|
|
1)
|
chain |
A |
residue |
191 |
type |
|
sequence |
P
|
description |
BINDING SITE FOR RESIDUE 3NE A 361
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
192 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE 3NE A 361
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
195 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE 3NE A 361
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
197 |
type |
|
sequence |
W
|
description |
BINDING SITE FOR RESIDUE 3NE A 361
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
246 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE 3NE A 361
|
source |
: AC1
|
|
6)
|
chain |
A |
residue |
249 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE 3NE A 361
|
source |
: AC1
|
|
7)
|
chain |
A |
residue |
250 |
type |
|
sequence |
I
|
description |
BINDING SITE FOR RESIDUE 3NE A 361
|
source |
: AC1
|
|
8)
|
chain |
A |
residue |
251 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE 3NE A 361
|
source |
: AC1
|
|
9)
|
chain |
A |
residue |
252 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE 3NE A 361
|
source |
: AC1
|
|
10)
|
chain |
A |
residue |
259 |
type |
|
sequence |
I
|
description |
BINDING SITE FOR RESIDUE 3NE A 361
|
source |
: AC1
|
|
11)
|
chain |
A |
residue |
291 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE 3NE A 361
|
source |
: AC1
|
|
12)
|
chain |
A |
residue |
336 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE 3NE A 361
|
source |
: AC1
|
|
13)
|
chain |
A |
residue |
30-54 |
type |
prosite |
sequence |
VGSGAYGSVCAAFDTKTGLRVAVKK
|
description |
PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGSGAYGSVCaAfdtktglrv.........AVKK
|
source |
prosite : PS00107
|
|
14)
|
chain |
A |
residue |
59-162 |
type |
prosite |
sequence |
FQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEE
FNDVYLVTHLMGADLNNIVKCLTDDHVQFLIYQILRGLKY
IHSADIIHRDLKPSNLAVNEDS
|
description |
MAPK MAP kinase signature. FqsiihakrtyRElrllkhmkhenviglldvftparsleefndvylvthlmgadlnnivkcqkltddhvqfliyqilrglkyihsadiih.........RDlKpsnlavnedS
|
source |
prosite : PS01351
|
|
15)
|
chain |
A |
residue |
168 |
type |
ACT_SITE |
sequence |
D
|
description |
Proton acceptor
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
16)
|
chain |
A |
residue |
30 |
type |
BINDING |
sequence |
V
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
17)
|
chain |
A |
residue |
53 |
type |
BINDING |
sequence |
K
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
18)
|
chain |
A |
residue |
16 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine => ECO:0007744|PubMed:18691976
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
19)
|
chain |
A |
residue |
53 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0000269|PubMed:21444723
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
20)
|
chain |
A |
residue |
152 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0000269|PubMed:21444723
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
21)
|
chain |
A |
residue |
263 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine => ECO:0007744|PubMed:17525332
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
22)
|
chain |
A |
residue |
323 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine; by ZAP70 => ECO:0000269|PubMed:15735648
|
source |
Swiss-Prot : SWS_FT_FI9
|
|