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 similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Cofactori

Mg2+, Mn2+, Zn2+Note: 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' DNA helicase activity Source: MGI
  2. 3'-5' exonuclease activity Source: UniProtKB
  3. ATPase activity Source: MGI
  4. ATP binding Source: UniProtKB-KW
  5. ATP-dependent 3'-5' DNA helicase activity Source: InterPro
  6. ATP-dependent DNA helicase activity Source: MGI
  7. bubble DNA binding Source: MGI
  8. DNA binding Source: MGI
  9. DNA helicase activity Source: MGI
  10. exonuclease activity Source: MGI
  11. four-way junction helicase activity Source: MGI
  12. G-quadruplex DNA binding Source: MGI
  13. helicase activity Source: MGI
  14. magnesium ion binding Source: UniProtKB
  15. manganese ion binding Source: UniProtKB
  16. protein complex binding Source: MGI
  17. protein homodimerization activity Source: MGI
  18. Y-form DNA binding Source: MGI

GO - Biological processi

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

MaxQBiO09053.
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

BgeeiO09053.
CleanExiMM_WRN.
ExpressionAtlasiO09053. baseline and differential.
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:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E6LX-ray2.20A31-238[»]
2E6MX-ray2.00A31-238[»]
ProteinModelPortaliO09053.
SMRiO09053. Positions 37-225, 495-1058, 1107-1200.
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.
InParanoidiO09053.
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. 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.
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

        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 26, 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 (Ref. 2) Curated
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 (Ref. 2) Curated
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 (Ref. 2) Curated
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 (Ref. 2) Curated
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 (Ref. 2) Curated
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 (Ref. 2) Curated
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 (Ref. 2) Curated
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 (Ref. 2) Curated
Sequence conflicti955 – 98834NSQRL…SHHLI → VSVSVIAPGTVSDSAFHCVA MALAFFRWLTSNPC in AAC72359 (Ref. 2) CuratedAdd
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:
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_006509091.2.
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_006509091.2.
UniGeneiMm.228805.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E6LX-ray2.20A31-238[»]
2E6MX-ray2.00A31-238[»]
ProteinModelPortaliO09053.
SMRiO09053. Positions 37-225, 495-1058, 1107-1200.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-27642N.

PTM databases

PhosphoSiteiO09053.

Proteomic databases

MaxQBiO09053.
PaxDbiO09053.
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

eggNOGiCOG0514.
GeneTreeiENSGT00550000074520.
HOGENOMiHOG000146447.
HOVERGENiHBG000325.
InParanoidiO09053.
KOiK10900.
OMAiGIEGDQW.
OrthoDBiEOG7J70F2.
TreeFamiTF312852.

Miscellaneous databases

EvolutionaryTraceiO09053.
NextBioi302865.
PROiO09053.
SOURCEiSearch...

Gene expression databases

BgeeiO09053.
CleanExiMM_WRN.
ExpressionAtlasiO09053. baseline and differential.
GenevestigatoriO09053.

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.
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]
ProtoNetiSearch...

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(1996) [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 (AUG-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(2003) [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(1997) [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(2000) [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(2006) [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 14, 1998
Last sequence update: July 26, 2011
Last modified: March 31, 2015
This is version 138 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

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 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.