|
|
1)
|
chain |
B |
residue |
95-120 |
type |
prosite |
sequence |
VGDGTTSVTVLAAELLREAESLIAKK
|
description |
PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGDGTTSVTVlAaellreaesl........IAKK
|
source |
prosite : PS00107
|
|
2)
|
chain |
H |
residue |
282-293 |
type |
prosite |
sequence |
AIADTGANVVVT
|
description |
ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. AIADTGANVVVT
|
source |
prosite : PS00141
|
|
3)
|
chain |
C |
residue |
38-50 |
type |
prosite |
sequence |
RTCLGPKSMMKML
|
description |
TCP1_1 Chaperonins TCP-1 signature 1. RTcLGPkSmmKML
|
source |
prosite : PS00750
|
|
4)
|
chain |
D |
residue |
49-61 |
type |
prosite |
sequence |
RTSLGPKGMDKMI
|
description |
TCP1_1 Chaperonins TCP-1 signature 1. RTcLGPkSmmKML
|
source |
prosite : PS00750
|
|
5)
|
chain |
F |
residue |
35-47 |
type |
prosite |
sequence |
RTNLGPKGTMKML
|
description |
TCP1_1 Chaperonins TCP-1 signature 1. RTcLGPkSmmKML
|
source |
prosite : PS00750
|
|
6)
|
chain |
A |
residue |
33-45 |
type |
prosite |
sequence |
KSSLGPVGLDKML
|
description |
TCP1_1 Chaperonins TCP-1 signature 1. RTcLGPkSmmKML
|
source |
prosite : PS00750
|
|
7)
|
chain |
H |
residue |
44-56 |
type |
prosite |
sequence |
RTAYGPNGMNKMV
|
description |
TCP1_1 Chaperonins TCP-1 signature 1. RTcLGPkSmmKML
|
source |
prosite : PS00750
|
|
8)
|
chain |
E |
residue |
49-61 |
type |
prosite |
sequence |
RTSLGPNGLDKMM
|
description |
TCP1_1 Chaperonins TCP-1 signature 1. RTcLGPkSmmKML
|
source |
prosite : PS00750
|
|
9)
|
chain |
B |
residue |
40-52 |
type |
prosite |
sequence |
KSTLGPKGMDKIL
|
description |
TCP1_1 Chaperonins TCP-1 signature 1. RTcLGPkSmmKML
|
source |
prosite : PS00750
|
|
10)
|
chain |
G |
residue |
37-49 |
type |
prosite |
sequence |
RTTLGPRGMDKLI
|
description |
TCP1_1 Chaperonins TCP-1 signature 1. RTcLGPkSmmKML
|
source |
prosite : PS00750
|
|
11)
|
chain |
C |
residue |
59-75 |
type |
prosite |
sequence |
MTNDGNAILREIQVQHP
|
description |
TCP1_2 Chaperonins TCP-1 signature 2. MTNDGNAILreIqVqHP
|
source |
prosite : PS00751
|
|
12)
|
chain |
D |
residue |
70-86 |
type |
prosite |
sequence |
ITNDGATILKQMQVLHP
|
description |
TCP1_2 Chaperonins TCP-1 signature 2. MTNDGNAILreIqVqHP
|
source |
prosite : PS00751
|
|
13)
|
chain |
F |
residue |
56-72 |
type |
prosite |
sequence |
LTKDGNVLLHEMQIQHP
|
description |
TCP1_2 Chaperonins TCP-1 signature 2. MTNDGNAILreIqVqHP
|
source |
prosite : PS00751
|
|
14)
|
chain |
A |
residue |
54-70 |
type |
prosite |
sequence |
ITNDGATILKLLEVEHP
|
description |
TCP1_2 Chaperonins TCP-1 signature 2. MTNDGNAILreIqVqHP
|
source |
prosite : PS00751
|
|
15)
|
chain |
H |
residue |
65-81 |
type |
prosite |
sequence |
VTNDAATILRELEVQHP
|
description |
TCP1_2 Chaperonins TCP-1 signature 2. MTNDGNAILreIqVqHP
|
source |
prosite : PS00751
|
|
16)
|
chain |
E |
residue |
70-86 |
type |
prosite |
sequence |
VTNDGATILSMMDVDHQ
|
description |
TCP1_2 Chaperonins TCP-1 signature 2. MTNDGNAILreIqVqHP
|
source |
prosite : PS00751
|
|
17)
|
chain |
B |
residue |
63-79 |
type |
prosite |
sequence |
VTNDGATILKNIGVDNP
|
description |
TCP1_2 Chaperonins TCP-1 signature 2. MTNDGNAILreIqVqHP
|
source |
prosite : PS00751
|
|
18)
|
chain |
G |
residue |
58-74 |
type |
prosite |
sequence |
ISNDGATILKLLDVVHP
|
description |
TCP1_2 Chaperonins TCP-1 signature 2. MTNDGNAILreIqVqHP
|
source |
prosite : PS00751
|
|
19)
|
chain |
C |
residue |
87-95 |
type |
prosite |
sequence |
QDEEVGDGT
|
description |
TCP1_3 Chaperonins TCP-1 signature 3. QDeeVGDGT
|
source |
prosite : PS00995
|
|
20)
|
chain |
D |
residue |
98-106 |
type |
prosite |
sequence |
QDIEAGDGT
|
description |
TCP1_3 Chaperonins TCP-1 signature 3. QDeeVGDGT
|
source |
prosite : PS00995
|
|
21)
|
chain |
F |
residue |
84-92 |
type |
prosite |
sequence |
