eF-site ID 2xew-ABCDEFGHIJKL
PDB Code 2xew
Chain A, B, C, D, E, F, G, H, I, J, K, L

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Title Crystal structure of K11-linked diubiquitin
Classification CELL CYCLE
Compound UBIQUITIN
Source (UBIQ_HUMAN)
Sequence A:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG
B:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG
C:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLR
D:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG
E:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG
F:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG
G:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG
H:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG
I:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG
J:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG
K:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG
L:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLR
Description


Functional site
1) chain A
residue 70
type
sequence V
description BINDING SITE FOR RESIDUE EDO A 1077
source : AC1
2) chain A
residue 71
type
sequence L
description BINDING SITE FOR RESIDUE EDO A 1077
source : AC1
3) chain G
residue 7
type
sequence T
description BINDING SITE FOR RESIDUE EDO A 1077
source : AC1
4) chain G
residue 9
type
sequence T
description BINDING SITE FOR RESIDUE EDO A 1077
source : AC1
5) chain G
residue 11
type
sequence K
description BINDING SITE FOR RESIDUE EDO A 1077
source : AC1
6) chain A
residue 7
type
sequence T
description BINDING SITE FOR RESIDUE EDO A 1078
source : AC2
7) chain A
residue 9
type
sequence T
description BINDING SITE FOR RESIDUE EDO A 1078
source : AC2
8) chain A
residue 11
type
sequence K
description BINDING SITE FOR RESIDUE EDO A 1078
source : AC2
9) chain G
residue 70
type
sequence V
description BINDING SITE FOR RESIDUE EDO A 1078
source : AC2
10) chain G
residue 71
type
sequence L
description BINDING SITE FOR RESIDUE EDO A 1078
source : AC2
11) chain A
residue 45
type
sequence F
description BINDING SITE FOR RESIDUE EDO A 1079
source : AC3
12) chain A
residue 65
type
sequence S
description BINDING SITE FOR RESIDUE EDO A 1079
source : AC3
13) chain A
residue 66
type
sequence T
description BINDING SITE FOR RESIDUE EDO A 1079
source : AC3
14) chain K
residue 44
type
sequence I
description BINDING SITE FOR RESIDUE EDO A 1079
source : AC3
15) chain K
residue 45
type
sequence F
description BINDING SITE FOR RESIDUE EDO A 1079
source : AC3
16) chain K
residue 46
type
sequence A
description BINDING SITE FOR RESIDUE EDO A 1079
source : AC3
17) chain K
residue 47
type
sequence G
description BINDING SITE FOR RESIDUE EDO A 1079
source : AC3
18) chain K
residue 68
type
sequence H
description BINDING SITE FOR RESIDUE EDO A 1079
source : AC3
19) chain A
residue 16
type
sequence E
description BINDING SITE FOR RESIDUE CL A 1080
source : AC4
20) chain A
residue 33
type
sequence K
description BINDING SITE FOR RESIDUE CL A 1080
source : AC4
21) chain B
residue 70
type
sequence V
description BINDING SITE FOR RESIDUE EDO B 1077
source : AC5
22) chain B
residue 71
type
sequence L
description BINDING SITE FOR RESIDUE EDO B 1077
source : AC5
23) chain F
residue 7
type
sequence T
description BINDING SITE FOR RESIDUE EDO B 1077
source : AC5
24) chain F
residue 9
type
sequence T
description BINDING SITE FOR RESIDUE EDO B 1077
source : AC5
25) chain F
residue 11
type
sequence K
description BINDING SITE FOR RESIDUE EDO B 1077
source : AC5
26) chain A
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE EDO B 1078
source : AC6
27) chain A
residue 19
type
sequence P
description BINDING SITE FOR RESIDUE EDO B 1078
source : AC6
28) chain A
residue 20
type
sequence S
description BINDING SITE FOR RESIDUE EDO B 1078
source : AC6
29) chain B
residue 18
type
sequence E
description BINDING SITE FOR RESIDUE EDO B 1078
source : AC6
30) chain B
residue 20
type
sequence S
description BINDING SITE FOR RESIDUE EDO B 1078
source : AC6
31) chain A
residue 53
type
sequence G
description BINDING SITE FOR RESIDUE EDO B 1079
source : AC7
32) chain B
residue 15
type
sequence L
description BINDING SITE FOR RESIDUE EDO B 1079
source : AC7
33) chain B
residue 16
type
sequence E
description BINDING SITE FOR RESIDUE EDO B 1079
source : AC7
34) chain B
residue 29
type
sequence K
description BINDING SITE FOR RESIDUE EDO B 1079
source : AC7
