|
|
1)
|
chain |
A |
residue |
377 |
type |
|
sequence |
L
|
description |
binding site for residue X7G A 701
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
400 |
type |
|
sequence |
A
|
description |
binding site for residue X7G A 701
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
448 |
type |
|
sequence |
M
|
description |
binding site for residue X7G A 701
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
449 |
type |
|
sequence |
E
|
description |
binding site for residue X7G A 701
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
450 |
type |
|
sequence |
M
|
description |
binding site for residue X7G A 701
|
source |
: AC1
|
|
6)
|
chain |
A |
residue |
451 |
type |
|
sequence |
A
|
description |
binding site for residue X7G A 701
|
source |
: AC1
|
|
7)
|
chain |
A |
residue |
454 |
type |
|
sequence |
G
|
description |
binding site for residue X7G A 701
|
source |
: AC1
|
|
8)
|
chain |
A |
residue |
455 |
type |
|
sequence |
P
|
description |
binding site for residue X7G A 701
|
source |
: AC1
|
|
9)
|
chain |
A |
residue |
498 |
type |
|
sequence |
R
|
description |
binding site for residue X7G A 701
|
source |
: AC1
|
|
10)
|
chain |
A |
residue |
499 |
type |
|
sequence |
N
|
description |
binding site for residue X7G A 701
|
source |
: AC1
|
|
11)
|
chain |
A |
residue |
501 |
type |
|
sequence |
L
|
description |
binding site for residue X7G A 701
|
source |
: AC1
|
|
12)
|
chain |
A |
residue |
512 |
type |
|
sequence |
D
|
description |
binding site for residue X7G A 701
|
source |
: AC1
|
|
13)
|
chain |
A |
residue |
377-402 |
type |
prosite |
sequence |
LGTVKKGYYQMKKVVKTVAVK
|
description |
PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGNFGTVKkGyyqmkkvvkt........VAVK
|
source |
prosite : PS00107
|
|
14)
|
chain |
A |
residue |
490-502 |
type |
prosite |
sequence |
FVHRDLAARNVLL
|
description |
PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNVLL
|
source |
prosite : PS00109
|
|
15)
|
chain |
A |
residue |
494 |
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 |
377 |
type |
BINDING |
sequence |
L
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
17)
|
chain |
A |
residue |
402 |
type |
BINDING |
sequence |
K
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
18)
|
chain |
A |
residue |
364 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000269|PubMed:21469132
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
19)
|
chain |
A |
residue |
484 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000269|PubMed:21469132
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
20)
|
chain |
A |
residue |
507 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000269|PubMed:21469132
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
21)
|
chain |
A |
residue |
526 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000269|PubMed:21469132
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
22)
|
chain |
A |
residue |
629 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000269|PubMed:21469132
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
23)
|
chain |
A |
residue |
631 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000269|PubMed:21469132
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
24)
|
chain |
A |
residue |
579 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0000269|PubMed:21469132
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
25)
|
chain |
A |
residue |
384 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine => ECO:0000269|PubMed:21469132
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
26)
|
chain |
A |
residue |
530 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine => ECO:0000269|PubMed:21469132
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
27)
|
chain |
A |
residue |
582 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine => ECO:0000269|PubMed:21469132
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
28)
|
chain |
A |
residue |
525 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:21469132
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
29)
|
chain |
A |
residue |
546 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000250|UniProtKB:P48025
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
30)
|
chain |
A |
residue |
630 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000269|PubMed:18369315, ECO:0000269|PubMed:21469132
|
source |
Swiss-Prot : SWS_FT_FI8
|
|