QDDITGDGT
|
description |
TCP1_3 Chaperonins TCP-1 signature 3. QDeeVGDGT
|
source |
prosite : PS00995
|
|
22)
|
chain |
A |
residue |
82-90 |
type |
prosite |
sequence |
QDKEVGDGT
|
description |
TCP1_3 Chaperonins TCP-1 signature 3. QDeeVGDGT
|
source |
prosite : PS00995
|
|
23)
|
chain |
H |
residue |
93-101 |
type |
prosite |
sequence |
QEQEVGDGT
|
description |
TCP1_3 Chaperonins TCP-1 signature 3. QDeeVGDGT
|
source |
prosite : PS00995
|
|
24)
|
chain |
E |
residue |
98-106 |
type |
prosite |
sequence |
QDDEIGDGT
|
description |
TCP1_3 Chaperonins TCP-1 signature 3. QDeeVGDGT
|
source |
prosite : PS00995
|
|
25)
|
chain |
B |
residue |
91-99 |
type |
prosite |
sequence |
QDDEVGDGT
|
description |
TCP1_3 Chaperonins TCP-1 signature 3. QDeeVGDGT
|
source |
prosite : PS00995
|
|
26)
|
chain |
G |
residue |
86-94 |
type |
prosite |
sequence |
QDAEVGDGT
|
description |
TCP1_3 Chaperonins TCP-1 signature 3. QDeeVGDGT
|
source |
prosite : PS00995
|
|
27)
|
chain |
H |
residue |
23 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
28)
|
chain |
P |
residue |
23 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
29)
|
chain |
O |
residue |
67 |
type |
MOD_RES |
sequence |
K
|
description |
Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
30)
|
chain |
O |
residue |
320 |
type |
MOD_RES |
sequence |
K
|
description |
Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
31)
|
chain |
N |
residue |
199 |
type |
MOD_RES |
sequence |
K
|
description |
Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
32)
|
chain |
N |
residue |
365 |
type |
MOD_RES |
sequence |
K
|
description |
Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
33)
|
chain |
N |
residue |
377 |
type |
MOD_RES |
sequence |
K
|
description |
Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
34)
|
chain |
N |
residue |
388 |
type |
MOD_RES |
sequence |
K
|
description |
Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
35)
|
chain |
H |
residue |
30 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
36)
|
chain |
P |
residue |
30 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
37)
|
chain |
M |
residue |
346 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
38)
|
chain |
M |
residue |
539 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
39)
|
chain |
L |
residue |
288 |
type |
MOD_RES |
sequence |
K
|
description |
Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
40)
|
chain |
L |
residue |
302 |
type |
MOD_RES |
sequence |
K
|
description |
Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
41)
|
chain |
L |
residue |
319 |
type |
MOD_RES |
sequence |
K
|
description |
Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
42)
|
chain |
L |
residue |
326 |
type |
MOD_RES |
sequence |
K
|
description |
Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
43)
|
chain |
H |
residue |
162 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
44)
|
chain |
M |
residue |
214 |
type |
MOD_RES |
sequence |
K
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
45)
|
chain |
M |
residue |
265 |
type |
MOD_RES |
sequence |
K
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
46)
|
chain |
M |
residue |
275 |
type |
MOD_RES |
sequence |
K
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
47)
|
chain |
M |
residue |
279 |
type |
MOD_RES |
sequence |
K
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
48)
|
chain |
M |
residue |
392 |
type |
MOD_RES |
sequence |
K
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
49)
|
chain |
H |
residue |
213 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
50)
|
chain |
H |
residue |
269 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
51)
|
chain |
H |
residue |
317 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
52)
|
chain |
