYTL FQEKKMPLHS IAENRLLPLT
1260 1270 1280 1290 1300
AAGMHLAQAV KAGYPLDMER AGLTPETWKI IMDVIRNPPI NSDMYKVKLI
1310 1320 1330 1340 1350
RMLVPENLDT YLIHMAIEIL QSGSDSRTQP PCDSSRKRRF PSSAESCESC
1360 1370 1380 1390 1400
KESKEAVTET KASSSESKRK LPEWFAKGNV PSADTGSSSS MAKTKKKGLF

S
Length:1,401
Mass (Da):157,204
Last modified:July 27, 2011 - v3
Checksum:i66DF2252B17C24C3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti101S → N in BAA20269 (PubMed:9143515).Curated1
Sequence conflicti101S → N in BAA20270 (PubMed:9143515).Curated1
Sequence conflicti101S → N in AAC72359 (Ref. 2) Curated1
Sequence conflicti101S → N in AAF64490 (PubMed:10757812).Curated1
Sequence conflicti228A → V in BAA20269 (PubMed:9143515).Curated1
Sequence conflicti228A → V in BAA20270 (PubMed:9143515).Curated1
Sequence conflicti228A → V in AAC72359 (Ref. 2) Curated1
Sequence conflicti228A → V in AAF64490 (PubMed:10757812).Curated1
Sequence conflicti250S → L in BAA20269 (PubMed:9143515).Curated1
Sequence conflicti250S → L in BAA20270 (PubMed:9143515).Curated1
Sequence conflicti250S → L in AAC72359 (Ref. 2) Curated1
Sequence conflicti250S → L in AAF64490 (PubMed:10757812).Curated1
Sequence conflicti452V → M in BAA20269 (PubMed:9143515).Curated1
Sequence conflicti452V → M in BAA20270 (PubMed:9143515).Curated1
Sequence conflicti452V → M in AAC72359 (Ref. 2) Curated1
Sequence conflicti452V → M in AAF64490 (PubMed:10757812).Curated1
Sequence conflicti459T → K in BAA20269 (PubMed:9143515).Curated1
Sequence conflicti459T → K in BAA20270 (PubMed:9143515).Curated1
Sequence conflicti459T → K in AAC72359 (Ref. 2) Curated1
Sequence conflicti459T → K in AAF64490 (PubMed:10757812).Curated1
Sequence conflicti468R → C in BAA20269 (PubMed:9143515).Curated1
Sequence conflicti468R → C in BAA20270 (PubMed:9143515).Curated1
Sequence conflicti468R → C in AAC72359 (Ref. 2) Curated1
Sequence conflicti468R → C in AAF64490 (PubMed:10757812).Curated1
Sequence conflicti619Q → K in BAA20269 (PubMed:9143515).Curated1
Sequence conflicti619Q → K in BAA20270 (PubMed:9143515).Curated1
Sequence conflicti619Q → K in AAC72359 (Ref. 2) Curated1
Sequence conflicti619Q → K in AAF64490 (PubMed:10757812).Curated1
Sequence conflicti800K → Q in BAA20270 (PubMed:9143515).Curated1
Sequence conflicti800K → Q in BAA20269 (PubMed:9143515).Curated1
Sequence conflicti844L → H in AAC72359 (Ref. 2) Curated1
Sequence conflicti955 – 988NSQRL…SHHLI → VSVSVIAPGTVSDSAFHCVA MALAFFRWLTSNPC in AAC72359 (Ref. 2) CuratedAdd BLAST34
Sequence conflicti1021S → L in BAA20269 (PubMed:9143515).Curated1
Sequence conflicti1021S → L in BAA20270 (PubMed:9143515).Curated1
Sequence conflicti1021S → L in AAF64490 (PubMed:10757812).Curated1
Sequence conflicti1145T → A in BAA20270 (PubMed:9143515).Curated1
Sequence conflicti1145T → A in BAA20269 (PubMed:9143515).Curated1
Sequence conflicti1181L → V in BAA20270 (PubMed:9143515).Curated1
Sequence conflicti1181L → V in BAA20269 (PubMed:9143515).Curated1
Sequence conflicti1182E → G in BAA20269 (PubMed:9143515).Curated1
Sequence conflicti1182E → G in BAA20270 (PubMed:9143515).Curated1
Sequence conflicti1182E → G in AAF64490 (PubMed:10757812).Curated1
Sequence conflicti1252A → V in BAA20269 (PubMed:9143515).Curated1
Sequence conflicti1252A → V in BAA20270 (PubMed:9143515).Curated1
Sequence conflicti1252A → V in AAF64490 (PubMed:10757812).Curated1
Sequence conflicti1308L → I in BAA20269 (PubMed:9143515).Curated1
Sequence conflicti1308L → I in BAA20270 (PubMed:9143515).Curated1
Sequence conflicti1308L → I in AAF64490 (PubMed:10757812).Curated1
Sequence conflicti1356A → V in BAA20269 (PubMed:9143515).Curated1
Sequence conflicti1356A → V in BAA20270 (PubMed:9143515).Curated1
Sequence conflicti1356A → V in AAF64490 (PubMed:10757812).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006509091.3.
XP_017168151.1. XM_017312662.1.
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:
EMBLi
GenBanki
DDBJi
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_006509091.3.
XP_017168151.1. XM_017312662.1.
UniGeneiMm.228805.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E6LX-ray2.20A31-238[»]
2E6MX-ray2.00A31-238[»]
ProteinModelPortaliO09053.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-27642N.
STRINGi10090.ENSMUSP00000033990.

PTM databases

iPTMnetiO09053.
PhosphoSitePlusiO09053.

Proteomic databases

MaxQBiO09053.
PaxDbiO09053.
PeptideAtlasiO09053.
PRIDEiO09053.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7486.
MGIiMGI:109635. Wrn.

Phylogenomic databases

eggNOGiKOG0351. Eukaryota.
KOG4373. Eukaryota.
COG0514. LUCA.
GeneTreeiENSGT00550000074520.
HOGENOMiHOG000146447.
HOVERGENiHBG000325.
InParanoidiO09053.
KOiK10900.
OMAiYLIHMAI.
OrthoDBiEOG091G0B07.
TreeFamiTF312852.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiO09053.
PROiO09053.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031583.
CleanExiMM_WRN.
GenevisibleiO09053. MM.

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. DEAD/DEAH_box_helicase_dom.
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.
IPR032284. RecQ_Zn-bd.
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.
PF16124. RecQ_Zn_bind. 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]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF47819. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 154 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.