35) chain B
residue 33
type
sequence K
description BINDING SITE FOR RESIDUE EDO B 1079
source : AC7
36) chain C
residue 15
type
sequence L
description BINDING SITE FOR RESIDUE EDO C 1075
source : AC8
37) chain C
residue 16
type
sequence E
description BINDING SITE FOR RESIDUE EDO C 1075
source : AC8
38) chain C
residue 29
type
sequence K
description BINDING SITE FOR RESIDUE EDO C 1075
source : AC8
39) chain C
residue 33
type
sequence K
description BINDING SITE FOR RESIDUE EDO C 1075
source : AC8
40) chain C
residue 2
type
sequence Q
description BINDING SITE FOR RESIDUE CL C 1076
source : AC9
41) chain C
residue 63
type
sequence K
description BINDING SITE FOR RESIDUE CL C 1076
source : AC9
42) chain D
residue 45
type
sequence F
description BINDING SITE FOR RESIDUE EDO D 1077
source : BC1
43) chain D
residue 65
type
sequence S
description BINDING SITE FOR RESIDUE EDO D 1077
source : BC1
44) chain D
residue 66
type
sequence T
description BINDING SITE FOR RESIDUE EDO D 1077
source : BC1
45) chain L
residue 44
type
sequence I
description BINDING SITE FOR RESIDUE EDO D 1077
source : BC1
46) chain L
residue 45
type
sequence F
description BINDING SITE FOR RESIDUE EDO D 1077
source : BC1
47) chain L
residue 46
type
sequence A
description BINDING SITE FOR RESIDUE EDO D 1077
source : BC1
48) chain L
residue 47
type
sequence G
description BINDING SITE FOR RESIDUE EDO D 1077
source : BC1
49) chain L
residue 68
type
sequence H
description BINDING SITE FOR RESIDUE EDO D 1077
source : BC1
50) chain D
residue 16
type
sequence E
description BINDING SITE FOR RESIDUE CL D 1078
source : BC2
51) chain D
residue 33
type
sequence K
description BINDING SITE FOR RESIDUE CL D 1078
source : BC2
52) chain C
residue 7
type
sequence T
description BINDING SITE FOR RESIDUE EDO E 1077
source : BC3
53) chain C
residue 9
type
sequence T
description BINDING SITE FOR RESIDUE EDO E 1077
source : BC3
54) chain E
residue 70
type
sequence V
description BINDING SITE FOR RESIDUE EDO E 1077
source : BC3
55) chain E
residue 71
type
sequence L
description BINDING SITE FOR RESIDUE EDO E 1077
source : BC3
56) chain A
residue 37
type
sequence P
description BINDING SITE FOR RESIDUE FLC F 1077
source : BC4
57) chain A
residue 39
type
sequence D
description BINDING SITE FOR RESIDUE FLC F 1077
source : BC4
58) chain A
residue 40
type
sequence Q
description BINDING SITE FOR RESIDUE FLC F 1077
source : BC4
59) chain A
residue 74
type
sequence R
description BINDING SITE FOR RESIDUE FLC F 1077
source : BC4
60) chain B
residue 35
type
sequence G
description BINDING SITE FOR RESIDUE FLC F 1077
source : BC4
61) chain B
residue 37
type
sequence P
description BINDING SITE FOR RESIDUE FLC F 1077
source : BC4
62) chain F
residue 37
type
sequence P
description BINDING SITE FOR RESIDUE FLC F 1077
source : BC4
63) chain F
residue 39
type
sequence D
description BINDING SITE FOR RESIDUE FLC F 1077
source : BC4
64) chain F
residue 40
type
sequence Q
description BINDING SITE FOR RESIDUE FLC F 1077
source : BC4
65) chain F
residue 74
type
sequence R
description BINDING SITE FOR RESIDUE FLC F 1077
source : BC4
66) chain B
residue 39
type
sequence D
description BINDING SITE FOR RESIDUE FLC F 1078
source : BC5
67) chain B
residue 40
type
sequence Q
description BINDING SITE FOR RESIDUE FLC F 1078
source : BC5
68) chain B
residue 74
type
sequence R
description BINDING SITE FOR RESIDUE FLC F 1078
source : BC5
69) chain E
residue 37
type
sequence P
description BINDING SITE FOR RESIDUE FLC F 1078
source : BC5
70) chain E
residue 39
type
sequence D
description BINDING SITE FOR RESIDUE FLC F 1078
source : BC5
71) chain E
residue 40
type
sequence Q
description BINDING SITE FOR RESIDUE FLC F 1078
source : BC5
72) chain E
residue 74
type
sequence R
description BINDING SITE FOR RESIDUE FLC F 1078
source : BC5
73) chain F
residue 35
type
sequence G
description BINDING SITE FOR RESIDUE FLC F 1078
source : BC5
74) chain F
residue 37
type
sequence P
description BINDING SITE FOR RESIDUE FLC F 1078
source : BC5
75) chain B
residue 7
type
sequence T
description BINDING SITE FOR RESIDUE EDO F 1079
source : BC6
76) chain B
residue 9
type
sequence T
description BINDING SITE FOR RESIDUE EDO F 1079
source : BC6
77) chain B
residue 11
type
sequence K
description BINDING SITE FOR RESIDUE EDO F 1079
source : BC6
78) chain F
residue 70
type
sequence V
description BINDING SITE FOR RESIDUE EDO F 1079
