|
|
1)
|
chain |
A |
residue |
1084 |
type |
|
sequence |
I
|
description |
BINDING SITE FOR RESIDUE 0JJ A 1401
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
1108 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE 0JJ A 1401
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
1158 |
type |
|
sequence |
P
|
description |
BINDING SITE FOR RESIDUE 0JJ A 1401
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
1160 |
type |
|
sequence |
M
|
description |
BINDING SITE FOR RESIDUE 0JJ A 1401
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
1164 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE 0JJ A 1401
|
source |
: AC1
|
|
6)
|
chain |
A |
residue |
1208 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE 0JJ A 1401
|
source |
: AC1
|
|
7)
|
chain |
A |
residue |
1211 |
type |
|
sequence |
M
|
description |
BINDING SITE FOR RESIDUE 0JJ A 1401
|
source |
: AC1
|
|
8)
|
chain |
A |
residue |
1221 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE 0JJ A 1401
|
source |
: AC1
|
|
9)
|
chain |
A |
residue |
1222 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE 0JJ A 1401
|
source |
: AC1
|
|
10)
|
chain |
A |
residue |
1226 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE 0JJ A 1401
|
source |
: AC1
|
|
11)
|
chain |
A |
residue |
1230 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE 0JJ A 1401
|
source |
: AC1
|
|
12)
|
chain |
A |
residue |
1289 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine => ECO:0007744|PubMed:19369195
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
13)
|
chain |
A |
residue |
1234 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
14)
|
chain |
A |
residue |
1235 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:1655790
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
15)
|
chain |
A |
residue |
1204 |
type |
ACT_SITE |
sequence |
D
|
description |
Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
16)
|
chain |
A |
residue |
1084 |
type |
BINDING |
sequence |
I
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
17)
|
chain |
A |
residue |
1110 |
type |
BINDING |
sequence |
K
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
18)
|
chain |
A |
residue |
1230 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000269|PubMed:12475979
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
19)
|
chain |
A |
residue |
1084-1110 |
type |
prosite |
sequence |
IGRGHFGCVYHGTLKIHCAVK
|
description |
PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGHFGCVYhGtlldndgkkih.......CAVK
|
source |
prosite : PS00107
|
|
20)
|
chain |
A |
residue |
1200-1212 |
type |
prosite |
sequence |
FVHRDLAARNCML
|
description |
PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCML
|
source |
prosite : PS00109
|
|