|
|
1)
|
chain |
A |
residue |
1011 |
type |
|
sequence |
W
|
description |
BINDING SITE FOR RESIDUE PHU A 1201
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
1030 |
type |
|
sequence |
P
|
description |
BINDING SITE FOR RESIDUE PHU A 1201
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
1059 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE PHU A 1201
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
1060 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE PHU A 1201
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
1078 |
type |
|
sequence |
W
|
description |
BINDING SITE FOR RESIDUE PHU A 1201
|
source |
: AC1
|
|
6)
|
chain |
A |
residue |
828 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE 933 A 1202
|
source |
: AC2
|
|
7)
|
chain |
A |
residue |
829 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE 933 A 1202
|
source |
: AC2
|
|
8)
|
chain |
A |
residue |
853 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE 933 A 1202
|
source |
: AC2
|
|
9)
|
chain |
A |
residue |
903 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE 933 A 1202
|
source |
: AC2
|
|
10)
|
chain |
A |
residue |
904 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE 933 A 1202
|
source |
: AC2
|
|
11)
|
chain |
A |
residue |
905 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE 933 A 1202
|
source |
: AC2
|
|
12)
|
chain |
A |
residue |
954 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE 933 A 1202
|
source |
: AC2
|
|
13)
|
chain |
A |
residue |
956 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE 933 A 1202
|
source |
: AC2
|
|
14)
|
chain |
A |
residue |
980 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15831699
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
15)
|
chain |
A |
residue |
981 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15831699
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
16)
|
chain |
A |
residue |
949 |
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 |
828 |
type |
BINDING |
sequence |
L
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
18)
|
chain |
A |
residue |
855 |
type |
BINDING |
sequence |
K
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
19)
|
chain |
A |
residue |
904 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000269|PubMed:18250158
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
20)
|
chain |
A |
residue |
939 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000269|PubMed:18250158
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
21)
|
chain |
A |
residue |
828-855 |
type |
prosite |
sequence |
LGKGNFGSVELCRYDPLGDNTGALVAVK
|
description |
PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGNFGSVElCrydplgdntgal......VAVK
|
source |
prosite : PS00107
|
|
22)
|
chain |
A |
residue |
945-957 |
type |
prosite |
sequence |
CVHRDLAARNILV
|
description |
PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CVHrDLAARNILV
|
source |
prosite : PS00109
|
|