|
|
1)
|
chain |
c |
residue |
113 |
type |
|
sequence |
H
|
description |
binding site for residue ZN c 401
|
source |
: AC1
|
|
2)
|
chain |
c |
residue |
115 |
type |
|
sequence |
H
|
description |
binding site for residue ZN c 401
|
source |
: AC1
|
|
3)
|
chain |
c |
residue |
126 |
type |
|
sequence |
D
|
description |
binding site for residue ZN c 401
|
source |
: AC1
|
|
4)
|
chain |
u |
residue |
76 |
type |
|
sequence |
G
|
description |
binding site for residue ZN c 401
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
176 |
type |
|
sequence |
D
|
description |
binding site for residue ADP A 501
|
source |
: AC2
|
|
6)
|
chain |
A |
residue |
177 |
type |
|
sequence |
V
|
description |
binding site for residue ADP A 501
|
source |
: AC2
|
|
7)
|
chain |
A |
residue |
178 |
type |
|
sequence |
G
|
description |
binding site for residue ADP A 501
|
source |
: AC2
|
|
8)
|
chain |
A |
residue |
219 |
type |
|
sequence |
G
|
description |
binding site for residue ADP A 501
|
source |
: AC2
|
|
9)
|
chain |
A |
residue |
220 |
type |
|
sequence |
T
|
description |
binding site for residue ADP A 501
|
source |
: AC2
|
|
10)
|
chain |
A |
residue |
222 |
type |
|
sequence |
K
|
description |
binding site for residue ADP A 501
|
source |
: AC2
|
|
11)
|
chain |
A |
residue |
223 |
type |
|
sequence |
T
|
description |
binding site for residue ADP A 501
|
source |
: AC2
|
|
12)
|
chain |
A |
residue |
224 |
type |
|
sequence |
L
|
description |
binding site for residue ADP A 501
|
source |
: AC2
|
|
13)
|
chain |
A |
residue |
353 |
type |
|
sequence |
H
|
description |
binding site for residue ADP A 501
|
source |
: AC2
|
|
14)
|
chain |
A |
residue |
354 |
type |
|
sequence |
I
|
description |
binding site for residue ADP A 501
|
source |
: AC2
|
|
15)
|
chain |
A |
residue |
358 |
type |
|
sequence |
H
|
description |
binding site for residue ADP A 501
|
source |
: AC2
|
|
16)
|
chain |
A |
residue |
382 |
type |
|
sequence |
G
|
description |
binding site for residue ADP A 501
|
source |
: AC2
|
|
17)
|
chain |
C |
residue |
150 |
type |
|
sequence |
M
|
description |
binding site for residue ATP C 501
|
source |
: AC3
|
|
18)
|
chain |
C |
residue |
151 |
type |
|
sequence |
I
|
description |
binding site for residue ATP C 501
|
source |
: AC3
|
|
19)
|
chain |
C |
residue |
192 |
type |
|
sequence |
P
|
description |
binding site for residue ATP C 501
|
source |
: AC3
|
|
20)
|
chain |
C |
residue |
193 |
type |
|
sequence |
G
|
description |
binding site for residue ATP C 501
|
source |
: AC3
|
|
21)
|
chain |
C |
residue |
194 |
type |
|
sequence |
T
|
description |
binding site for residue ATP C 501
|
source |
: AC3
|
|
22)
|
chain |
C |
residue |
195 |
type |
|
sequence |
G
|
description |
binding site for residue ATP C 501
|
source |
: AC3
|
|
23)
|
chain |
C |
residue |
196 |
type |
|
sequence |
K
|
description |
binding site for residue ATP C 501
|
source |
: AC3
|
|
24)
|
chain |
C |
residue |
197 |
type |
|
sequence |
T
|
description |
binding site for residue ATP C 501
|
source |
: AC3
|
|
25)
|
chain |
C |
residue |
198 |
type |
|
sequence |
L
|
description |
binding site for residue ATP C 501
|
source |
: AC3
|
|
26)
|
chain |
C |
residue |
328 |
type |
|
sequence |
I
|
description |
binding site for residue ATP C 501
|
source |
: AC3
|
|
27)
|
chain |
C |
residue |
357 |
type |
|
sequence |
A
|
description |
binding site for residue ATP C 501
|
source |
: AC3
|
|
28)
|
chain |
C |
residue |
360 |
type |
|
sequence |
K
|
description |
binding site for residue ATP C 501
|
source |
: AC3
|
|
29)
|
chain |
D |
residue |
323 |
type |
|
sequence |
R
|
description |
binding site for residue ATP C 501
|
source |
: AC3
|
|
30)
|
chain |
C |
residue |
197 |
type |
|
sequence |
