|
|
1)
|
chain |
I |
residue |
3 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE IOD I 384
|
source |
: AC1
|
|
2)
|
chain |
I |
residue |
3 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE IOD I 385
|
source |
: AC2
|
|
3)
|
chain |
E |
residue |
1 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE MYR E 0
|
source |
: AC3
|
|
4)
|
chain |
E |
residue |
14 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE MYR E 0
|
source |
: AC3
|
|
5)
|
chain |
E |
residue |
18 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE MYR E 0
|
source |
: AC3
|
|
6)
|
chain |
E |
residue |
100 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE MYR E 0
|
source |
: AC3
|
|
7)
|
chain |
E |
residue |
152 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE MYR E 0
|
source |
: AC3
|
|
8)
|
chain |
E |
residue |
156 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE MYR E 0
|
source |
: AC3
|
|
9)
|
chain |
E |
residue |
303 |
type |
|
sequence |
I
|
description |
BINDING SITE FOR RESIDUE MYR E 0
|
source |
: AC3
|
|
10)
|
chain |
E |
residue |
306 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE MYR E 0
|
source |
: AC3
|
|
11)
|
chain |
E |
residue |
51 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
12)
|
chain |
E |
residue |
84 |
type |
|
sequence |
Q
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
13)
|
chain |
E |
residue |
87 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
14)
|
chain |
E |
residue |
127 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
15)
|
chain |
E |
residue |
129 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
16)
|
chain |
E |
residue |
133 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
17)
|
chain |
E |
residue |
168 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
18)
|
chain |
E |
residue |
169 |
type |
|
sequence |
P
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
19)
|
chain |
E |
residue |
170 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
20)
|
chain |
E |
residue |
187 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
21)
|
chain |
E |
residue |
197 |
type |
|
sequence |
X
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
22)
|
chain |
E |
residue |
198 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
23)
|
chain |
E |
residue |
199 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
24)
|
chain |
E |
residue |
200 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
25)
|
chain |
E |
residue |
201 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
26)
|
chain |
E |
residue |
202 |
type |
|
sequence |
P
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
27)
|
chain |
E |
residue |
203 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
28)
|
chain |
E |
residue |
204 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
29)
|
chain |
E |
residue |
230 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
30)
|
chain |
E |
residue |
235 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
31)
|
chain |
E |
residue |
239 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
32)
|
chain |
E |
residue |
240 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
33)
|
chain |
E |
residue |
241 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
34)
|
chain |
E |
residue |
241 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
35)
|
chain |
E |
residue |
246 |
type |
|
sequence |
I
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
36)
|
chain |
E |
residue |
247 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
37)
|
chain |
E |
residue |
321 |
type |
|
sequence |
P
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
38)
|
chain |
E |
residue |
322 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
39)
|
chain |
E |
residue |
326 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
40)
|
chain |
E |
residue |
327 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
41)
|
chain |
E |
residue |
328 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
42)
|
chain |
E |
residue |
329 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
43)
|
chain |
E |
residue |
330 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM
|
source |
: AC4
|
|
44)
|
chain |
E |
residue |
167 |
type |
catalytic |
sequence |
L
|
description |
757
|
source |
MCSA : MCSA1
|
|
45)
|
chain |
E |
residue |
169 |
type |
catalytic |
sequence |
P
|
description |
757
|
source |
MCSA : MCSA1
|
|
46)
|
chain |
E |
residue |
172 |
type |
catalytic |
sequence |
L
|
description |
757
|
source |
MCSA : MCSA1
|
|
47)
|
chain |
E |
residue |
185 |
type |
catalytic |
sequence |
F
|
description |
757
|
source |
MCSA : MCSA1
|
|
48)
|
chain |
E |
residue |
202 |
type |
catalytic |
sequence |
P
|
description |
757
|
source |
MCSA : MCSA1
|
|
49)
|
chain |
E |
residue |
2 |
type |
LIPID |
sequence |
N
|
description |
N-myristoyl glycine => ECO:0000269|PubMed:6262777
|
source |
Swiss-Prot : SWS_FT_FI11
|
|
50)
|
chain |
E |
residue |
166 |
type |
ACT_SITE |
sequence |
