|
|
1)
|
chain |
A |
residue |
132 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE IOD A 601
|
source |
: AC1
|
|
2)
|
chain |
C |
residue |
468 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE IOD C 602
|
source |
: AC2
|
|
3)
|
chain |
C |
residue |
470 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE IOD C 602
|
source |
: AC2
|
|
4)
|
chain |
D |
residue |
325 |
type |
|
sequence |
P
|
description |
BINDING SITE FOR RESIDUE IOD D 604
|
source |
: AC4
|
|
5)
|
chain |
A |
residue |
114 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE IOD A 607
|
source |
: AC6
|
|
6)
|
chain |
A |
residue |
102 |
type |
|
sequence |
Q
|
description |
BINDING SITE FOR RESIDUE IOD B 608
|
source |
: AC7
|
|
7)
|
chain |
B |
residue |
98 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE IOD B 608
|
source |
: AC7
|
|
8)
|
chain |
C |
residue |
466 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE IOD C 610
|
source |
: AC9
|
|
9)
|
chain |
D |
residue |
268 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE IOD C 610
|
source |
: AC9
|
|
10)
|
chain |
C |
residue |
364 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE IOD C 611
|
source |
: BC1
|
|
11)
|
chain |
C |
residue |
325 |
type |
|
sequence |
P
|
description |
BINDING SITE FOR RESIDUE IOD C 613
|
source |
: BC2
|
|
12)
|
chain |
A |
residue |
119 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE IOD A 614
|
source |
: BC3
|
|
13)
|
chain |
A |
residue |
120 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE IOD B 615
|
source |
: BC4
|
|
14)
|
chain |
B |
residue |
119 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE IOD B 615
|
source |
: BC4
|
|
15)
|
chain |
D |
residue |
399 |
type |
|
sequence |
M
|
description |
BINDING SITE FOR RESIDUE IOD D 619
|
source |
: BC7
|
|
16)
|
chain |
A |
residue |
134 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE IOD A 620
|
source |
: BC8
|
|
17)
|
chain |
D |
residue |
364 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE IOD D 621
|
source |
: BC9
|
|
18)
|
chain |
D |
residue |
265 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE IOD D 622
|
source |
: CC1
|
|
19)
|
chain |
C |
residue |
444 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE IOD C 623
|
source |
: CC2
|
|
20)
|
chain |
C |
residue |
347 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE IOD D 625
|
source |
: CC4
|
|
21)
|
chain |
D |
residue |
400 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE IOD D 625
|
source |
: CC4
|
|
22)
|
chain |
C |
residue |
514 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE IOD C 627
|
source |
: CC5
|
|
23)
|
chain |
D |
residue |
323 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE IOD D 628
|
source |
: CC6
|
|
24)
|
chain |
D |
residue |
324 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE IOD D 628
|
source |
: CC6
|
|
25)
|
chain |
C |
residue |
385-397 |
type |
prosite |
sequence |
VIHRDIKSDNILL
|
description |
PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKsdNILL
|
source |
prosite : PS00108
|
|
26)
|
chain |
C |
residue |
389 |
type |
ACT_SITE |
sequence |
D
|
description |
Proton acceptor => ECO:0000269|PubMed:22153498
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
27)
|
chain |
D |
residue |
389 |
type |
ACT_SITE |
sequence |
D
|
description |
Proton acceptor => ECO:0000269|PubMed:22153498
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
28)
|
chain |
C |
residue |
276 |
type |
BINDING |
sequence |
I
|
description |
BINDING => ECO:0000269|PubMed:22153498
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
29)
|
chain |
C |
residue |
299 |
type |
BINDING |
sequence |
R
|
description |
BINDING => ECO:0000269|PubMed:22153498
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
30)
|
chain |
C |
residue |
345 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000269|PubMed:22153498
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
31)
|
chain |
D |
residue |
276 |
type |
BINDING |
sequence |
I
|
description |
BINDING => ECO:0000269|PubMed:22153498
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
32)
|
chain |
D |
residue |
299 |
type |
BINDING |
sequence |
R
|
description |
BINDING => ECO:0000269|PubMed:22153498
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
33)
|
chain |
D |
residue |
345 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000269|PubMed:22153498
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
34)
|
chain |
C |
residue |
285 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine; by JAK2 => ECO:0000269|PubMed:17726028, ECO:0000269|PubMed:17989089
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
35)
|
chain |
D |
residue |
285 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine; by JAK2 => ECO:0000269|PubMed:17726028, ECO:0000269|PubMed:17989089
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
36)
|
chain |
B |
residue |
131 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine; by JAK2 => ECO:0000269|PubMed:17726028, ECO:0000269|PubMed:17989089
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
37)
|
chain |
B |
residue |
142 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine; by JAK2 => ECO:0000269|PubMed:17726028, ECO:0000269|PubMed:17989089
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
38)
|
chain |
C |
residue |
423 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine; by autocatalysis, BRSK2 and PDPK1 => ECO:0000269|PubMed:10551809, ECO:0000269|PubMed:10995762, ECO:0000269|PubMed:22153498, ECO:0000269|PubMed:22669945
|
source |
Swiss-Prot : SWS_FT_FI4
|
|