source : BC6
79) chain F
residue 71
type
sequence L
description BINDING SITE FOR RESIDUE EDO F 1079
source : BC6
80) chain D
residue 70
type
sequence V
description BINDING SITE FOR RESIDUE EDO H 1077
source : BC7
81) chain D
residue 71
type
sequence L
description BINDING SITE FOR RESIDUE EDO H 1077
source : BC7
82) chain H
residue 7
type
sequence T
description BINDING SITE FOR RESIDUE EDO H 1077
source : BC7
83) chain H
residue 9
type
sequence T
description BINDING SITE FOR RESIDUE EDO H 1077
source : BC7
84) chain H
residue 11
type
sequence K
description BINDING SITE FOR RESIDUE EDO H 1077
source : BC7
85) chain C
residue 45
type
sequence F
description BINDING SITE FOR RESIDUE EDO I 1077
source : BC8
86) chain C
residue 65
type
sequence S
description BINDING SITE FOR RESIDUE EDO I 1077
source : BC8
87) chain C
residue 66
type
sequence T
description BINDING SITE FOR RESIDUE EDO I 1077
source : BC8
88) chain I
residue 44
type
sequence I
description BINDING SITE FOR RESIDUE EDO I 1077
source : BC8
89) chain I
residue 45
type
sequence F
description BINDING SITE FOR RESIDUE EDO I 1077
source : BC8
90) chain I
residue 46
type
sequence A
description BINDING SITE FOR RESIDUE EDO I 1077
source : BC8
91) chain I
residue 47
type
sequence G
description BINDING SITE FOR RESIDUE EDO I 1077
source : BC8
92) chain I
residue 68
type
sequence H
description BINDING SITE FOR RESIDUE EDO I 1077
source : BC8
93) chain I
residue 42
type
sequence R
description BINDING SITE FOR RESIDUE CL I 1078
source : BC9
94) chain B
residue 45
type
sequence F
description BINDING SITE FOR RESIDUE EDO J 1077
source : CC1
95) chain B
residue 65
type
sequence S
description BINDING SITE FOR RESIDUE EDO J 1077
source : CC1
96) chain B
residue 66
type
sequence T
description BINDING SITE FOR RESIDUE EDO J 1077
source : CC1
97) chain J
residue 45
type
sequence F
description BINDING SITE FOR RESIDUE EDO J 1077
source : CC1
98) chain J
residue 46
type
sequence A
description BINDING SITE FOR RESIDUE EDO J 1077
source : CC1
99) chain J
residue 47
type
sequence G
description BINDING SITE FOR RESIDUE EDO J 1077
source : CC1
100) chain J
residue 68
type
sequence H
description BINDING SITE FOR RESIDUE EDO J 1077
source : CC1
101) chain J
residue 7
type
sequence T
description BINDING SITE FOR RESIDUE EDO K 1077
source : CC2
102) chain J
residue 9
type
sequence T
description BINDING SITE FOR RESIDUE EDO K 1077
source : CC2
103) chain K
residue 70
type
sequence V
description BINDING SITE FOR RESIDUE EDO K 1077
source : CC2
104) chain K
residue 71
type
sequence L
description BINDING SITE FOR RESIDUE EDO K 1077
source : CC2
105) chain I
residue 70
type
sequence V
description BINDING SITE FOR RESIDUE EDO L 1075
source : CC3
106) chain I
residue 71
type
sequence L
description BINDING SITE FOR RESIDUE EDO L 1075
source : CC3
107) chain L
residue 7
type
sequence T
description BINDING SITE FOR RESIDUE EDO L 1075
source : CC3
108) chain L
residue 9
type
sequence T
description BINDING SITE FOR RESIDUE EDO L 1075
source : CC3
109) chain L
residue 11
type
sequence K
description BINDING SITE FOR RESIDUE EDO L 1075
source : CC3
110) chain I
residue 7
type
sequence T
description BINDING SITE FOR RESIDUE EDO L 1076
source : CC4
111) chain I
residue 9
type
sequence T
description BINDING SITE FOR RESIDUE EDO L 1076
source : CC4
112) chain I
residue 11
type
sequence K
description BINDING SITE FOR RESIDUE EDO L 1076
source : CC4
113) chain L
residue 70
type
sequence V
description BINDING SITE FOR RESIDUE EDO L 1076
source : CC4
114) chain L
residue 71
type
sequence L
description BINDING SITE FOR RESIDUE EDO L 1076
source : CC4
115) chain L
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE EDO L 1077
source : CC5
116) chain L
residue 2
type
sequence Q
description BINDING SITE FOR RESIDUE EDO L 1077
source : CC5
117) chain L
residue 14
type
sequence T
description BINDING SITE FOR RESIDUE EDO L 1077
source : CC5
118) chain L
residue 15
type
sequence L
description BINDING SITE FOR RESIDUE EDO L 1077
source : CC5
119) chain L
residue 16
type
sequence E
description BINDING SITE FOR RESIDUE EDO L 1077
source : CC5
120) chain L
residue 25
type
sequence N
description BINDING SITE FOR RESIDUE CL L 1078
source : CC6
121) chain L
residue 28
type
sequence A
description BINDING SITE FOR RESIDUE CL L 1078
source : CC6
122) chain L
residue 14
