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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-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 similarity6 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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Nucleotide bindingi571 – 578ATPPROSITE-ProRule annotation8

GO - Molecular functioni

  • 3'-5' DNA helicase activity Source: UniProtKB
  • 3'-5' exonuclease activity Source: UniProtKB
  • ATPase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • ATP-dependent 3'-5' DNA helicase activity Source: GO_Central
  • ATP-dependent DNA helicase activity Source: UniProtKB
  • bubble DNA binding Source: UniProtKB
  • chromatin binding Source: Ensembl
  • DNA binding Source: UniProtKB
  • DNA helicase activity Source: UniProtKB
  • exonuclease activity Source: MGI
  • four-way junction helicase activity Source: UniProtKB
  • G-quadruplex DNA binding Source: UniProtKB
  • helicase activity Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • manganese ion binding Source: UniProtKB
  • protein complex binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • Y-form DNA binding Source: UniProtKB

GO - Biological processi

  • aging Source: UniProtKB
  • base-excision repair Source: UniProtKB
  • brain development Source: Ensembl
  • cell aging Source: UniProtKB
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to gamma radiation Source: UniProtKB
  • cellular response to starvation Source: MGI
  • DNA metabolic process Source: UniProtKB
  • DNA replication Source: UniProtKB
  • DNA synthesis involved in DNA repair Source: UniProtKB
  • double-strand break repair Source: UniProtKB
  • multicellular organism aging Source: UniProtKB
  • nucleolus to nucleoplasm transport Source: MGI
  • positive regulation of hydrolase activity Source: UniProtKB
  • protein sumoylation Source: Reactome
  • regulation of apoptotic process Source: MGI
  • regulation of growth rate Source: Ensembl
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • replication fork processing Source: UniProtKB
  • replicative cell aging Source: Ensembl
  • response to oxidative stress Source: UniProtKB
  • response to UV-C Source: UniProtKB
  • strand displacement Source: Reactome
  • telomere maintenance Source: UniProtKB
  • 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

BioCyciZFISH:ENSG00000165392-MONOMER.
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.

Names & Taxonomyi

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
Gene namesi
Name:WRN
Synonyms:RECQ3, RECQL2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:12791. WRN.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

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
Natural variantiVAR_026588125K → N in WRN. 1 PublicationCorresponds to variant rs387906337dbSNPEnsembl.1
Natural variantiVAR_026589135K → E in WRN. 1 PublicationCorresponds to variant rs267607008dbSNPEnsembl.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
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

DisGeNETi7486.
MalaCardsiWRN.
MIMi114500. phenotype.
277700. phenotype.
OpenTargetsiENSG00000165392.
Orphaneti902. Werner syndrome.
PharmGKBiPA367.

Chemistry databases

ChEMBLiCHEMBL2146312.

Polymorphism and mutation databases

BioMutaiWRN.
DMDMi322510082.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002050452 – 1432Werner syndrome ATP-dependent helicaseAdd BLAST1431

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei426PhosphoserineCombined sources1
Modified residuei440PhosphoserineCombined sources1
Modified residuei453PhosphoserineCombined sources1
Modified residuei467PhosphoserineCombined sources1
Modified residuei478PhosphoserineCombined sources1
Modified residuei1133PhosphoserineCombined sources1
Modified residuei1400PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated by PRKDC.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ14191.
MaxQBiQ14191.
PaxDbiQ14191.
PeptideAtlasiQ14191.
PRIDEiQ14191.

PTM databases

iPTMnetiQ14191.
PhosphoSitePlusiQ14191.

Expressioni

Gene expression databases

BgeeiENSG00000165392.
CleanExiHS_WRN.
GenevisibleiQ14191. HS.

Organism-specific databases

HPAiHPA028661.

