Werner syndrome ATP-dependent helicase

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Reviewed, UniProtKB/Swiss-Prot Q14191 (WRN_HUMAN)

Last modified February 9, 2010. Version 121. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
Werner syndrome ATP-dependent helicase
EC=3.6.1.-

Gene names

Name:	WRN
Synonyms:	RECQ3, RECQL2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	1432 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Essential for the formation of DNA replication focal centers; stably associates with foci elements generating binding sites for RP-A. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity. May be involved in the control of genomic stability By similarity.
Subunit structure	Interacts via its N-terminal domain with WRNIP1 By similarity. Interacts with EXO1. Ref.8
Subcellular location	Nucleus › nucleolus Ref.5.
Post-translational modification	Phosphorylated by PRKDC. Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.7 Ref.9 Ref.10 Ref.12 Ref.13
Involvement in disease	Defects in WRN are a cause of Werner syndrome (WRN) [MIM:277700]. WRN is a 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. Currently all known WS mutations produces prematurely terminated proteins. Ref.24 Defects in WRN may be a cause of colorectal cancer (CRC) [MIM:114500].
Sequence similarities	Belongs to the helicase family. RecQ subfamily. Contains 1 3'-5' exonuclease domain. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain. Contains 1 HRDC domain.

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Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Repeat
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	DNA recombination Inferred from electronic annotation. Source: InterPro DNA synthesis during DNA repair Inferred from direct assay. Source: UniProtKB base-excision repair Inferred from direct assay. Source: UniProtKB multicellular organismal aging Ref.24 Inferred from mutant phenotype. Source: UniProtKB positive regulation of hydrolase activity Inferred from direct assay. Source: UniProtKB regulation of apoptosis Inferred from genetic interaction. Source: MGI replication fork processing Inferred from direct assay. Source: UniProtKB response to UV-C Inferred from direct assay. Source: UniProtKB response to oxidative stress Inferred from direct assay. Source: UniProtKB telomere maintenance Inferred from mutant phenotype. Source: UniProtKB
Cellular component	centrosome Inferred from direct assay. Source: UniProtKB nucleolus Ref.5 Inferred from direct assay. Source: UniProtKB nucleoplasm Inferred from direct assay. Source: MGI
Molecular function	3'-5' exonuclease activity Inferred from direct assay. Source: UniProtKB ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent 3'-5' DNA helicase activity Inferred from electronic annotation. Source: InterPro G-quadruplex DNA binding Inferred from direct assay. Source: UniProtKB Y-form DNA binding Inferred from direct assay. Source: UniProtKB bubble DNA binding Inferred from direct assay. Source: UniProtKB four-way junction helicase activity Inferred from direct assay. Source: UniProtKB protein complex binding Inferred from direct assay. Source: UniProtKB protein homodimerization activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
BLM	P54132	4	EBI-368417,EBI-621372
FEN1	P39748	7	EBI-368417,EBI-707816
PARP1	P09874	2	EBI-368417,EBI-355676
RAD52	P43351	4	EBI-368417,EBI-706448
RPA1	P27694	4	EBI-368417,EBI-621389
TERF2	Q15554	4	EBI-368417,EBI-706637
TP53	P04637	2	EBI-368417,EBI-366083
VCP	P55072	1	EBI-368417,EBI-355164
VCP	Q3ZBT1	1	EBI-368417,EBI-706432	From a different organism.

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1432

1432

Werner syndrome ATP-dependent helicase

PRO_0000205045

Regions

Repeat

424 – 450

Repeat

451 – 477

Domain

558 – 724

167

Helicase ATP-binding

Domain

749 – 899

151

Helicase C-terminal

Domain

1150 – 1229

HRDC

Nucleotide binding

571 – 578

ATP By similarity

Region

1 – 277

277

Interaction with WRNIP1 By similarity

Region

424 – 477

2 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-K

Motif

668 – 671

DEAH box

Compositional bias

507 – 510

Poly-Glu

Amino acid modifications

Modified residue

426

Phosphoserine Ref.13

Modified residue

453

Phosphoserine Ref.10

Modified residue

467

Phosphoserine Ref.10 Ref.13

Modified residue

1058

Phosphoserine Ref.9

Modified residue

1133

Phosphoserine Ref.12 Ref.13

Modified residue

1141

Phosphoserine Ref.9

Natural variations

Natural variant

K → R: dbSNP rs34477820. Ref.23

VAR_017453

Natural variant

G → V in a colorectal cancer sample; somatic mutation. Ref.25

VAR_036318

Natural variant

114

V → I: dbSNP rs2230009. Ref.23 Ref.4

VAR_017454

Natural variant

125

K → N in WRN. Ref.24

VAR_026588

Natural variant

135

K → E in WRN. Ref.24

VAR_026589

Natural variant

172

T → P

VAR_017455

Natural variant

240

N → K

VAR_017456

Natural variant

324

T → A: dbSNP rs1800390. Ref.22

VAR_006904

Natural variant

329

Q → R: dbSNP rs4987237.