type
sequence T
description BINDING SITE FOR RESIDUE CL L 1079
source : CC7
123) chain I
residue 16
type
sequence E
description BINDING SITE FOR RESIDUE CL L 1080
source : CC8
124) chain I
residue 33
type
sequence K
description BINDING SITE FOR RESIDUE CL L 1080
source : CC8
125) chain A
residue 65
type MOD_RES
sequence S
description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291
source Swiss-Prot : SWS_FT_FI3
126) chain J
residue 65
type MOD_RES
sequence S
description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291
source Swiss-Prot : SWS_FT_FI3
127) chain K
residue 65
type MOD_RES
sequence S
description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291
source Swiss-Prot : SWS_FT_FI3
128) chain L
residue 65
type MOD_RES
sequence S
description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291
source Swiss-Prot : SWS_FT_FI3
129) chain B
residue 65
type MOD_RES
sequence S
description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291
source Swiss-Prot : SWS_FT_FI3
130) chain C
residue 65
type MOD_RES
sequence S
description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291
source Swiss-Prot : SWS_FT_FI3
131) chain D
residue 65
type MOD_RES
sequence S
description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291
source Swiss-Prot : SWS_FT_FI3
132) chain E
residue 65
type MOD_RES
sequence S
description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291
source Swiss-Prot : SWS_FT_FI3
133) chain F
residue 65
type MOD_RES
sequence S
description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291
source Swiss-Prot : SWS_FT_FI3
134) chain G
residue 65
type MOD_RES
sequence S
description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291
source Swiss-Prot : SWS_FT_FI3
135) chain H
residue 65
type MOD_RES
sequence S
description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291
source Swiss-Prot : SWS_FT_FI3
136) chain I
residue 65
type MOD_RES
sequence S
description Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291
source Swiss-Prot : SWS_FT_FI3
137) chain A
residue 66
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4
138) chain J
residue 66
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4
139) chain K
residue 66
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4
140) chain L
residue 66
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4
141) chain B
residue 66
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4
142) chain C
residue 66
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4
143) chain D
residue 66
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4
144) chain E
residue 66
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4
145) chain F
residue 66
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4
146) chain G
residue 66
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4
147) chain H
residue 66
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4
148) chain I
residue 66
type MOD_RES
sequence T
description (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
source Swiss-Prot : SWS_FT_FI4
149) chain A
residue 54
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
150) chain E
residue 72
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
151) chain F
residue 54
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
152) chain F
residue 72
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
153) chain G
residue 54
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
154) chain G
residue 72
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
155) chain H
residue 54
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
156) chain H
residue 72
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
157) chain I
residue 54
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
158) chain I
residue 72
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
159) chain J
residue 54
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
160) chain A
residue 72
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
161) chain J
residue 72
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
162) chain K
residue 54
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
163) chain K
residue 72
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
164) chain L
residue 54
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
165) chain L
residue 72
