|
|
1)
|
chain |
A |
residue |
13 |
type |
|
sequence |
V
|
description |
binding site for residue R34 A 601
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
20 |
type |
|
sequence |
L
|
description |
binding site for residue R34 A 601
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
31 |
type |
|
sequence |
K
|
description |
binding site for residue R34 A 601
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
33 |
type |
|
sequence |
K
|
description |
binding site for residue R34 A 601
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
50 |
type |
|
sequence |
N
|
description |
binding site for residue R34 A 601
|
source |
: AC1
|
|
6)
|
chain |
A |
residue |
53 |
type |
|
sequence |
K
|
description |
binding site for residue R34 A 601
|
source |
: AC1
|
|
7)
|
chain |
A |
residue |
90 |
type |
|
sequence |
D
|
description |
binding site for residue R34 A 601
|
source |
: AC1
|
|
8)
|
chain |
B |
residue |
83 |
type |
|
sequence |
R
|
description |
binding site for residue R34 A 601
|
source |
: AC1
|
|
9)
|
chain |
B |
residue |
106 |
type |
|
sequence |
T
|
description |
binding site for residue R34 A 601
|
source |
: AC1
|
|
10)
|
chain |
B |
residue |
108 |
type |
|
sequence |
D
|
description |
binding site for residue R34 A 601
|
source |
: AC1
|
|
11)
|
chain |
B |
residue |
113 |
type |
|
sequence |
V
|
description |
binding site for residue R34 A 601
|
source |
: AC1
|
|
12)
|
chain |
B |
residue |
115 |
type |
|
sequence |
I
|
description |
binding site for residue R34 A 601
|
source |
: AC1
|
|
13)
|
chain |
A |
residue |
24 |
type |
|
sequence |
L
|
description |
binding site for residue STU A 602
|
source |
: AC2
|
|
14)
|
chain |
A |
residue |
25 |
type |
|
sequence |
G
|
description |
binding site for residue STU A 602
|
source |
: AC2
|
|
15)
|
chain |
A |
residue |
26 |
type |
|
sequence |
V
|
description |
binding site for residue STU A 602
|
source |
: AC2
|
|
16)
|
chain |
A |
residue |
27 |
type |
|
sequence |
G
|
description |
binding site for residue STU A 602
|
source |
: AC2
|
|
17)
|
chain |
A |
residue |
45 |
type |
|
sequence |
A
|
description |
binding site for residue STU A 602
|
source |
: AC2
|
|
18)
|
chain |
A |
residue |
95 |
type |
|
sequence |
M
|
description |
binding site for residue STU A 602
|
source |
: AC2
|
|
19)
|
chain |
A |
residue |
96 |
type |
|
sequence |
E
|
description |
binding site for residue STU A 602
|
source |
: AC2
|
|
20)
|
chain |
A |
residue |
97 |
type |
|
sequence |
Y
|
description |
binding site for residue STU A 602
|
source |
: AC2
|
|
21)
|
chain |
A |
residue |
98 |
type |
|
sequence |
V
|
description |
binding site for residue STU A 602
|
source |
: AC2
|
|
22)
|
chain |
A |
residue |
102 |
type |
|
sequence |
E
|
description |
binding site for residue STU A 602
|
source |
: AC2
|
|
23)
|
chain |
A |
residue |
145 |
type |
|
sequence |
E
|
description |
binding site for residue STU A 602
|
source |
: AC2
|
|
24)
|
chain |
A |
residue |
146 |
type |
|
sequence |
N
|
description |
binding site for residue STU A 602
|
source |
: AC2
|
|
25)
|
chain |
A |
residue |
148 |
type |
|
sequence |
L
|
description |
binding site for residue STU A 602
|
source |
: AC2
|
|
26)
|
chain |
A |
residue |
159 |
type |
|
sequence |
D
|
description |
binding site for residue STU A 602
|
source |
: AC2
|
|
27)
|
chain |
C |
residue |
150 |
type |
|
sequence |
H
|
description |
binding site for residue AMP C 401
|
source |
: AC3
|
|
28)
|
chain |
C |
residue |
199 |
type |
|
sequence |
T
|
description |
binding site for residue AMP C 401
|
source |
: AC3
|
|
29)
|
chain |
C |
residue |
203 |
type |
|
sequence |
I
|
description |
binding site for residue AMP C 401
|
source |
: AC3
|
|
30)
|
chain |
C |
residue |
204 |
type |
|
sequence |
A
|
description |
binding site for residue AMP C 401
|
source |
: AC3
|
|
31)
|
chain |
C |
residue |
224 |
type |
|
sequence |
V
|
description |
binding site for residue AMP C 401
|
source |
: AC3
|
|
32)
|
chain |
C |
residue |
225 |
type |
|
sequence |
S
|
description |
binding site for residue AMP C 401
|
source |
: AC3
|
|
33)
|
chain |
C |
residue |
226 |
type |
|
sequence |
A
|
description |
binding site for residue AMP C 401
|
source |
: AC3
|
|
34)
|
chain |
C |
residue |
228 |
type |
|
sequence |
P
|
description |
binding site for residue AMP C 401
|
source |
: AC3
|
|
35)
|
chain |
C |
residue |
311 |
type |
|
sequence |
I
|
description |
binding site for residue AMP C 401
|
source |
: AC3
|
|
36)
|
chain |
C |
residue |
313 |
type |
|
sequence |
S
|
description |
binding site for residue AMP C 401
|
source |
: AC3
|
|
37)
|
chain |
C |
residue |
315 |
type |
|
sequence |
S
|
description |
binding site for residue AMP C 401
|
source |
: AC3
|
|
38)
|
chain |
C |
residue |
316 |
type |
|
sequence |
D
|
description |
binding site for residue AMP C 401
|
source |
: AC3
|
|
39)
|
chain |
A |
residue |
24-47 |
type |
prosite |
sequence |
