|
|
1)
|
chain |
A |
residue |
5 |
type |
|
sequence |
C
|
description |
binding site for residue ZN A 101
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
7 |
type |
|
sequence |
C
|
description |
binding site for residue ZN A 101
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
27 |
type |
|
sequence |
H
|
description |
binding site for residue ZN A 101
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
30 |
type |
|
sequence |
C
|
description |
binding site for residue ZN A 101
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
19 |
type |
|
sequence |
C
|
description |
binding site for residue ZN A 102
|
source |
: AC2
|
|
6)
|
chain |
A |
residue |
22 |
type |
|
sequence |
C
|
description |
binding site for residue ZN A 102
|
source |
: AC2
|
|
7)
|
chain |
A |
residue |
45 |
type |
|
sequence |
C
|
description |
binding site for residue ZN A 102
|
source |
: AC2
|
|
8)
|
chain |
A |
residue |
48 |
type |
|
sequence |
C
|
description |
binding site for residue ZN A 102
|
source |
: AC2
|
|
9)
|
chain |
A |
residue |
44 |
type |
|
sequence |
L
|
description |
binding site for residue NA A 103
|
source |
: AC3
|
|
10)
|
chain |
A |
residue |
45 |
type |
|
sequence |
C
|
description |
binding site for residue NA A 103
|
source |
: AC3
|
|
11)
|
chain |
A |
residue |
49 |
type |
|
sequence |
D
|
description |
binding site for residue NA A 103
|
source |
: AC3
|
|
12)
|
chain |
A |
residue |
51 |
type |
|
sequence |
R
|
description |
binding site for residue NA A 103
|
source |
: AC3
|
|
13)
|
chain |
A |
residue |
5-48 |
type |
prosite |
sequence |
CICDLNDDDGFTIQCDHCNRWQHAICYGIKDIGMAPDDYL
CNSC
|
description |
ZF_PHD_1 Zinc finger PHD-type signature. Ci.Cdlndddgft....................................IqCdh..Cnrw.QHaiCygikdigmapdd.................................YlCnsC
|
source |
prosite : PS01359
|
|
14)
|
chain |
B |
residue |
2 |
type |
MOD_RES |
sequence |
R
|
description |
Citrulline; alternate => ECO:0000269|PubMed:16567635
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
15)
|
chain |
B |
residue |
3 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
16)
|
chain |
B |
residue |
4 |
type |
MOD_RES |
sequence |
X
|
description |
N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
17)
|
chain |
B |
residue |
5 |
type |
MOD_RES |
sequence |
Q
|
description |
5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
18)
|
chain |
B |
residue |
6 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
19)
|
chain |
B |
residue |
8 |
type |
MOD_RES |
sequence |
R
|
description |
Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
20)
|
chain |
B |
residue |
9 |
type |
MOD_RES |
sequence |
K
|
description |
N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
21)
|
chain |
B |
residue |
10 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16457588
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
22)
|
chain |
B |
residue |
11 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine; by PKC and CHEK1 => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:22901803
|
source |
Swiss-Prot : SWS_FT_FI9
|
|