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
166) chain B
residue 54
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
167) chain B
residue 72
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
168) chain C
residue 54
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
169) chain C
residue 72
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
170) chain D
residue 54
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
171) chain D
residue 72
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
172) chain E
residue 54
type SITE
sequence R
description Interacts with activating enzyme
source Swiss-Prot : SWS_FT_FI1
173) chain A
residue 68
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2
174) chain J
residue 68
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2
175) chain K
residue 68
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2
176) chain L
residue 68
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2
177) chain B
residue 68
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2
178) chain C
residue 68
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2
179) chain D
residue 68
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2
180) chain E
residue 68
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2
181) chain F
residue 68
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2
182) chain G
residue 68
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2
183) chain H
residue 68
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2
184) chain I
residue 68
type SITE
sequence H
description Essential for function
source Swiss-Prot : SWS_FT_FI2
185) chain A
residue 6
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
source Swiss-Prot : SWS_FT_FI6
186) chain J
residue 6
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
source Swiss-Prot : SWS_FT_FI6
187) chain K
residue 6
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
source Swiss-Prot : SWS_FT_FI6
188) chain L
residue 6
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
source Swiss-Prot : SWS_FT_FI6
189) chain B
residue 6
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
source Swiss-Prot : SWS_FT_FI6
190) chain C
residue 6
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
source Swiss-Prot : SWS_FT_FI6
191) chain D
residue 6
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
source Swiss-Prot : SWS_FT_FI6
192) chain E
residue 6
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
source Swiss-Prot : SWS_FT_FI6
193) chain F
residue 6
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
source Swiss-Prot : SWS_FT_FI6
194) chain G
residue 6
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
source Swiss-Prot : SWS_FT_FI6
195) chain H
residue 6
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
source Swiss-Prot : SWS_FT_FI6
196) chain I
residue 6
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
source Swiss-Prot : SWS_FT_FI6
197) chain A
residue 63
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
source Swiss-Prot : SWS_FT_FI12
198) chain J
residue 63
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
source Swiss-Prot : SWS_FT_FI12
199) chain K
residue 63
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
source Swiss-Prot : SWS_FT_FI12
200) chain L
residue 63
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
source Swiss-Prot : SWS_FT_FI12
201) chain B
residue 63
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
source Swiss-Prot : SWS_FT_FI12
202) chain C
residue 63
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
source Swiss-Prot : SWS_FT_FI12
203) chain D
residue 63
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
source Swiss-Prot : SWS_FT_FI12
204) chain E
residue 63
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
source Swiss-Prot : SWS_FT_FI12
205) chain F
residue 63
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
source Swiss-Prot : SWS_FT_FI12
206) chain G
residue 63
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
source Swiss-Prot : SWS_FT_FI12
207) chain H
residue 63
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
source Swiss-Prot : SWS_FT_FI12
208) chain I
residue 63
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
source Swiss-Prot : SWS_FT_FI12
209) chain A
residue 29
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127
source Swiss-Prot : SWS_FT_FI10
210) chain J
residue 29
