|
|
1)
|
chain |
A |
residue |
381 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 1436
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
384 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 1436
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
401 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 1436
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
404 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 1436
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
396 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 1437
|
source |
: AC2
|
|
6)
|
chain |
A |
residue |
398 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN A 1437
|
source |
: AC2
|
|
7)
|
chain |
A |
residue |
416 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 1437
|
source |
: AC2
|
|
8)
|
chain |
A |
residue |
419 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 1437
|
source |
: AC2
|
|
9)
|
chain |
A |
residue |
229 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE CA A 1438
|
source |
: AC3
|
|
10)
|
chain |
A |
residue |
231 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE CA A 1438
|
source |
: AC3
|
|
11)
|
chain |
A |
residue |
233 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE CA A 1438
|
source |
: AC3
|
|
12)
|
chain |
A |
residue |
235 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE CA A 1438
|
source |
: AC3
|
|
13)
|
chain |
A |
residue |
240 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE CA A 1438
|
source |
: AC3
|
|
14)
|
chain |
C |
residue |
74-89 |
type |
prosite |
sequence |
YHPNINSNGSICLDIL
|
description |
UBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNInsn.GsICLdiL
|
source |
prosite : PS00183
|
|
15)
|
chain |
A |
residue |
396-405 |
type |
prosite |
sequence |
CGHLMCTSCL
|
description |
ZF_RING_1 Zinc finger RING-type signature. CgHlMCtsCL
|
source |
prosite : PS00518
|
|
16)
|
chain |
C |
residue |
85 |
type |
ACT_SITE |
sequence |
C
|
description |
Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
17)
|
chain |
B |
residue |
7 |
type |
MOD_RES |
sequence |
X
|
description |
Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
18)
|
chain |
A |
residue |
231 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
19)
|
chain |
A |
residue |
233 |
type |
MOD_RES |
sequence |
N
|
description |
Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
20)
|
chain |
A |
residue |
235 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
21)
|
chain |
A |
residue |
240 |
type |
MOD_RES |
sequence |
E
|
description |
Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
22)
|
chain |
A |
residue |
294 |
type |
BINDING |
sequence |
R
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
23)
|
chain |
A |
residue |
371 |
type |
MOD_RES |
sequence |
X
|
description |
Phosphotyrosine; by INSR => ECO:0000269|PubMed:11997497
|
source |
Swiss-Prot : SWS_FT_FI4
|
|