T
|
description |
binding site for residue MG C 502
|
source |
: AC4
|
|
31)
|
chain |
D |
residue |
168 |
type |
|
sequence |
G
|
description |
binding site for residue ATP D 501
|
source |
: AC5
|
|
32)
|
chain |
D |
residue |
208 |
type |
|
sequence |
P
|
description |
binding site for residue ATP D 501
|
source |
: AC5
|
|
33)
|
chain |
D |
residue |
209 |
type |
|
sequence |
G
|
description |
binding site for residue ATP D 501
|
source |
: AC5
|
|
34)
|
chain |
D |
residue |
211 |
type |
|
sequence |
G
|
description |
binding site for residue ATP D 501
|
source |
: AC5
|
|
35)
|
chain |
D |
residue |
212 |
type |
|
sequence |
K
|
description |
binding site for residue ATP D 501
|
source |
: AC5
|
|
36)
|
chain |
D |
residue |
213 |
type |
|
sequence |
T
|
description |
binding site for residue ATP D 501
|
source |
: AC5
|
|
37)
|
chain |
D |
residue |
214 |
type |
|
sequence |
M
|
description |
binding site for residue ATP D 501
|
source |
: AC5
|
|
38)
|
chain |
D |
residue |
372 |
type |
|
sequence |
G
|
description |
binding site for residue ATP D 501
|
source |
: AC5
|
|
39)
|
chain |
D |
residue |
373 |
type |
|
sequence |
A
|
description |
binding site for residue ATP D 501
|
source |
: AC5
|
|
40)
|
chain |
D |
residue |
376 |
type |
|
sequence |
N
|
description |
binding site for residue ATP D 501
|
source |
: AC5
|
|
41)
|
chain |
E |
residue |
265 |
type |
|
sequence |
D
|
description |
binding site for residue ATP D 501
|
source |
: AC5
|
|
42)
|
chain |
E |
residue |
291 |
type |
|
sequence |
R
|
description |
binding site for residue ATP D 501
|
source |
: AC5
|
|
43)
|
chain |
E |
residue |
294 |
type |
|
sequence |
R
|
description |
binding site for residue ATP D 501
|
source |
: AC5
|
|
44)
|
chain |
E |
residue |
134 |
type |
|
sequence |
E
|
description |
binding site for residue ATP E 401
|
source |
: AC7
|
|
45)
|
chain |
E |
residue |
135 |
type |
|
sequence |
I
|
description |
binding site for residue ATP E 401
|
source |
: AC7
|
|
46)
|
chain |
E |
residue |
176 |
type |
|
sequence |
P
|
description |
binding site for residue ATP E 401
|
source |
: AC7
|
|
47)
|
chain |
E |
residue |
177 |
type |
|
sequence |
G
|
description |
binding site for residue ATP E 401
|
source |
: AC7
|
|
48)
|
chain |
E |
residue |
178 |
type |
|
sequence |
T
|
description |
binding site for residue ATP E 401
|
source |
: AC7
|
|
49)
|
chain |
E |
residue |
179 |
type |
|
sequence |
G
|
description |
binding site for residue ATP E 401
|
source |
: AC7
|
|
50)
|
chain |
E |
residue |
180 |
type |
|
sequence |
K
|
description |
binding site for residue ATP E 401
|
source |
: AC7
|
|
51)
|
chain |
E |
residue |
181 |
type |
|
sequence |
T
|
description |
binding site for residue ATP E 401
|
source |
: AC7
|
|
52)
|
chain |
E |
residue |
182 |
type |
|
sequence |
L
|
description |
binding site for residue ATP E 401
|
source |
: AC7
|
|
53)
|
chain |
E |
residue |
312 |
type |
|
sequence |
I
|
description |
binding site for residue ATP E 401
|
source |
: AC7
|
|
54)
|
chain |
E |
residue |
316 |
type |
|
sequence |
H
|
description |
binding site for residue ATP E 401
|
source |
: AC7
|
|
55)
|
chain |
E |
residue |
340 |
type |
|
sequence |
G
|
description |
binding site for residue ATP E 401
|
source |
: AC7
|
|
56)
|
chain |
E |
residue |
341 |
type |
|
sequence |
A
|
description |
binding site for residue ATP E 401
|
source |
: AC7
|
|
57)
|
chain |
E |
residue |
344 |
type |
|
sequence |
R
|
description |
binding site for residue ATP E 401
|
source |
: AC7
|
|
58)
|
chain |
F |
residue |
344 |
type |
|
sequence |
R
|
description |
binding site for residue ATP E 401
|
source |
: AC7
|
|
59)
|
chain |
E |
residue |
181 |
type |
|
sequence |
T
|
description |
binding site for residue MG E 402