D
|
description |
Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
|
source |
Swiss-Prot : SWS_FT_FI12
|
|
51)
|
chain |
E |
residue |
2 |
type |
MOD_RES |
sequence |
N
|
description |
Deamidated asparagine; partial => ECO:0000269|PubMed:10684253, ECO:0000269|PubMed:9521123
|
source |
Swiss-Prot : SWS_FT_FI13
|
|
52)
|
chain |
E |
residue |
197 |
type |
MOD_RES |
sequence |
X
|
description |
Phosphothreonine; by PDPK1 => ECO:0000250|UniProtKB:P00517
|
source |
Swiss-Prot : SWS_FT_FI14
|
|
53)
|
chain |
E |
residue |
338 |
type |
MOD_RES |
sequence |
X
|
description |
Phosphoserine => ECO:0000250|UniProtKB:P00517
|
source |
Swiss-Prot : SWS_FT_FI15
|
|
54)
|
chain |
E |
residue |
1 |
type |
LIPID |
sequence |
G
|
description |
N-myristoyl glycine => ECO:0000269|PubMed:9521123
|
source |
Swiss-Prot : SWS_FT_FI16
|
|
55)
|
chain |
I |
residue |
14 |
type |
SITE |
sequence |
R
|
description |
Important for inhibition => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
56)
|
chain |
I |
residue |
15 |
type |
SITE |
sequence |
R
|
description |
Important for inhibition => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
57)
|
chain |
I |
residue |
11 |
type |
SITE |
sequence |
R
|
description |
Important for inhibition => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
58)
|
chain |
E |
residue |
50 |
type |
BINDING |
sequence |
G
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
59)
|
chain |
E |
residue |
73 |
type |
BINDING |
sequence |
I
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
60)
|
chain |
E |
residue |
49 |
type |
BINDING |
sequence |
L
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
61)
|
chain |
E |
residue |
72 |
type |
BINDING |
sequence |
K
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
62)
|
chain |
E |
residue |
122 |
type |
BINDING |
sequence |
Y
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
63)
|
chain |
E |
residue |
169 |
type |
BINDING |
sequence |
P
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
64)
|
chain |
E |
residue |
121 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
65)
|
chain |
E |
residue |
168 |
type |
BINDING |
sequence |
K
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
66)
|
chain |
E |
residue |
3 |
type |
MOD_RES |
sequence |
A
|
description |
Deamidated asparagine; partial => ECO:0000269|PubMed:10684253, ECO:0000269|PubMed:11152138, ECO:0000269|PubMed:9521123
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
67)
|
chain |
E |
residue |
11 |
type |
MOD_RES |
sequence |
E
|
description |
Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P05132
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
68)
|
chain |
E |
residue |
10 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P05132
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
69)
|
chain |
E |
residue |
49 |
type |
MOD_RES |
sequence |
L
|
description |
Phosphothreonine => ECO:0000250|UniProtKB:P17612
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
70)
|
chain |
E |
residue |
196 |
type |
MOD_RES |
sequence |
W
|
description |
Phosphothreonine => ECO:0000250|UniProtKB:P17612
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
71)
|
chain |
E |
residue |
48 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine => ECO:0000250|UniProtKB:P17612
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
72)
|
chain |
E |
residue |
195 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine => ECO:0000250|UniProtKB:P17612
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
73)
|
chain |
E |
residue |
140 |
type |
MOD_RES |
sequence |
E
|
description |
Phosphoserine => ECO:0000250|UniProtKB:P05132
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
74)
|
chain |
E |
residue |
139 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0000250|UniProtKB:P05132
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
75)
|
chain |
E |
residue |
198 |
type |
MOD_RES |
sequence |
L
|
description |
Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:6262777
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
76)
|
chain |
E |
residue |
331 |
type |
MOD_RES |
sequence |
E
|
description |
Phosphotyrosine => ECO:0000250|UniProtKB:P05132
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
77)
|
chain |
E |
residue |
330 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000250|UniProtKB:P05132
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
78)
|
chain |
E |
residue |
339 |
type |
MOD_RES |
sequence |
I
|
description |
Phosphoserine => ECO:0000269|PubMed:6262777
|
source |
Swiss-Prot : SWS_FT_FI10
|
|
79)
|
chain |
E |
residue |
49-72 |
type |
prosite |
sequence |
LGTGSFGRVMLVKHKETGNHFAMK
|
description |
PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhketgnh..........FAMK
|
source |
prosite : PS00107
|
|
80)
|
chain |
E |
residue |
162-174 |
type |
prosite |
sequence |
LIYRDLKPENLLI
|
description |
PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLLI
|
source |
prosite : PS00108
|
|