|
|
1)
|
chain |
A |
residue |
248 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE 627 A 1504
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
250 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE 627 A 1504
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
269 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE 627 A 1504
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
271 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE 627 A 1504
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
316 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE 627 A 1504
|
source |
: AC1
|
|
6)
|
chain |
A |
residue |
317 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE 627 A 1504
|
source |
: AC1
|
|
7)
|
chain |
A |
residue |
318 |
type |
|
sequence |
M
|
description |
BINDING SITE FOR RESIDUE 627 A 1504
|
source |
: AC1
|
|
8)
|
chain |
A |
residue |
319 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE 627 A 1504
|
source |
: AC1
|
|
9)
|
chain |
A |
residue |
321 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE 627 A 1504
|
source |
: AC1
|
|
10)
|
chain |
A |
residue |
367 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE 627 A 1504
|
source |
: AC1
|
|
11)
|
chain |
A |
residue |
370 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE 627 A 1504
|
source |
: AC1
|
|
12)
|
chain |
A |
residue |
368 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE MG A 1505
|
source |
: AC3
|
|
13)
|
chain |
A |
residue |
381 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE MG A 1505
|
source |
: AC3
|
|
14)
|
chain |
A |
residue |
248-271 |
type |
prosite |
sequence |
LGGGQYGEVYEGVWKKYSLTVAVK
|
description |
PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGGGQYGEVYeGvwkkyslt..........VAVK
|
source |
prosite : PS00107
|
|
15)
|
chain |
A |
residue |
359-371 |
type |
prosite |
sequence |
FIHRDLAARNCLV
|
description |
PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FIHrDLAARNCLV
|
source |
prosite : PS00109
|
|
16)
|
chain |
A |
residue |
363 |
type |
ACT_SITE |
sequence |
D
|
description |
Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
17)
|
chain |
A |
residue |
248 |
type |
BINDING |
sequence |
L
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
18)
|
chain |
A |
residue |
271 |
type |
BINDING |
sequence |
K
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
19)
|
chain |
A |
residue |
316 |
type |
BINDING |
sequence |
E
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
20)
|
chain |
A |
residue |
253 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
21)
|
chain |
A |
residue |
257 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
22)
|
chain |
A |
residue |
413 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
23)
|
chain |
A |
residue |
393 |
type |
MOD_RES |
sequence |
X
|
description |
Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases => ECO:0000269|PubMed:16912036
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
24)
|
chain |
A |
residue |
446 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0000250|UniProtKB:P00520
|
source |
Swiss-Prot : SWS_FT_FI6
|
|