VAR_020450

Natural variant

343

E → K: dbSNP rs11574222. Ref.4

VAR_018941

Natural variant

383

L → F: dbSNP rs4987238.

VAR_020451

Natural variant

383

L → W

VAR_017457

Natural variant

387

M → I: dbSNP rs1800391. Ref.23 Ref.4 Ref.20 Ref.21

VAR_006905

Natural variant

533

N → S: dbSNP rs11574240. Ref.4

VAR_018942

Natural variant

612

S → C: dbSNP rs11574250. Ref.4

VAR_018943

Natural variant

708

S → F: dbSNP rs11574289. Ref.4

VAR_018944

Natural variant

711

R → W: dbSNP rs34560788.

VAR_057124

Natural variant

724

Q → L

VAR_017458

Natural variant

834

R → C: dbSNP rs3087425. Ref.4

VAR_014913

Natural variant

912

I → S: dbSNP rs11574323. Ref.4

VAR_018945

Natural variant

1074

F → L: dbSNP rs1801195. Ref.23 Ref.4 Ref.20

VAR_007903

Natural variant

1079

S → L: dbSNP rs3087414. Ref.4

VAR_014914

Natural variant

1133

S → A: dbSNP rs11574358. Ref.4

VAR_018946

Natural variant

1141

S → L

VAR_054162

Natural variant

1269

K → E

VAR_017459

Natural variant

1339

V → I: dbSNP rs11574395. Ref.4

VAR_018947

Natural variant

1367

C → R Polymorphism associated with a higher risk of myocardial infarction. dbSNP rs1346044. Ref.23 Ref.4 Ref.22 Ref.18

VAR_006906

Secondary structure

1432

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q14191-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: DF02C0059F7B62EB
Show »

FASTA

1,432

162,495

        10         20         30         40         50         60 
MSEKKLETTA QQRKCPEWMN VQNKRCAVEE RKACVRKSVF EDDLPFLEFT GSIVYSYDAS 

        70         80         90        100        110        120 
DCSFLSEDIS MSLSDGDVVG FDMEWPPLYN RGKLGKVALI QLCVSESKCY LFHVSSMSVF 

       130        140        150        160        170        180 
PQGLKMLLEN KAVKKAGVGI EGDQWKLLRD FDIKLKNFVE LTDVANKKLK CTETWSLNSL 

       190        200        210        220        230        240 
VKHLLGKQLL KDKSIRCSNW SKFPLTEDQK LYAATDAYAG FIIYRNLEIL DDTVQRFAIN 

       250        260        270        280        290        300 
KEEEILLSDM NKQLTSISEE VMDLAKHLPH AFSKLENPRR VSILLKDISE NLYSLRRMII 

       310        320        330        340        350        360 
GSTNIETELR PSNNLNLLSF EDSTTGGVQQ KQIREHEVLI HVEDETWDPT LDHLAKHDGE 

       370        380        390        400        410        420 
DVLGNKVERK EDGFEDGVED NKLKENMERA CLMSLDITEH ELQILEQQSQ EEYLSDIAYK 

       430        440        450        460        470        480 
STEHLSPNDN ENDTSYVIES DEDLEMEMLK HLSPNDNEND TSYVIESDED LEMEMLKSLE 

       490        500        510        520        530        540 
NLNSGTVEPT HSKCLKMERN LGLPTKEEEE DDENEANEGE EDDDKDFLWP APNEEQVTCL 

       550        560        570        580        590        600 
KMYFGHSSFK PVQWKVIHSV LEERRDNVAV MATGYGKSLC FQYPPVYVGK IGLVISPLIS 

       610        620        630        640        650        660 
LMEDQVLQLK MSNIPACFLG SAQSENVLTD IKLGKYRIVY VTPEYCSGNM GLLQQLEADI 

