|
|
1)
|
chain |
A |
residue |
125 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 215
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
128 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 215
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
159 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN A 215
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
162 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 215
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
125-162 |
type |
prosite |
sequence |
CKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGC
|
description |
ZF_PARP_1 Zinc finger poly(ADP-ribose) polymerase (PARP)-type signature. CKgCmekIeKgqvRlskkmvdpekpqlgmidrWYHpgC
|
source |
prosite : PS00347
|
|
6)
|
chain |
A |
residue |
113-203 |
type |
ZN_FING |
sequence |
FAAEYAKSNRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLG
MIDRWYHPGCFVKNREELGFRPEYSASQLKGFSLLATEDK
EALKKQLPGVK
|
description |
PARP-type 2 => ECO:0000255|PROSITE-ProRule:PRU00264
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
7)
|
chain |
A |
residue |
125 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00264, ECO:0000269|PubMed:21233213, ECO:0000269|PubMed:22683995, ECO:0007744|PDB:3ODC, ECO:0007744|PDB:3ODE, ECO:0007744|PDB:4AV1
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
8)
|
chain |
A |
residue |
128 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00264, ECO:0000269|PubMed:21233213, ECO:0000269|PubMed:22683995, ECO:0007744|PDB:3ODC, ECO:0007744|PDB:3ODE, ECO:0007744|PDB:4AV1
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
9)
|
chain |
A |
residue |
159 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00264, ECO:0000269|PubMed:21233213, ECO:0000269|PubMed:22683995, ECO:0007744|PDB:3ODC, ECO:0007744|PDB:3ODE, ECO:0007744|PDB:4AV1
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
10)
|
chain |
A |
residue |
162 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00264, ECO:0000269|PubMed:21233213, ECO:0000269|PubMed:22683995, ECO:0007744|PDB:3ODC, ECO:0007744|PDB:3ODE, ECO:0007744|PDB:4AV1
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
11)
|
chain |
A |
residue |
214 |
type |
SITE |
sequence |
D
|
description |
Cleavage; by caspase-3 and caspase-7 => ECO:0000269|PubMed:10497198, ECO:0000269|PubMed:22464733, ECO:0000269|PubMed:7596430
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
12)
|
chain |
A |
residue |
105 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
13)
|
chain |
A |
residue |
131 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
14)
|
chain |
A |
residue |
177 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
15)
|
chain |
A |
residue |
185 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
16)
|
chain |
A |
residue |
179 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
17)
|
chain |
A |
residue |
192 |
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_FI7
|
|
18)
|
chain |
A |
residue |
203 |
type |
CROSSLNK |
sequence |
K
|
description |
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733
|
source |
Swiss-Prot : SWS_FT_FI8
|
|