|
|
1)
|
chain |
A |
residue |
93 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN A 1329
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
212 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 1329
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
255 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 1329
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
91 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE TLA A 1330
|
source |
: AC2
|
|
5)
|
chain |
A |
residue |
93 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE TLA A 1330
|
source |
: AC2
|
|
6)
|
chain |
A |
residue |
94 |
type |
|
sequence |
Q
|
description |
BINDING SITE FOR RESIDUE TLA A 1330
|
source |
: AC2
|
|
7)
|
chain |
A |
residue |
97 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE TLA A 1330
|
source |
: AC2
|
|
8)
|
chain |
A |
residue |
212 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE TLA A 1330
|
source |
: AC2
|
|
9)
|
chain |
A |
residue |
255 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE TLA A 1330
|
source |
: AC2
|
|
10)
|
chain |
A |
residue |
256 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE TLA A 1330
|
source |
: AC2
|
|
11)
|
chain |
A |
residue |
57 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE 939 A 1331
|
source |
: AC3
|
|
12)
|
chain |
A |
residue |
59 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE 939 A 1331
|
source |
: AC3
|
|
13)
|
chain |
A |
residue |
67 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE 939 A 1331
|
source |
: AC3
|
|
14)
|
chain |
A |
residue |
80 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE 939 A 1331
|
source |
: AC3
|
|
15)
|
chain |
A |
residue |
82 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE 939 A 1331
|
source |
: AC3
|
|
16)
|
chain |
A |
residue |
131 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE 939 A 1331
|
source |
: AC3
|
|
17)
|
chain |
A |
residue |
132 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE 939 A 1331
|
source |
: AC3
|
|
18)
|
chain |
A |
residue |
133 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE 939 A 1331
|
source |
: AC3
|
|
19)
|
chain |
A |
residue |
134 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE 939 A 1331
|
source |
: AC3
|
|
20)
|
chain |
A |
residue |
136 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE 939 A 1331
|
source |
: AC3
|
|
21)
|
chain |
A |
residue |
137 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE 939 A 1331
|
source |
: AC3
|
|
22)
|
chain |
A |
residue |
140 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE 939 A 1331
|
source |
: AC3
|
|
23)
|
chain |
A |
residue |
180 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE 939 A 1331
|
source |
: AC3
|
|
24)
|
chain |
A |
residue |
183 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE 939 A 1331
|
source |
: AC3
|
|
25)
|
chain |
A |
residue |
194 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE 939 A 1331
|
source |
: AC3
|
|
26)
|
chain |
A |
residue |
59-82 |
type |
prosite |
sequence |
LGKGGFAKCFEISDADTKEVFAGK
|
description |
PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGGFAKCFeIsdadtkev..........FAGK
|
source |
prosite : PS00107
|
|
27)
|
chain |
A |
residue |
172-184 |
type |
prosite |
sequence |
VIHRDLKLGNLFL
|
description |
PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDLKlgNLFL
|
source |
prosite : PS00108
|
|
28)
|
chain |
A |
residue |
176 |
type |
ACT_SITE |
sequence |
D
|
description |
Proton acceptor => ECO:0000269|PubMed:18615013
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
29)
|
chain |
A |
residue |
59 |
type |
BINDING |
sequence |
L
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
30)
|
chain |
A |
residue |
82 |
type |
BINDING |
sequence |
K
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
31)
|
chain |
A |
residue |
131 |
type |
BINDING |
sequence |
E
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
32)
|
chain |
A |
residue |
178 |
type |
BINDING |
sequence |
K
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
33)
|
chain |
A |
residue |
194 |
type |
BINDING |
sequence |
D
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
34)
|
chain |
A |
residue |
103 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:18691976
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
35)
|
chain |
A |
residue |
137 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0000305|PubMed:12207013
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
36)
|
chain |
A |
residue |
210 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine; by AURKA => ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:18477460, ECO:0000269|PubMed:18615013, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
37)
|
chain |
A |
residue |
214 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
38)
|
chain |
A |
residue |
269 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine; by autocatalysis => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI7
|
|