       670        680        690        700        710        720 
GITLIAVDEA HCISEWGHDF RDSFRKLGSL KTALPMVPIV ALTATASSSI REDIVRCLNL 

       730        740        750        760        770        780 
RNPQITCTGF DRPNLYLEVR RKTGNILQDL QPFLVKTSSH WEFEGPTIIY CPSRKMTQQV 

       790        800        810        820        830        840 
TGELRKLNLS CGTYHAGMSF STRKDIHHRF VRDEIQCVIA TIAFGMGINK ADIRQVIHYG 

       850        860        870        880        890        900 
APKDMESYYQ EIGRAGRDGL QSSCHVLWAP ADINLNRHLL TEIRNEKFRL YKLKMMAKME 

       910        920        930        940        950        960 
KYLHSSRCRR QIILSHFEDK QVQKASLGIM GTEKCCDNCR SRLDHCYSMD DSEDTSWDFG 

       970        980        990       1000       1010       1020 
PQAFKLLSAV DILGEKFGIG LPILFLRGSN SQRLADQYRR HSLFGTGKDQ TESWWKAFSR 

      1030       1040       1050       1060       1070       1080 
QLITEGFLVE VSRYNKFMKI CALTKKGRNW LHKANTESQS LILQANEELC PKKFLLPSSK 

      1090       1100       1110       1120       1130       1140 
TVSSGTKEHC YNQVPVELST EKKSNLEKLY SYKPCDKISS GSNISKKSIM VQSPEKAYSS 

      1150       1160       1170       1180       1190       1200 
SQPVISAQEQ ETQIVLYGKL VEARQKHANK MDVPPAILAT NKILVDMAKM RPTTVENVKR 

      1210       1220       1230       1240       1250       1260 
IDGVSEGKAA MLAPLLEVIK HFCQTNSVQT DLFSSTKPQE EQKTSLVAKN KICTLSQSMA 

      1270       1280       1290       1300       1310       1320 
ITYSLFQEKK MPLKSIAESR ILPLMTIGMH LSQAVKAGCP LDLERAGLTP EVQKIIADVI 

      1330       1340       1350       1360       1370       1380 
RNPPVNSDMS KISLIRMLVP ENIDTYLIHM AIEILKHGPD SGLQPSCDVN KRRCFPGSEE 