|
source |
: AC8
|
|
60)
|
chain |
E |
residue |
233 |
type |
|
sequence |
D
|
description |
binding site for residue MG E 402
|
source |
: AC8
|
|
61)
|
chain |
F |
residue |
187 |
type |
|
sequence |
D
|
description |
binding site for residue ADP F 501
|
source |
: AC9
|
|
62)
|
chain |
F |
residue |
188 |
type |
|
sequence |
I
|
description |
binding site for residue ADP F 501
|
source |
: AC9
|
|
63)
|
chain |
F |
residue |
189 |
type |
|
sequence |
G
|
description |
binding site for residue ADP F 501
|
source |
: AC9
|
|
64)
|
chain |
F |
residue |
230 |
type |
|
sequence |
G
|
description |
binding site for residue ADP F 501
|
source |
: AC9
|
|
65)
|
chain |
F |
residue |
231 |
type |
|
sequence |
T
|
description |
binding site for residue ADP F 501
|
source |
: AC9
|
|
66)
|
chain |
F |
residue |
233 |
type |
|
sequence |
K
|
description |
binding site for residue ADP F 501
|
source |
: AC9
|
|
67)
|
chain |
F |
residue |
234 |
type |
|
sequence |
T
|
description |
binding site for residue ADP F 501
|
source |
: AC9
|
|
68)
|
chain |
F |
residue |
235 |
type |
|
sequence |
L
|
description |
binding site for residue ADP F 501
|
source |
: AC9
|
|
69)
|
chain |
F |
residue |
365 |
type |
|
sequence |
I
|
description |
binding site for residue ADP F 501
|
source |
: AC9
|
|
70)
|
chain |
F |
residue |
369 |
type |
|
sequence |
H
|
description |
binding site for residue ADP F 501
|
source |
: AC9
|
|
71)
|
chain |
F |
residue |
393 |
type |
|
sequence |
G
|
description |
binding site for residue ADP F 501
|
source |
: AC9
|
|
72)
|
chain |
F |
residue |
394 |
type |
|
sequence |
A
|
description |
binding site for residue ADP F 501
|
source |
: AC9
|
|
73)
|
chain |
E |
residue |
174 |
type |
BINDING |
sequence |
G
|
description |
BINDING => ECO:0000255
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
74)
|
chain |
S |
residue |
134 |
type |
BINDING |
sequence |
S
|
description |
BINDING => ECO:0000255
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
75)
|
chain |
s |
residue |
34 |
type |
BINDING |
sequence |
S
|
description |
BINDING => ECO:0000255
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
76)
|
chain |
s |
residue |
40 |
type |
BINDING |
sequence |
S
|
description |
BINDING => ECO:0000255
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
77)
|
chain |
s |
residue |
134 |
type |
BINDING |
sequence |
S
|
description |
BINDING => ECO:0000255
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
78)
|
chain |
E |
residue |
72 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
79)
|
chain |
E |
residue |
206 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
80)
|
chain |
M |
residue |
229 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
81)
|
chain |
m |
residue |
56 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
82)
|
chain |
m |
residue |
205 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
83)
|
chain |
m |
residue |
229 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
84)
|
chain |
H |
residue |
76 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
85)
|
chain |
h |
residue |
76 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
86)
|
chain |
u |
residue |
63 |
type |
CROSSLNK |
sequence |
R
|
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
|
|
87)
|
chain |
K |
residue |
198 |
type |
CARBOHYD |
sequence |
S
|
description |
O-linked (GlcNAc) serine => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
88)
|
chain |
k |
residue |
198 |
type |
CARBOHYD |
sequence |
S
|
description |
O-linked (GlcNAc) serine => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
89)
|
chain |
h |
residue |
70 |
type |
CARBOHYD |
sequence |
K
|
description |
O-linked (GlcNAc) serine => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
