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Protein Page:
WRN (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
WRN 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. 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 EXO1, PCNA and SUPV3L1. Belongs to the helicase family. RecQ subfamily. Note: This description may include information from UniProtKB.
Protein type: DNA repair, damage; EC 3.6.4.12; EC 3.1.-.-; Nucleolus; DNA binding protein; Helicase; EC 3.6.1.-; Cell cycle regulation
Cellular Component: MutLalpha complex; nucleoplasm; centrosome; nucleolus
Molecular Function: G-quadruplex DNA binding; protein homodimerization activity; ATPase activity; 3'-5' DNA helicase activity; magnesium ion binding; bubble DNA binding; helicase activity; ATP-dependent DNA helicase activity; four-way junction helicase activity; Y-form DNA binding; protein binding; DNA helicase activity; DNA binding; ATP-dependent 3'-5' DNA helicase activity; manganese ion binding; exonuclease activity; protein complex binding; 3'-5' exonuclease activity; ATP binding
Biological Process: ATP catabolic process; nucleolus to nucleoplasm transport; positive regulation of hydrolase activity; cell aging; multicellular organismal aging; replicative cell aging; cellular response to starvation; DNA duplex unwinding; response to UV-C; replication fork processing; DNA recombination; regulation of apoptosis; DNA synthesis during DNA repair; base-excision repair; double-strand break repair; regulation of growth rate; response to oxidative stress; DNA replication; telomere maintenance; DNA metabolic process; response to DNA damage stimulus; aging
Reference #:  Q14191 (UniProtKB)
Alt. Names/Synonyms: DKFZp686C2056; DNA helicase, RecQ-like type 3; RecQ protein-like 2; RECQ3; RECQL2; RECQL3; Werner syndrome ATP-dependent helicase; Werner syndrome, RecQ helicase-like; WRN
Gene Symbols: WRN
Molecular weight: 162,461 Da
Basal Isoelectric point: 5.96  Predict pI for various phosphorylation states
Select Structure to View Below

WRN

Protein Structure Not Found.


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Sites Implicated In
DNA repair, induced: S440‑p, S467‑p
intracellular localization: S440‑p, S467‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K32-ac RCAVEERkACVRKSV
0 1 K241-ub VQRFAINkEEEILLs
0 1 S248-p kEEEILLsDMNKQLT
0 1 S294 DISENLYSLRRMIIG
1 0 S319-p SNNLNLLsFEDSTTG
1 0 K366-ac GEDVLGNkVERKEDG
0 1 K366-ub GEDVLGNkVERKEDG
0 1 F374 VERKEDGFEDGVEDN
0 1 K382-ub EDGVEDNkLKENMER
0 3 S409-p LQILEQQsQEEYLSD
0 4 S426-p YKSTEHLsPNDNEND
1 8 S440-p DTSYVIEsDEDLEME
0 4 S453-p MEMLKHLsPNDNEND
1 7 S467-p DTSYVIEsDEDLEME
0 2 S478-p LEMEMLKsLENLNSG
1 0 K496-sm PTHSKCLkMERNLGL
0 1 S689-p DSFRKLGsLKtALPM
0 1 T692-p RKLGsLKtALPMVPI
0 1 T777-p YCPSRKMtQQVTGEL
0 1 S790-p ELRKLNLsCGTYHAG
0 1 S801-p YHAGMSFsTRKDIHH
0 1 Y849-p PKDMESYyQEIGRAG
1 0 K887-ac LTEIRNEkFRLYKLK
0 1 S968-p PQAFKLLsAVDILGE
0 1 S1058-p LHKANTEsQSLILQA
0 2 S1078 PKKLLLPSsKTVSsG
0 3 S1079-p KKLLLPSsKTVSsGT
0 7 S1083 LPSsKTVSsGTKEHC
0 1 S1084-p PSsKTVSsGTKEHCY
0 1 T1086 sKTVSsGTKEHCYNQ
0 1 K1087 KTVSsGTKEHCYNQV
0 1 Y1091 sGTKEHCYNQVPVEL
0 1 T1100-p QVPVELStEKKSNLE
0 3 Y1110-p KSNLEKLysyKPCDk
0 2 S1111-p SNLEKLysyKPCDkI
0 1 Y1112-p NLEKLysyKPCDkIS
1 0 K1117-ac ysyKPCDkISSGSNI
1 0 K1127-ac SGSNISKksIMVQsP
0 1 S1128-p GSNISKksIMVQsPE
0 8 S1133-p KksIMVQsPEKAYSS
1 1 S1141-p PEKAYSSsQPVISAQ
0 1 K1189-ub KILVDMAkMRPTTVE
0 1 S1205-p VKRIDGVsEGKAAML
0 1 K1270-ub YSLFQEKkMPLkSIA
0 1 K1274-ac QEKkMPLkSIAESRI
0 17 G1377 NKRRCFPGsEEICSS
0 2 S1378-p KRRCFPGsEEICSSS
1 0 K1389-ac CSSSKRSkEEVGINT
0 1 E1397 EEVGINTETSsAERK
0 2 S1400-p GINTETSsAERKRRL
0 1 K1404 ETSsAERKRRLPVWF
1 0 K1413-ac RLPVWFAkGSDTSKK
  mouse