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 (By similarity). Interacts with EXO1, PCNA and SUPV3L1. Interacts with PML (isoform PML-4).By similarity6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei145Interaction with DNACurated1
Sitei1037Interaction with DNA1

Binary interactionsi

WithEntry#Exp.IntActNotes
BLMP541329EBI-368417,EBI-621372
FEN1P397489EBI-368417,EBI-707816
PARP1P098748EBI-368417,EBI-355676
RAD52P433519EBI-368417,EBI-706448
RPA1P276949EBI-368417,EBI-621389
SIRT1Q96EB69EBI-368417,EBI-1802965
TERF2Q155548EBI-368417,EBI-706637
TP53P046375EBI-368417,EBI-366083
XRCC6P129565EBI-368417,EBI-353208

GO - Molecular functioni

  • protein complex binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi113323. 49 interactors.
DIPiDIP-31380N.
IntActiQ14191. 24 interactors.
MINTiMINT-95856.
STRINGi9606.ENSP00000298139.

Chemistry databases

BindingDBiQ14191.

Structurei

Secondary structure

11432
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi39 – 41Combined sources3
Beta strandi51 – 56Combined sources6
Helixi59 – 72Combined sources14
Beta strandi78 – 84Combined sources7
Beta strandi99 – 105Combined sources7
Beta strandi108 – 112Combined sources5
Helixi114 – 116Combined sources3
Beta strandi117 – 119Combined sources3
Helixi122 – 128Combined sources7
Beta strandi133 – 139Combined sources7
Helixi140 – 151Combined sources12
Beta strandi157 – 160Combined sources4
Helixi161 – 169Combined sources9
Helixi177 – 185Combined sources9
Helixi193 – 196Combined sources4
Beta strandi202 – 204Combined sources3
Helixi207 – 228Combined sources22
Beta strandi955 – 958Combined sources4
Helixi960 – 972Combined sources13
Turni973 – 975Combined sources3
Helixi980 – 986Combined sources7
Helixi996 – 1000Combined sources5
Turni1002 – 1009Combined sources8
Helixi1012 – 1024Combined sources13
Beta strandi1027 – 1032Combined sources6
Turni1036 – 1038Combined sources3
Beta strandi1039 – 1043Combined sources5
Helixi1045 – 1054Combined sources10
Beta strandi1062 – 1064Combined sources3
Helixi1147 – 1171Combined sources25
Helixi1175 – 1178Combined sources4
Helixi1181 – 1190Combined sources10
Helixi1195 – 1198Combined sources4
Beta strandi1201 – 1203Combined sources3
Helixi1206 – 1211Combined sources6
Helixi1213 – 1225Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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...

Miscellaneous databases

EvolutionaryTraceiQ14191.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini60 – 2283'-5' exonucleaseAdd BLAST169
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
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
Motifi668 – 671DEAH box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi507 – 510Poly-Glu4

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0351. Eukaryota.
KOG4373. Eukaryota.
COG0514. LUCA.
GeneTreeiENSGT00550000074520.
HOGENOMiHOG000146447.
HOVERGENiHBG000325.
InParanoidiQ14191.
KOiK10900.
OMAiYLIHMAI.
OrthoDBiEOG091G0B07.
PhylomeDBiQ14191.
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.