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127
source Swiss-Prot : SWS_FT_FI10
211) chain K
residue 29
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127
source Swiss-Prot : SWS_FT_FI10
212) chain L
residue 29
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127
source Swiss-Prot : SWS_FT_FI10
213) chain B
residue 29
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127
source Swiss-Prot : SWS_FT_FI10
214) chain C
residue 29
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127
source Swiss-Prot : SWS_FT_FI10
215) chain D
residue 29
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127
source Swiss-Prot : SWS_FT_FI10
216) chain E
residue 29
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127
source Swiss-Prot : SWS_FT_FI10
217) chain F
residue 29
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127
source Swiss-Prot : SWS_FT_FI10
218) chain G
residue 29
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127
source Swiss-Prot : SWS_FT_FI10
219) chain H
residue 29
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127
source Swiss-Prot : SWS_FT_FI10
220) chain I
residue 29
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127
source Swiss-Prot : SWS_FT_FI10
221) chain A
residue 33
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
source Swiss-Prot : SWS_FT_FI11
222) chain J
residue 33
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
source Swiss-Prot : SWS_FT_FI11
223) chain K
residue 33
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
source Swiss-Prot : SWS_FT_FI11
224) chain L
residue 33
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
source Swiss-Prot : SWS_FT_FI11
225) chain B
residue 33
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
source Swiss-Prot : SWS_FT_FI11
226) chain C
residue 33
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
source Swiss-Prot : SWS_FT_FI11
227) chain D
residue 33
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
source Swiss-Prot : SWS_FT_FI11
228) chain E
residue 33
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
source Swiss-Prot : SWS_FT_FI11
229) chain F
residue 33
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
source Swiss-Prot : SWS_FT_FI11
230) chain G
residue 33
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
source Swiss-Prot : SWS_FT_FI11
231) chain H
residue 33
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
source Swiss-Prot : SWS_FT_FI11
232) chain I
residue 33
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
source Swiss-Prot : SWS_FT_FI11
233) chain A
residue 27
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
source Swiss-Prot : SWS_FT_FI9
234) chain J
residue 27
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
source Swiss-Prot : SWS_FT_FI9
235) chain K
residue 27
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
source Swiss-Prot : SWS_FT_FI9
236) chain L
residue 27
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
source Swiss-Prot : SWS_FT_FI9
237) chain B
residue 27
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
source Swiss-Prot : SWS_FT_FI9
238) chain C
residue 27
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
source Swiss-Prot : SWS_FT_FI9
239) chain D
residue 27
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
source Swiss-Prot : SWS_FT_FI9
240) chain E
residue 27
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
source Swiss-Prot : SWS_FT_FI9
241) chain F
residue 27
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
source Swiss-Prot : SWS_FT_FI9
242) chain G
residue 27
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
source Swiss-Prot : SWS_FT_FI9
243) chain H
residue 27
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
source Swiss-Prot : SWS_FT_FI9
244) chain I
residue 27
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
source Swiss-Prot : SWS_FT_FI9
245) chain A
residue 27-52
type prosite
sequence KAKIQDKEGIPPDQQRLIFAGKQLED
description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
source prosite : PS00299
246) chain A
residue 76
type MOD_RES
sequence G
description ADP-ribosylglycine => ECO:0000269|PubMed:28525742
source Swiss-Prot : SWS_FT_FI5
247) chain J
residue 76
type MOD_RES
sequence G
description ADP-ribosylglycine => ECO:0000269|PubMed:28525742
source Swiss-Prot : SWS_FT_FI5
248) chain K
residue 76
type MOD_RES
sequence G
