|
|
1)
|
chain |
A |
residue |
408 |
type |
|
sequence |
L
|
description |
binding site for residue GJJ A 701
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
428 |
type |
|
sequence |
A
|
description |
binding site for residue GJJ A 701
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
474 |
type |
|
sequence |
T
|
description |
binding site for residue GJJ A 701
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
475 |
type |
|
sequence |
E
|
description |
binding site for residue GJJ A 701
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
476 |
type |
|
sequence |
Y
|
description |
binding site for residue GJJ A 701
|
source |
: AC1
|
|
6)
|
chain |
A |
residue |
477 |
type |
|
sequence |
M
|
description |
binding site for residue GJJ A 701
|
source |
: AC1
|
|
7)
|
chain |
A |
residue |
478 |
type |
|
sequence |
A
|
description |
binding site for residue GJJ A 701
|
source |
: AC1
|
|
8)
|
chain |
A |
residue |
480 |
type |
|
sequence |
G
|
description |
binding site for residue GJJ A 701
|
source |
: AC1
|
|
9)
|
chain |
A |
residue |
481 |
type |
|
sequence |
C
|
description |
binding site for residue GJJ A 701
|
source |
: AC1
|
|
10)
|
chain |
A |
residue |
484 |
type |
|
sequence |
N
|
description |
binding site for residue GJJ A 701
|
source |
: AC1
|
|
11)
|
chain |
A |
residue |
525 |
type |
|
sequence |
R
|
description |
binding site for residue GJJ A 701
|
source |
: AC1
|
|
12)
|
chain |
A |
residue |
528 |
type |
|
sequence |
L
|
description |
binding site for residue GJJ A 701
|
source |
: AC1
|
|
13)
|
chain |
A |
residue |
403 |
type |
|
sequence |
T
|
description |
binding site for residue DMS A 702
|
source |
: AC2
|
|
14)
|
chain |
A |
residue |
404 |
type |
|
sequence |
F
|
description |
binding site for residue DMS A 702
|
source |
: AC2
|
|
15)
|
chain |
A |
residue |
631 |
type |
|
sequence |
Y
|
description |
binding site for residue DMS A 702
|
source |
: AC2
|
|
16)
|
chain |
A |
residue |
408-430 |
type |
prosite |
sequence |
LVVKYGKWRGQYDVAIK
|
description |
PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGQFGVVKyGkwrgqyd...........VAIK
|
source |
prosite : PS00107
|
|
17)
|
chain |
A |
residue |
517-529 |
type |
prosite |
sequence |
FLHRDLAARNCLV
|
description |
PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FLHrDLAARNCLV
|
source |
prosite : PS00109
|
|
18)
|
chain |
A |
residue |
487 |
type |
ACT_SITE |
sequence |
R
|
description |
Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
19)
|
chain |
A |
residue |
396 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
20)
|
chain |
A |
residue |
440 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000269|PubMed:20052711, ECO:0007744|PDB:3K54, ECO:0007744|PDB:3OCT
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
21)
|
chain |
A |
residue |
508 |
type |
BINDING |
sequence |
A
|
description |
BINDING => ECO:0000269|PubMed:21280133, ECO:0007744|PDB:3PIY
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
22)
|
chain |
A |
residue |
517 |
type |
MOD_RES |
sequence |
F
|
description |
Phosphotyrosine; by LYN and SYK => ECO:0000269|PubMed:8630736, ECO:0000269|PubMed:9012831
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
23)
|
chain |
A |
residue |
570 |
type |
MOD_RES |
sequence |
M
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
24)
|
chain |
A |
residue |
583 |
type |
MOD_RES |
sequence |
F
|
description |
Phosphotyrosine => ECO:0000269|PubMed:15375214
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
25)
|
chain |
A |
residue |
589 |
type |
MOD_RES |
sequence |
E
|
description |
Phosphoserine => ECO:0000269|PubMed:15375214
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
26)
|
chain |
A |
residue |
625 |
type |
MOD_RES |
sequence |
K
|
description |
Phosphoserine => ECO:0007744|PubMed:19369195
|
source |
Swiss-Prot : SWS_FT_FI9
|
|