|
|
1)
|
chain |
A |
residue |
158 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE MG A 401
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
171 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE MG A 401
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
171 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE MG A 402
|
source |
: AC2
|
|
4)
|
chain |
A |
residue |
41 |
type |
|
sequence |
V
|
description |
BINDING SITE FOR RESIDUE ANP A 400
|
source |
: AC5
|
|
5)
|
chain |
A |
residue |
54 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE ANP A 400
|
source |
: AC5
|
|
6)
|
chain |
A |
residue |
56 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE ANP A 400
|
source |
: AC5
|
|
7)
|
chain |
A |
residue |
87 |
type |
|
sequence |
I
|
description |
BINDING SITE FOR RESIDUE ANP A 400
|
source |
: AC5
|
|
8)
|
chain |
A |
residue |
109 |
type |
|
sequence |
M
|
description |
BINDING SITE FOR RESIDUE ANP A 400
|
source |
: AC5
|
|
9)
|
chain |
A |
residue |
110 |
type |
|
sequence |
P
|
description |
BINDING SITE FOR RESIDUE ANP A 400
|
source |
: AC5
|
|
10)
|
chain |
A |
residue |
112 |
type |
|
sequence |
M
|
description |
BINDING SITE FOR RESIDUE ANP A 400
|
source |
: AC5
|
|
11)
|
chain |
A |
residue |
115 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE ANP A 400
|
source |
: AC5
|
|
12)
|
chain |
A |
residue |
155 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE ANP A 400
|
source |
: AC5
|
|
13)
|
chain |
A |
residue |
157 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE ANP A 400
|
source |
: AC5
|
|
14)
|
chain |
A |
residue |
158 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE ANP A 400
|
source |
: AC5
|
|
15)
|
chain |
A |
residue |
170 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE ANP A 400
|
source |
: AC5
|
|
16)
|
chain |
A |
residue |
171 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE ANP A 400
|
source |
: AC5
|
|
17)
|
chain |
A |
residue |
153 |
type |
ACT_SITE |
sequence |
D
|
description |
Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
18)
|
chain |
A |
residue |
33 |
type |
BINDING |
sequence |
V
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
19)
|
chain |
A |
residue |
56 |
type |
BINDING |
sequence |
K
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
20)
|
chain |
A |
residue |
183 |
type |
MOD_RES |
sequence |
X
|
description |
Phosphothreonine; by MAP2K3 and MAP2K6 => ECO:0000250|UniProtKB:Q63538
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
21)
|
chain |
A |
residue |
185 |
type |
MOD_RES |
sequence |
X
|
description |
Phosphotyrosine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
22)
|
chain |
A |
residue |
33-57 |
type |
prosite |
sequence |
VAVCSAVDGRTGAKVAIKK
|
description |
PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGSGAYGAVCsAvdgrtgakv.........AIKK
|
source |
prosite : PS00107
|
|
23)
|
chain |
A |
residue |
62-165 |
type |
prosite |
sequence |
FQSELFAKRAYRELRLLKHMRHENVIGLLDVFTPDETLDD
FTDFYLVMPFMGTDLGKLMKHEKLGEDRIQFLVYQMLKGL
RYIHAAGIIHRDLKPGNLAVNEDC
|
description |
MAPK MAP kinase signature. FqselfakrayRElrllkhmrhenviglldvftpdetlddftdfylvmpfmgtdlgklmkheklgedriqflvyqmlkglryihaagiih.........RDlKpgnlavnedC
|
source |
prosite : PS01351
|
|