description ADP-ribosylglycine => ECO:0000269|PubMed:28525742
source Swiss-Prot : SWS_FT_FI5
249) chain B
residue 76
type MOD_RES
sequence G
description ADP-ribosylglycine => ECO:0000269|PubMed:28525742
source Swiss-Prot : SWS_FT_FI5
250) chain D
residue 76
type MOD_RES
sequence G
description ADP-ribosylglycine => ECO:0000269|PubMed:28525742
source Swiss-Prot : SWS_FT_FI5
251) chain E
residue 76
type MOD_RES
sequence G
description ADP-ribosylglycine => ECO:0000269|PubMed:28525742
source Swiss-Prot : SWS_FT_FI5
252) chain F
residue 76
type MOD_RES
sequence G
description ADP-ribosylglycine => ECO:0000269|PubMed:28525742
source Swiss-Prot : SWS_FT_FI5
253) chain G
residue 76
type MOD_RES
sequence G
description ADP-ribosylglycine => ECO:0000269|PubMed:28525742
source Swiss-Prot : SWS_FT_FI5
254) chain H
residue 76
type MOD_RES
sequence G
description ADP-ribosylglycine => ECO:0000269|PubMed:28525742
source Swiss-Prot : SWS_FT_FI5
255) chain I
residue 76
type MOD_RES
sequence G
description ADP-ribosylglycine => ECO:0000269|PubMed:28525742
source Swiss-Prot : SWS_FT_FI5
256) chain E
residue 76
type CROSSLNK
sequence G
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
source Swiss-Prot : SWS_FT_FI7
257) chain F
residue 76
type CROSSLNK
sequence G
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
source Swiss-Prot : SWS_FT_FI7
258) chain G
residue 76
type CROSSLNK
sequence G
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
source Swiss-Prot : SWS_FT_FI7
259) chain H
residue 76
type CROSSLNK
sequence G
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
source Swiss-Prot : SWS_FT_FI7
260) chain I
residue 76
type CROSSLNK
sequence G
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
source Swiss-Prot : SWS_FT_FI7
261) chain A
residue 76
type CROSSLNK
sequence G
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
source Swiss-Prot : SWS_FT_FI7
262) chain J
residue 76
type CROSSLNK
sequence G
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
source Swiss-Prot : SWS_FT_FI7
263) chain K
residue 76
type CROSSLNK
sequence G
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
source Swiss-Prot : SWS_FT_FI7
264) chain B
residue 76
type CROSSLNK
sequence G
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
source Swiss-Prot : SWS_FT_FI7
265) chain D
residue 76
type CROSSLNK
sequence G
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
source Swiss-Prot : SWS_FT_FI7
266) chain A
residue 11
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8
267) chain E
residue 48
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8
268) chain F
residue 11
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8
269) chain F
residue 48
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8
270) chain G
residue 11
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8
271) chain G
residue 48
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8
272) chain H
residue 11
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8
273) chain H
residue 48
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8
274) chain I
residue 11
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8
275) chain I
residue 48
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8
276) chain J
residue 11
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8
277) chain A
residue 48
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8
278) chain J
residue 48
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8
279) chain K
residue 11
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8
280) chain K
residue 48
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8
281) chain L
residue 11
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8
282) chain L
residue 48
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8
283) chain B
residue 11
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8
284) chain B
residue 48
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8
285) chain C
residue 11
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8
286) chain C
residue 48
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8
287) chain D
residue 11
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8
288) chain D
residue 48
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8
289) chain E
residue 11
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI8

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