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Protein Page:
WRN (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

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: Cell cycle regulation; Helicase; EC 3.6.4.12; EC 3.6.1.-; EC 3.1.-.-; DNA repair, damage; DNA binding protein
Cellular Component: nucleoplasm; MutLalpha complex; centrosome; nucleolus
Molecular Function: G-quadruplex DNA binding; protein homodimerization activity; ATPase activity; magnesium ion binding; 3'-5' DNA helicase activity; bubble DNA binding; helicase activity; ATP-dependent DNA helicase activity; four-way junction helicase activity; Y-form DNA binding; DNA helicase activity; protein binding; ATP-dependent 3'-5' DNA helicase activity; DNA binding; 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; multicellular organismal aging; cell 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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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 K241-u VQRFAINkEEEILLS
0 1 S294 DISENLYSLRRMIIG
1 0 S319-p SNNLNLLsFEDSTTG
1 0 K366-a GEDVLGNkVERKEDG
0 1 K366-u GEDVLGNkVERKEDG
0 1 F374 VERKEDGFEDGVEDN
0 1 K382-u EDGVEDNkLKENMER
0 2 S409-p LQILEQQsQEEYLSD
0 2 S426-p YKSTEHLsPNDNEND
1 5 S440-p DTSYVIEsDEDLEME
0 2 S453-p MEMLKHLsPNDNEND
1 5 S467-p DTSYVIEsDEDLEME
0 1 S478-p LEMEMLKsLENLNSG
1 0 K496-s PTHSKCLkMERNLGL
1 0 K887-a LTEIRNEkFRLYKLK
0 1 S968-p PQAFKLLsAVDILGE
0 1 S1058-p LHKANTEsQSLILQA
0 2 S1078 PKKLLLPSsKTVSSG
0 3 S1079-p KKLLLPSsKTVSSGT
0 6 S1083 LPSsKTVSSGTKEHC
1 0 K1117-a YSYKPCDkISSGSNI
1 0 K1127-a SGSNISKkSIMVQsP
0 5 S1133-p KkSIMVQsPEKAYSS
1 1 S1141-p PEKAYSSsQPVISAQ
0 17 G1377 NKRRCFPGsEEICSS
0 2 S1378-p KRRCFPGsEEICSSS
1 0 K1389-a CSSSKRSkEEVGINT
0 1 S1400-p GINTETSsAERKRRL
1 0 K1413-a RLPVWFAkGSDTSKK
  mouse

 
K235 AQVFALNKAEENLPL
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
K852 LIEIHDEKFRLYKLK
S933 PQAFQLLSAVDILQE
S1023 LGEASSQSPPSLLLQ
S1044-p PRKVLLPssNPVsPE
S1045-p RKVLLPssNPVsPET
S1049-p LPssNPVsPETTQHS
K1082 HSYKVPEKVSSGTNI
K1092 SGTNIPKKSAVMPSP
S1098 KKSAVMPSPGTSSSP
L1106 PGTSSSPLEPAISAQ
S1342-p SRKRRFPssAESCES
S1343-p RKRRFPssAESCESC
K1354 CESCKESKEAVTETK
S1364 VTETKASSSESKRKL
K1377-a KLPEWFAkGNVPSAD
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