      1390       1400       1410       1420       1430 
ICSSSKRSKE EVGINTETSS AERKRRLPVW FAKGSDTSKK LMDKTKRGGL FS

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Positional cloning of the Werner's syndrome gene." Yu C.-E., Oshima J., Fu Y.-H., Wijsman E.M., Hisama F., Alisch R., Matthews S., Nakura J., Miki T., Ouais S., Martin G.M., Mulligan J., Schellenberg G.D. Science 272:258-262(1996) [PubMed: 8602509] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genomic structure of the human Werner's gene and cloning of the 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-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Epigenetic inactivation of the premature aging Werner syndrome gene in human cancer." Agrelo R., Cheng W.H., Setien F., Ropero S., Espada J., Fraga M.F., Herranz M., Paz M.F., Sanchez-Cespedes M., Artiga M.J., Guerrero D., Castells A., von Kobbe C., Bohr V.A., Esteller M. Proc. Natl. Acad. Sci. U.S.A. 103:8822-8827(2006) [PubMed: 16723399] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	NIEHS SNPs program Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-114; LYS-343; ILE-387; SER-533; CYS-612; PHE-708; CYS-834; SER-912; LEU-1074; LEU-1079; ALA-1133; ILE-1339 AND ARG-1367.
[5]	"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: 9618508] [Abstract] Cited for: SUBCELLULAR LOCATION.
[6]	"Evolution of the RECQ family of helicases: a Drosophila homolog, Dmblm, is similar to the human Bloom syndrome gene." Kusano K., Berres M.E., Engels W.R. Genetics 151:1027-1039(1999) [PubMed: 10049920] [Abstract] Cited for: REPEATS.
[7]	"Werner protein is a target of DNA-dependent protein kinase in vivo and in vitro, and its catalytic activities are regulated by phosphorylation." Karmakar P., Piotrowski J., Brosh R.M. Jr., Sommers J.A., Miller S.P., Cheng W.H., Snowden C.M., Ramsden D.A., Bohr V.A. J. Biol. Chem. 277:18291-18302(2002) [PubMed: 11889123] [Abstract] Cited for: PHOSPHORYLATION.
[8]	"The exonucleolytic and endonucleolytic cleavage activities of human exonuclease 1 are stimulated by an interaction with the carboxyl-terminal region of the Werner syndrome protein." Sharma S., Sommers J.A., Driscoll H.C., Uzdilla L.A., Wilson T.M., Brosh R.M. Jr. J. Biol. Chem. 278:23487-23496(2003) [PubMed: 12704184] [Abstract] Cited for: INTERACTION WITH EXO1.
[9]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1058 AND SER-1141, MASS SPECTROMETRY.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453 AND SER-467, MASS SPECTROMETRY.
[11]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[12]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1133, MASS SPECTROMETRY.
[13]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426; SER-467 AND SER-1133, MASS SPECTROMETRY. Tissue: T-cell.
[14]	"Solution structure of a multifunctional DNA- and protein-binding motif of human Werner syndrome protein." Hu J.S., Feng H., Zeng W., Lin G.X., Xi X.G. Proc. Natl. Acad. Sci. U.S.A. 102:18379-18384(2005) [PubMed: 16339893] [Abstract] Cited for: STRUCTURE BY NMR OF 949-1092.
[15]	"WRN exonuclease structure and molecular mechanism imply an editing role in DNA end processing." Perry J.J., Yannone S.M., Holden L.G., Hitomi C., Asaithamby A., Han S., Cooper P.K., Chen D.J., Tainer J.A. Nat. Struct. Mol. Biol. 13:414-422(2006) [PubMed: 16622405] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 38-236.
[16]	"WRN mutations in Werner syndrome." Moser M.J., Oshima J., Monnat R.J. Jr. Hum. Mutat. 13:271-279(1999) [PubMed: 10220139] [Abstract] Cited for: REVIEW ON VARIANTS.
[17]	"Solution structure of the helicase and RNAse D C-terminal domain in Werner syndrome ATP-dependent helicase." RIKEN structural genomics initiative (RSGI) Submitted (SEP-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1140-1239.
[18]	"Association of a polymorphic variant of the Werner helicase gene with myocardial infarction in a Japanese population." Ye L., Miki T., Nakura J., Oshima J., Kamino K., Rakugi H., Ikegami H., Higaki J., Edland S.D., Martin G.M., Ogihara T. Am. J. Med. Genet. 68:494-498(1997) [PubMed: 9021029] [Abstract] Cited for: VARIANT ARG-1367.
[19]	Erratum Ye L., Miki T., Nakura J., Oshima J., Kamino K., Rakugi H., Ikegami H., Higaki J., Edland S.D., Martin G.M., Ogihara T. Am. J. Med. Genet. 70:103-103(1997)
[20]	"Werner syndrome: characterization of mutations in the WRN gene in an affected family." Meisslitzer C., Ruppitsch W., Weirich-Schwaiger H., Weirich H.G., Jabkowsky J., Klein G., Schweiger M., Hirsch-Kauffmann M. Eur. J. Hum. Genet. 5:364-370(1997) [PubMed: 9450180] [Abstract] Cited for: VARIANTS ILE-387 AND LEU-1074.
[21]	"The 1396del A mutation and a missense mutation or a rare polymorphism of the WRN gene detected in a French Werner family with a severe phenotype and a case of an unusual vulvar cancer." Vidal V., Bay J.-O., Champomier F., Grancho M., Beauville L., Glowaczower C., Lemery D., Ferrara M., Bignon Y.-J. Hum. Mutat. 11:413-414(1998) [PubMed: 10206685] [Abstract] Cited for: VARIANT ILE-387.
[22]	"Polymorphisms at the Werner locus: I. Newly identified polymorphisms, ethnic variability of 1367Cys/Arg, and its stability in a population of Finnish centenarians." Castro E., Ogburn C.E., Hunt K.E., Tilvis R., Louhija J., Penttinen R., Erkkola R., Panduro A., Riestra R., Piussan C., Deeb S.S., Wang L., Edland S.D., Martin G.M., Oshima J. Am. J. Med. Genet. 82:399-403(1999) [PubMed: 10069711] [Abstract] Cited for: VARIANTS ALA-324 AND ARG-1367.
[23]	"The Werner syndrome gene and global sequence variation." Passarino G., Shen P., Van Kirk J.B., Lin A.A., De Benedictis G., Cavalli-Sforza L.L., Oefner P.J., Underhill P.A. Genomics 71:118-122(2001) [PubMed: 11161804] [Abstract] Cited for: VARIANTS ARG-32; ILE-114; PRO-172; LYS-240; TRP-383; ILE-387; LEU-724; LEU-1074; GLU-1269 AND ARG-1367.
[24]	"The spectrum of WRN mutations in Werner syndrome patients." Huang S., Lee L., Hanson N.B., Lenaerts C., Hoehn H., Poot M., Rubin C.D., Chen D.-F., Yang C.-C., Juch H., Dorn T., Spiegel R., Oral E.A., Abid M., Battisti C., Lucci-Cordisco E., Neri G., Steed E.H. Oshima J. Hum. Mutat. 27:558-567(2006) [PubMed: 16673358] [Abstract] Cited for: VARIANTS WRN ASN-125 AND GLU-135.
[25]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-92.
[26]	"DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome." Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K., Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L., Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A., Abbott S. Wilson R.K. Nature 456:66-72(2008) [PubMed: 18987736] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-1141.
+	Additional computationally mapped references.