LGVGTFGKVKVGKHELTGHKVAVK
|
description |
PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGVGTFGKVKvGkheltghk..........VAVK
|
source |
prosite : PS00107
|
|
40)
|
chain |
A |
residue |
137-149 |
type |
prosite |
sequence |
VVHRDLKPENVLL
|
description |
PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvHrDLKpeNVLL
|
source |
prosite : PS00108
|
|
41)
|
chain |
C |
residue |
69 |
type |
BINDING |
sequence |
R
|
description |
BINDING => ECO:0000250|UniProtKB:P80385
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
42)
|
chain |
C |
residue |
84 |
type |
BINDING |
sequence |
M
|
description |
BINDING => ECO:0000250|UniProtKB:P80385
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
43)
|
chain |
C |
residue |
129 |
type |
BINDING |
sequence |
V
|
description |
BINDING => ECO:0000250|UniProtKB:P80385
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
44)
|
chain |
C |
residue |
151 |
type |
BINDING |
sequence |
R
|
description |
BINDING => ECO:0000250|UniProtKB:P80385
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
45)
|
chain |
C |
residue |
169 |
type |
BINDING |
sequence |
K
|
description |
BINDING => ECO:0000250|UniProtKB:P80385
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
46)
|
chain |
C |
residue |
241 |
type |
BINDING |
sequence |
S
|
description |
BINDING => ECO:0000250|UniProtKB:P80385
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
47)
|
chain |
C |
residue |
268 |
type |
BINDING |
sequence |
R
|
description |
BINDING => ECO:0000250|UniProtKB:P80385
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
48)
|
chain |
C |
residue |
276 |
type |
BINDING |
sequence |
L
|
description |
BINDING => ECO:0000250|UniProtKB:P80385
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
49)
|
chain |
A |
residue |
458 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:19369195
|
source |
Swiss-Prot : SWS_FT_FI12
|
|
50)
|
chain |
A |
residue |
531 |
type |
MOD_RES |
sequence |
G
|
description |
Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI13
|
|
51)
|
chain |
A |
residue |
535 |
type |
MOD_RES |
sequence |
I
|
description |
Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI14
|
|
52)
|
chain |
A |
residue |
541 |
type |
MOD_RES |
sequence |
C
|
description |
Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
|
source |
Swiss-Prot : SWS_FT_FI15
|
|
53)
|
chain |
C |
residue |
150 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000269|PubMed:17452784, ECO:0000269|PubMed:24352254, ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFF
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
54)
|
chain |
C |
residue |
199 |
type |
BINDING |
sequence |
T
|
description |
BINDING => ECO:0000269|PubMed:17452784, ECO:0000269|PubMed:24352254, ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFF
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
55)
|
chain |
C |
residue |
204 |
type |
BINDING |
sequence |
A
|
description |
BINDING => ECO:0000269|PubMed:17452784, ECO:0000269|PubMed:24352254, ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFF
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
56)
|
chain |
C |
residue |
225 |
type |
BINDING |
sequence |
S
|
description |
BINDING => ECO:0000269|PubMed:17452784, ECO:0000269|PubMed:24352254, ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFF
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
57)
|
chain |
C |
residue |
297 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000269|PubMed:17452784, ECO:0000269|PubMed:24352254, ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFF
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
58)
|
chain |
C |
residue |
313 |
type |
BINDING |
sequence |
S
|
description |
BINDING => ECO:0000269|PubMed:17452784, ECO:0000269|PubMed:24352254, ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFF
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
59)
|
chain |
C |
residue |
260 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine; by ULK1 => ECO:0000250|UniProtKB:P80385
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
60)
|
chain |
C |
residue |
269 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine; by ULK1 => ECO:0000250|UniProtKB:P80385
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
61)
|
chain |
C |
residue |
262 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine; by ULK1 => ECO:0000250|UniProtKB:P80385
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
62)
|
chain |
B |
residue |
171 |
type |
MOD_RES |
sequence |
Q
|
description |
Phosphoserine => ECO:0000250|UniProtKB:Q9R078
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
63)
|
chain |
A |
residue |
533 |
type |
MOD_RES |
sequence |
H
|
description |
Phosphoserine => ECO:0000250|UniProtKB:Q9R078
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
64)
|
chain |
A |
residue |
359 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine; by ULK1 => ECO:0000250|UniProtKB:P54645
|
source |
Swiss-Prot : SWS_FT_FI9
|
|