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
Checksum:i63F10D19E90AA461
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01745332K → R.1 PublicationCorresponds to variant rs34477820dbSNPEnsembl.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 rs2230009dbSNPEnsembl.1
Natural variantiVAR_026588125K → N in WRN. 1 PublicationCorresponds to variant rs387906337dbSNPEnsembl.1
Natural variantiVAR_026589135K → E in WRN. 1 PublicationCorresponds to variant rs267607008dbSNPEnsembl.1
Natural variantiVAR_017455172T → P Polymorphism; no effect on exonuclease activity. 2 PublicationsCorresponds to variant rs367991517dbSNPEnsembl.1
Natural variantiVAR_017456240N → K.1 PublicationCorresponds to variant rs148229804dbSNPEnsembl.1
Natural variantiVAR_006904324T → A.1 PublicationCorresponds to variant rs1800390dbSNPEnsembl.1
Natural variantiVAR_020450329Q → R.Corresponds to variant rs4987237dbSNPEnsembl.1
Natural variantiVAR_018941343E → K.1 PublicationCorresponds to variant rs11574222dbSNPEnsembl.1
Natural variantiVAR_020451383L → F.Corresponds to variant rs4987238dbSNPEnsembl.1
Natural variantiVAR_017457383L → W.1 Publication1
Natural variantiVAR_006905387M → I.4 PublicationsCorresponds to variant rs1800391dbSNPEnsembl.1
Natural variantiVAR_018942533N → S.1 PublicationCorresponds to variant rs11574240dbSNPEnsembl.1
Natural variantiVAR_018943612S → C.1 PublicationCorresponds to variant rs11574250dbSNPEnsembl.1
Natural variantiVAR_018944708S → F.1 PublicationCorresponds to variant rs11574289dbSNPEnsembl.1
Natural variantiVAR_057124711R → W.Corresponds to variant rs34560788dbSNPEnsembl.1
Natural variantiVAR_017458724Q → L.1 Publication1
Natural variantiVAR_014913834R → C.1 PublicationCorresponds to variant rs3087425dbSNPEnsembl.1
Natural variantiVAR_018945912I → S.1 PublicationCorresponds to variant rs11574323dbSNPEnsembl.1
Natural variantiVAR_0079031074L → F.5 PublicationsCorresponds to variant rs1801195dbSNPEnsembl.1
Natural variantiVAR_0149141079S → L.1 PublicationCorresponds to variant rs3087414dbSNPEnsembl.1
Natural variantiVAR_0189461133S → A.1 PublicationCorresponds to variant rs11574358dbSNPEnsembl.1
Natural variantiVAR_0541621141S → L.1 PublicationCorresponds to variant rs139323683dbSNPEnsembl.1
Natural variantiVAR_0174591269K → E.1 PublicationCorresponds to variant rs746648510dbSNPEnsembl.1
Natural variantiVAR_0189471339V → I.1 PublicationCorresponds to variant rs11574395dbSNPEnsembl.1
Natural variantiVAR_0069061367C → R Polymorphism associated with a higher risk of myocardial infarction. 4 PublicationsCorresponds to variant rs1346044dbSNPEnsembl.1

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.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

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:
PDBei
RCSB PDBi
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. 49 interactors.
DIPiDIP-31380N.
IntActiQ14191. 24 interactors.
MINTiMINT-95856.
STRINGi9606.ENSP00000298139.

Chemistry databases

BindingDBiQ14191.
ChEMBLiCHEMBL2146312.

PTM databases

iPTMnetiQ14191.
PhosphoSitePlusiQ14191.

Polymorphism and mutation databases

BioMutaiWRN.
DMDMi322510082.

Proteomic databases

EPDiQ14191.
MaxQBiQ14191.
PaxDbiQ14191.
PeptideAtlasiQ14191.
PRIDEiQ14191.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7486.
DisGeNETi7486.
GeneCardsiWRN.
GeneReviewsiWRN.
H-InvDBHIX0007441.
HGNCiHGNC:12791. WRN.
HPAiHPA028661.
MalaCardsiWRN.
MIMi114500. phenotype.
277700. phenotype.
604611. gene.
neXtProtiNX_Q14191.
OpenTargetsiENSG00000165392.
Orphaneti902. Werner syndrome.
PharmGKBiPA367.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0351. Eukaryota.
KOG4373. Eukaryota.
COG0514. LUCA.
GeneTreeiENSGT00550000074520.
HOGENOMiHOG000146447.
HOVERGENiHBG000325.
InParanoidiQ14191.
KOiK10900.
OMAiYLIHMAI.
OrthoDBiEOG091G0B07.
PhylomeDBiQ14191.
TreeFamiTF312852.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000165392-MONOMER.
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

ChiTaRSiWRN. human.
EvolutionaryTraceiQ14191.
GeneWikiiWerner_syndrome_ATP-dependent_helicase.
GenomeRNAii7486.
PROiQ14191.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000165392.
CleanExiHS_WRN.
GenevisibleiQ14191. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: Q14191
Secondary accession number(s): A1KYY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: February 8, 2011
Last modified: November 30, 2016
This is version 192 of the entry and version 2 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.