P |
residue |
162 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
53)
|
chain |
P |
residue |
213 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
54)
|
chain |
P |
residue |
269 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
55)
|
chain |
P |
residue |
317 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
56)
|
chain |
H |
residue |
318 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
57)
|
chain |
H |
residue |
400 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
58)
|
chain |
H |
residue |
466 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
59)
|
chain |
P |
residue |
318 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
60)
|
chain |
P |
residue |
400 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
61)
|
chain |
P |
residue |
466 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
62)
|
chain |
H |
residue |
505 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0007744|PubMed:15592455
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
63)
|
chain |
P |
residue |
505 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0007744|PubMed:15592455
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
64)
|
chain |
J |
residue |
248 |
type |
MOD_RES |
sequence |
K
|
description |
Phosphotyrosine => ECO:0007744|PubMed:15592455
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
65)
|
chain |
H |
residue |
224 |
type |
CROSSLNK |
sequence |
K
|
description |
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
66)
|
chain |
H |
residue |
254 |
type |
CROSSLNK |
sequence |
K
|
description |
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
67)
|
chain |
H |
residue |
260 |
type |
CROSSLNK |
sequence |
K
|
description |
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
68)
|
chain |
P |
residue |
224 |
type |
CROSSLNK |
sequence |
K
|
description |
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
69)
|
chain |
P |
residue |
254 |
type |
CROSSLNK |
sequence |
K
|
description |
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
70)
|
chain |
P |
residue |
260 |
type |
CROSSLNK |
sequence |
K
|
description |
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
71)
|
chain |
C |
residue |
430 |
type |
CROSSLNK |
sequence |
T
|
description |
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
72)
|
chain |
H |
residue |
459 |
type |
CROSSLNK |
sequence |
K
|
description |
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
73)
|
chain |
K |
residue |
430 |
type |
CROSSLNK |
sequence |
T
|
description |
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
74)
|
chain |
P |
residue |
459 |
type |
CROSSLNK |
sequence |
K
|
description |
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
75)
|
chain |
C |
residue |
248 |
type |
CROSSLNK |
sequence |
K
|
description |
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
76)
|
chain |
C |
residue |
249 |
type |
CROSSLNK |
sequence |
K
|
description |
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
77)
|
chain |
K |
residue |
15 |
type |
CROSSLNK |
sequence |
K
|
description |
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
78)
|
chain |
K |
residue |
248 |
type |
CROSSLNK |
sequence |
K
|
description |
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
79)
|
chain |
K |
residue |
249 |
type |
CROSSLNK |
sequence |
K
|
description |
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
80)
|
chain |
C |
residue |
381 |
type |
CROSSLNK |
sequence |
K
|
description |
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25114211
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
81)
|
chain |
K |
residue |
381 |
type |
CROSSLNK |
sequence |
K
|
description |
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25114211
|
source |
Swiss-Prot : SWS_FT_FI9
|
|