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Web resources

WRN

WRN mutation db (Warner disease)

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

NIEHS-SNPs

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L76937 Genomic DNA. Translation: AAC41981.1.
AF091214 mRNA. Translation: AAC63361.1.
AF181897, AF181896 Genomic DNA. Translation: AAF06162.1.
AY818673 mRNA. Translation: AAX21098.1.
AY442327 Genomic DNA. Translation: AAR05448.1.

IPI

IPI00029107.

RefSeq

NP_000544.2.

UniGene

Hs.632050

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AXL	NMR	-	A	949-1092	[»]
2DGZ	NMR	-	A	1140-1239	[»]
2E1E	X-ray	2.30	A	1142-1242	[»]
2E1F	X-ray	2.00	A	1142-1242	[»]
2FBT	X-ray	2.05	A	38-236	[»]
2FBV	X-ray	2.40	A	38-236	[»]
2FBX	X-ray	2.20	A	38-236	[»]
2FBY	X-ray	2.00	A	38-236	[»]
2FC0	X-ray	2.00	A	38-236	[»]

SMR

Q14191. Positions 538-1053.

DisProt

DP00443.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q14191. 13 interactions.

STRING

Q14191.

PTM databases

PhosphoSite

Q14191.

Proteomic databases

PRIDE

Q14191.

Genome annotation databases

Ensembl

ENST00000298139; ENSP00000298139; ENSG00000165392; Homo sapiens. [Genome view]

GeneID

7486.

KEGG

hsa:7486.

Organism-specific databases

CTD

7486.

GeneCards

GC08P031010.
GC08P031011.

H-InvDB

HIX0007441.

HGNC

HGNC:12791. WRN.

MIM

114500. phenotype.
277700. phenotype.
604611. gene.

Orphanet

902. Werner syndrome.

PharmGKB

PA367.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG15288.

HOGENOM

HBG447065.

HOVERGEN

Q14191.

InParanoid

Q14191.

PhylomeDB

Q14191.

Enzyme and pathway databases

Pathway_Interaction_DB

telomerasepathway. Regulation of Telomerase.

Gene expression databases

ArrayExpress

Q14191.

Bgee

Q14191.

CleanEx

HS_WRN.

Genevestigator

Q14191.

GermOnline

ENSG00000165392. Homo sapiens.

Family and domain databases

InterPro

IPR002562. 3_5_exonuclease.
IPR014001. DEAD-like_N.
IPR001650. DNA/RNA_helicase_C.
IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR004589. DNA_helicase_ATP-dep_RecQ.
IPR018329. DNA_helicase_ATP-dep_RecQ_N.
IPR002121. Helicase/RNaseD_C.
IPR014021. Helicase_SF1/SF2_ATP-bd.
IPR012337. PolynucTfrase_RNaseH_fold.
IPR018982. RQC_domain.
[Graphical view]

PANTHER

PTHR13710. RecQ. 1 hit.

Pfam

PF01612. 3_5_exonuc. 1 hit.
PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00570. HRDC. 1 hit.
PF09382. RQC. 1 hit.
[Graphical view]

SMART

SM00474. 35EXOc. 1 hit.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00341. HRDC. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00614. recQ_fam. 1 hit.

PROSITE

PS00690. DEAH_ATP_HELICASE. False negative.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50967. HRDC. 1 hit.
[Graphical view]

ProtoNet

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Other Resources

NextBio

29326.

SOURCE

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Entry information

Entry name

WRN_HUMAN

Accession

Primary (citable) accession number: Q14191
Secondary accession number(s): A1KYY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	February 9, 2010
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.

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