Sequence Browser (Q14191-1)

UniProt (Ref Seq)
Displayed Structure
Experimental Tertiary/Complex (PDB:XRay/EM)
Experimental Tertiary/Complex (PDB:NMR)
Modelled Tertiary (Phyre)
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1
1432
Isoform
Remark
Ref
Q14191-1  
Click on Isoform of interest to be redirected to the corresponding page
Type
Variation
Position
sequence variant
G → V
92
sequence variant
K → N
125
sequence variant
T → P
172
sequence variant
T → A
324
sequence variant
E → K
343
sequence variant
L → W
383
sequence variant
N → S
533
sequence variant
S → F
708
sequence variant
Q → L
724
sequence variant
I → S
912
sequence variant
S → L
1079
sequence variant
S → L
1141
sequence variant
V → I
1339
mutagenesis site
E → A
84
mutagenesis site
W → A
145
mutagenesis site
R → A
987
mutagenesis site
R → A
993
mutagenesis site
F → A
1037
sequence variant
K → R
32
sequence variant
V → I
114
sequence variant
K → E
135
sequence variant
N → K
240
sequence variant
Q → R
329
sequence variant
L → F
383
sequence variant
M → I
387
sequence variant
S → C
612
sequence variant
R → W
711
sequence variant
R → C
834
sequence variant
L → F
1074
sequence variant
S → A
1133
sequence variant
K → E
1269
sequence variant
C → R
1367
mutagenesis site
L → A
88
mutagenesis site
Y → F
212
mutagenesis site
S → A
989
mutagenesis site
R → E
993
mutagenesis site
M → A
1038

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Protein:
Other Names:
DNA helicase, RecQ-like type 3, Exonuclease WRN, RecQ protein-like 2
Primary Accession:
Other Accessions:
A1KYY9
Gene :
WRN*, synonyms (RECQ3, RECQL2)
Organism :
Human
Entry Name :
Length :
1,432
Mass (Da) :
162,461
Last modified :
08-Jan-2011
Version :
v2
Isoforms :
1 
Variants :
37 
Interactions :
10 
Structures :
Experimental 10 | Phyre prediction 6

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.

With
Entry
IntAct
Exp
BLM
P54132
EBI-368417, EBI-621372
9
FEN1
P39748
EBI-368417, EBI-707816
9
RAD52
P43351
EBI-368417, EBI-706448
9
SIRT1
Q96EB6
EBI-368417, EBI-1802965
9
TP53
P04637
EBI-368417, EBI-366083
5
CBX5
P45973
EBI-368417, EBI-78219
3
PARP1
P09874
EBI-368417, EBI-355676
8
RPA1
P27694
EBI-368417, EBI-621389
9
TERF2
Q15554
EBI-368417, EBI-706637
8
XRCC6
P12956
EBI-368417, EBI-353208
5