|
|
1)
|
chain |
B |
residue |
176 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN B 401
|
source |
: AC1
|
|
2)
|
chain |
B |
residue |
179 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN B 401
|
source |
: AC1
|
|
3)
|
chain |
B |
residue |
238 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN B 401
|
source |
: AC1
|
|
4)
|
chain |
B |
residue |
242 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN B 401
|
source |
: AC1
|
|
5)
|
chain |
B |
residue |
237-249 |
type |
prosite |
sequence |
MCNSSCMGGMNRR
|
description |
P53 p53 family signature. MCNSSCMGGMNRR
|
source |
prosite : PS00348
|
|
6)
|
chain |
A |
residue |
133-151 |
type |
prosite |
sequence |
LFRDGVNWGRIVAFFSFGG
|
description |
BH1 Apoptosis regulator, Bcl-2 family BH1 motif signature. LFrDGv.NWGRIVAFFsFGG
|
source |
prosite : PS01080
|
|
7)
|
chain |
A |
residue |
184-195 |
type |
prosite |
sequence |
WIQENGGWDTFV
|
description |
BH2 Apoptosis regulator, Bcl-2 family BH2 motif signature. WIqenGGWDtFV
|
source |
prosite : PS01258
|
|
8)
|
chain |
A |
residue |
89-103 |
type |
prosite |
sequence |
VKQALREAGDEFELR
|
description |
BH3 Apoptosis regulator, Bcl-2 family BH3 motif signature. VkqaLReAGDEFELR
|
source |
prosite : PS01259
|
|
9)
|
chain |
A |
residue |
7-27 |
type |
prosite |
sequence |
SNRELVVDFLSYKLSQKGYSW
|
description |
BH4_1 Apoptosis regulator, Bcl-2 family BH4 motif signature. SNRELVvDFLSYKLSQKGYsW
|
source |
prosite : PS01260
|
|
10)
|
chain |
B |
residue |
176 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000269|PubMed:14534297, ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:17015838, ECO:0000269|PubMed:18650397, ECO:0000269|PubMed:19515728, ECO:0000269|PubMed:20142040, ECO:0000269|PubMed:20364130
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
11)
|
chain |
B |
residue |
179 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000269|PubMed:14534297, ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:17015838, ECO:0000269|PubMed:18650397, ECO:0000269|PubMed:19515728, ECO:0000269|PubMed:20142040, ECO:0000269|PubMed:20364130
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
12)
|
chain |
B |
residue |
238 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000269|PubMed:14534297, ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:17015838, ECO:0000269|PubMed:18650397, ECO:0000269|PubMed:19515728, ECO:0000269|PubMed:20142040, ECO:0000269|PubMed:20364130
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
13)
|
chain |
B |
residue |
242 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000269|PubMed:14534297, ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:17015838, ECO:0000269|PubMed:18650397, ECO:0000269|PubMed:19515728, ECO:0000269|PubMed:20142040, ECO:0000269|PubMed:20364130
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
14)
|
chain |
B |
residue |
120 |
type |
SITE |
sequence |
K
|
description |
Interaction with DNA => ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
15)
|
chain |
B |
residue |
120 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0000269|PubMed:17189187, ECO:0000269|PubMed:19854137, ECO:0000269|PubMed:23431171
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
16)
|
chain |
B |
residue |
183 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
17)
|
chain |
B |
residue |
269 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
18)
|
chain |
B |
residue |
284 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462
|
source |
Swiss-Prot : SWS_FT_FI6
|
|