 
K26 QRCATEEKACVQKSV
K235 AQVFALNKAEENLPL
L242 KAEENLPLEMKKQLN
S288-p SISENLCsLRKVICG
S313 GSSFNLLSSEDSAAA
Q360 EVDVFRNQVKQEKGE
Q360 EVDVFRNQVKQEKGE
S368-p VKQEKGEsENEIEDN
L376 ENEIEDNLLREDMER
A402 LQDLEQQAKEEKYND
S419 HQLSEHLSPNDDEND
S433 DSSYIIESDEDLEME
- gap
- gap
S444 LEMEMLKSLENLNSD
E462 PTHSTWLEMGTNGRL
S653 SSFRMLGSLKTALPL
T656 RMLGSLKTALPLVPV
T742 YCPSRKMTEQVTAEL
A755 ELGKLNLACRTYHAG
S766 YHAGMKISERKDVHH
Y814 PKEMESYYQEIGRAG
K852 LIEIHDEKFRLYKLK
S933 PQAFQLLSAVDILQE
S1023 LGEASSQSPPSLLLQ
S1044-p PRKVLLPssNPVsPE
S1045-p RKVLLPssNPVsPEt
S1049-p LPssNPVsPEttQHS
P1050 PssNPVsPEttQHSs
T1052-p sNPVsPEttQHSsNQ
T1053-p NPVsPEttQHSsNQN
S1057-p PEttQHSsNQNPAGL
T1066 QNPAGLTTKQSNLER
H1075 QSNLERTHSYKVPEK
S1076 SNLERTHSYKVPEKV
Y1077 NLERTHSYKVPEKVS
K1082 HSYKVPEKVSSGTNI
K1092 SGTNIPKKSAVMPSP
S1093 GTNIPKKSAVMPSPG
S1098 KKSAVMPSPGTSSSP
L1106 PGTSSSPLEPAISAQ
K1154 KVLLDMAKMRPTTVE
S1170 MKQIDGVSEGKAALL
K1235 YTLFQEKKMPLHSIA
H1239 QEKKMPLHSIAENRL
S1342-p SRKRRFPssAESCES
S1343-p RKRRFPssAESCESC
K1354 CESCKESKEAVTETk
K1361-ac KEAVTETkASSSESk
S1364 VTETkASSSESkRKL
K1368-ac kASSSESkRKLPEWF
K1377-ac KLPEWFAkGNVPSAD
  rat

 
K26 KSCATQEKASIQKSV
K235 VQVFALNKAEESLPM
M242 KAEESLPMEMKKQLN
S288 NISENLCSLRKVICA
S313 GGGSHLLSSEGSAAV
Q360 AVDVFRKQVKQEKGG
Q360 AVDVFRKQVKQEKGG
F368 VKQEKGGFEDEMEDS
L376 EDEMEDSLLREVMER
A402 LQDLEQQAKEEKHNA
S419 HQFSEHLSPDDDEKD
S433-p DSSYIIEsDEDLEME
- gap
- gap
S444 LEMEMLKSLENLNSD
E462 PTHSKWLETGGSVNL
S653 SSFRTLGSLKTALPL
T656 RTLGSLKTALPLVPV
T742 YCPSRKVTEQVTVEL
A755 ELGKLNVACQAYHAG
S766 YHAGMKISERKDIHH
Y814 PKEMESYYQEIGRAG
K852 LIEIHNEKFRLHKLK
S933 PQAFQLLSAVDILQE
S1023 LGEAILQSPPSLVLQ
S1044 SRKALLSSSNPVSSE
S1045 RKALLSSSNPVSSET
S1049 LSSSNPVSSETKPHS
S1050 SSSNPVSSETKPHSS
T1052 SNPVSSETKPHSSNQ
K1053 NPVSSETKPHSSNQK
S1057 SETKPHSSNQKPTGS
T1066 QKPTGSSTQQSNLEG
Y1075 QSNLEGAYSDKVPEK
S1076 SNLEGAYSDKVPEKF
D1077 NLEGAYSDKVPEKFS
K1082 YSDKVPEKFSSGSNI
K1092 SGSNIPKKSVVMQSP
S1093 GSNIPKKSVVMQSPG
S1098 KKSVVMQSPGTSYSS
W1106 PGTSYSSWEPVISAQ
K1154 KVLLDMAKMRPTTVE
S1170 VKQIDGVSEGKAALL
K1235 YALFQEKKMSLHSIA
H1239 QEKKMSLHSIAENRL
S1342 NRKRCLPSPAESCGS
P1343 RKRCLPSPAESCGSF
K1354 CGSFKKSKEMVTETK
K1361 KEMVTETKAPSEMSQ
S1364 VTETKAPSEMSQRKL
Q1368 KAPSEMSQRKLPEWF
K1377 KLPEWFVKGNVPLAA
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