|
|
1)
|
chain |
A |
residue |
137 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE L0D A 1391
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
160 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE L0D A 1391
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
211 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE L0D A 1391
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
212 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE L0D A 1391
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
213 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE L0D A 1391
|
source |
: AC1
|
|
6)
|
chain |
A |
residue |
214 |
type |
|
sequence |
P
|
description |
BINDING SITE FOR RESIDUE L0D A 1391
|
source |
: AC1
|
|
7)
|
chain |
A |
residue |
216 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE L0D A 1391
|
source |
: AC1
|
|
8)
|
chain |
A |
residue |
263 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE L0D A 1391
|
source |
: AC1
|
|
9)
|
chain |
A |
residue |
139-162 |
type |
prosite |
sequence |
LGKGKFGNVYLAREKQSKFILALK
|
description |
PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGKFGNVYlArekqskfi..........LALK
|
source |
prosite : PS00107
|
|
10)
|
chain |
A |
residue |
252-264 |
type |
prosite |
sequence |
VIHRDIKPENLLL
|
description |
PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKpeNLLL
|
source |
prosite : PS00108
|
|
11)
|
chain |
A |
residue |
256 |
type |
ACT_SITE |
sequence |
D
|
description |
Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027, ECO:0000269|PubMed:14580337
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
12)
|
chain |
A |
residue |
143 |
type |
BINDING |
sequence |
K
|
description |
BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
13)
|
chain |
A |
residue |
162 |
type |
BINDING |
sequence |
K
|
description |
BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
14)
|
chain |
A |
residue |
211 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
15)
|
chain |
A |
residue |
260 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
16)
|
chain |
A |
residue |
274 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
17)
|
chain |
A |
residue |
342 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine; by PKA and PAK => ECO:0000269|PubMed:16246726
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
18)
|
chain |
A |
residue |
258 |
type |
CROSSLNK |
sequence |
K
|
description |
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
|
source |
Swiss-Prot : SWS_FT_FI6
|
|