90)
|
chain |
h |
residue |
171 |
type |
CARBOHYD |
sequence |
K
|
description |
O-linked (GlcNAc) serine => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
91)
|
chain |
u |
residue |
27-52 |
type |
prosite |
sequence |
KAKIQDKEGIPPDQQRLIFAGKQLED
|
description |
UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
|
source |
prosite : PS00299
|
|
92)
|
chain |
u |
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
|
|
93)
|
chain |
u |
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
|
|
94)
|
chain |
E |
residue |
244 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
95)
|
chain |
s |
residue |
176 |
type |
MOD_RES |
sequence |
K
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
96)
|
chain |
i |
residue |
127 |
type |
MOD_RES |
sequence |
K
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
97)
|
chain |
i |
residue |
176 |
type |
MOD_RES |
sequence |
K
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
98)
|
chain |
h |
residue |
14 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
99)
|
chain |
h |
residue |
16 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
100)
|
chain |
S |
residue |
30 |
type |
CARBOHYD |
sequence |
S
|
description |
O-linked (GlcNAc) serine => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
101)
|
chain |
S |
residue |
181 |
type |
CARBOHYD |
sequence |
S
|
description |
O-linked (GlcNAc) serine => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
102)
|
chain |
s |
residue |
30 |
type |
CARBOHYD |
sequence |
S
|
description |
O-linked (GlcNAc) serine => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
103)
|
chain |
s |
residue |
181 |
type |
CARBOHYD |
sequence |
S
|
description |
O-linked (GlcNAc) serine => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
104)
|
chain |
l |
residue |
202 |
type |
CARBOHYD |
sequence |
E
|
description |
O-linked (GlcNAc) serine => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
105)
|
chain |
H |
residue |
121 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000250|UniProtKB:P17220
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
106)
|
chain |
h |
residue |
121 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000250|UniProtKB:P17220
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
107)
|
chain |
u |
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
|
|
108)
|
chain |
u |
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
|
|
109)
|
chain |
u |
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
|
|
110)
|
chain |
E |
residue |
273-291 |
type |
prosite |
sequence |
VKMIMATNRPDTLDPALLR
|
description |
AAA AAA-protein family signature. VkMImATNrpdtLDpALl.R
|
source |
prosite : PS00674
|
|
111)
|
chain |
C |
residue |
289-307 |
type |
prosite |
sequence |
IKVIMATNRIDILDSALLR
|
description |
AAA AAA-protein family signature. VkMImATNrpdtLDpALl.R
|
source |
prosite : PS00674
|
|
112)
|
chain |
D |
residue |
305-323 |
type |
prosite |
sequence |
VKVIMATNRADTLDPALLR
|
description |
AAA AAA-protein family signature. VkMImATNrpdtLDpALl.R
|
source |
prosite : PS00674
|
|
113)
|
chain |
F |
residue |
326-344 |
type |
prosite |
sequence |
VKVIAATNRVDILDPALLR
|
description |
AAA AAA-protein family signature. VkMImATNrpdtLDpALl.R
|
source |
prosite : PS00674
|
|
114)
|
chain |
A |
residue |
315-333 |
type |
prosite |
sequence |
IKVLMATNRPDTLDPALMR
|
description |
AAA AAA-protein family signature. VkMImATNrpdtLDpALl.R
|
source |
prosite : PS00674
|
|
115)
|
chain |
B |
residue |
325-343 |
type |
prosite |
sequence |
VKVIMATNRIETLDPALIR
|
description |
AAA AAA-protein family signature. VkMImATNrpdtLDpALl.R
|
source |
prosite : PS00674
|
|
116)
|
chain |
l |
residue |
6-28 |
type |
prosite |
sequence |
YDNDVTVWSPQGRIHQIEYAMEA
|
description |
PROTEASOME_ALPHA_1 Proteasome alpha-type subunits signature. YdndvTvWSPqGRihQIEYAmeA
|
source |
prosite : PS00388
|
|
117)
|
chain |
k |
residue |
8-30 |
type |
prosite |
sequence |
YDRGVNTFSPEGRLFQVEYAIEA
|
description |
PROTEASOME_ALPHA_1 Proteasome alpha-type subunits signature. YdndvTvWSPqGRihQIEYAmeA
|
source |
prosite : PS00388
|
|
118)
|
chain |
j |
residue |
3-25 |
type |
prosite |
sequence |
YDRAITVFSPDGHLFQVEYAQEA
|
description |
PROTEASOME_ALPHA_1 Proteasome alpha-type subunits signature. YdndvTvWSPqGRihQIEYAmeA
|
source |
prosite : PS00388
|
|
119)
|
chain |
i |
residue |
5-27 |
type |
prosite |
sequence |
YDSRTTIFSPEGRLYQVEYAMEA
|
description |
PROTEASOME_ALPHA_1 Proteasome alpha-type subunits signature. YdndvTvWSPqGRihQIEYAmeA
|
source |
prosite : PS00388
|
|
120)
|
chain |
h |
residue |
6-28 |
type |
prosite |
sequence |
YSFSLTTFSPSGKLVQIEYALAA
|
description |
PROTEASOME_ALPHA_1 Proteasome alpha-type subunits signature. YdndvTvWSPqGRihQIEYAmeA
|
source |
prosite : PS00388
|
|
121)
|
chain |
M |
residue |
7-29 |
type |
prosite |
sequence |
YDLSASTFSPDGRVFQVEYAMKA
|
description |
PROTEASOME_ALPHA_1 Proteasome alpha-type subunits signature. YdndvTvWSPqGRihQIEYAmeA
|
source |
prosite : PS00388
|
|
122)
|
chain |
g |
residue |
9-31 |
type |
prosite |
sequence |
FDRHITIFSPEGRLYQVEYAFKA
|
description |
PROTEASOME_ALPHA_1 Proteasome alpha-type subunits signature. YdndvTvWSPqGRihQIEYAmeA
|
source |
prosite : PS00388
|
|
123)
|
chain |
R |
residue |
4-51 |
type |
prosite |
sequence |
LAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLG
TMAGGAAD
|
description |
PROTEASOME_BETA_1 Proteasome beta-type subunits signature. LAFkFrhGVIVAADsratagayiasqtvk.KvieinpyllgtmaGgaAD
|
source |
prosite : PS00854
|
|
124)
|
chain |
P |
residue |
12-59 |
type |
prosite |
sequence |
MAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYI
GLAGLATD
|
description |
PROTEASOME_BETA_1 Proteasome beta-type subunits signature. LAFkFrhGVIVAADsratagayiasqtvk.KvieinpyllgtmaGgaAD
|
source |
prosite : PS00854
|
|
125)
|
chain |
O |
residue |
4-51 |
type |
prosite |
sequence |
AGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYC
CGAGTAAD
|
description |
PROTEASOME_BETA_1 Proteasome beta-type subunits signature. LAFkFrhGVIVAADsratagayiasqtvk.KvieinpyllgtmaGgaAD
|
source |
prosite : PS00854
|
|
126)
|
chain |
S |
residue |
13-60 |
type |
prosite |
sequence |
LAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVI
GCSGFHGD
|
description |
PROTEASOME_BETA_1 Proteasome beta-type subunits signature. LAFkFrhGVIVAADsratagayiasqtvk.KvieinpyllgtmaGgaAD
|
source |
prosite : PS00854
|
|
127)
|
chain |
N |
residue |
4-51 |
type |
prosite |
sequence |
MAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFC
CRSGSAAD
|
description |
PROTEASOME_BETA_1 Proteasome beta-type subunits signature. LAFkFrhGVIVAADsratagayiasqtvk.KvieinpyllgtmaGgaAD
|
source |
prosite : PS00854
|
|
128)
|
chain |
i |
residue |
35-82 |
type |
prosite |
sequence |
LGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMAC
SVAGITSD
|
description |
PROTEASOME_BETA_1 Proteasome beta-type subunits signature. LAFkFrhGVIVAADsratagayiasqtvk.KvieinpyllgtmaGgaAD
|
source |
prosite : PS00854
|
|
129)
|
chain |
T |
residue |
12-59 |
type |
prosite |
sequence |
LGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTML
GASGDYAD
|
description |
PROTEASOME_BETA_1 Proteasome beta-type subunits signature. LAFkFrhGVIVAADsratagayiasqtvk.KvieinpyllgtmaGgaAD
|
source |
prosite : PS00854
|
|
130)
|
chain |
Q |
residue |
5-52 |
type |
prosite |
sequence |
IGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILL
LCVGEAGD
|
description |
PROTEASOME_BETA_1 Proteasome beta-type subunits signature. LAFkFrhGVIVAADsratagayiasqtvk.KvieinpyllgtmaGgaAD
|
source |
prosite : PS00854
|
|