6FQ6
Class 2 : distorted nucleosome
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000786 | cellular_component | nucleosome |
A | 0003677 | molecular_function | DNA binding |
A | 0030527 | molecular_function | structural constituent of chromatin |
A | 0046982 | molecular_function | protein heterodimerization activity |
B | 0003677 | molecular_function | DNA binding |
B | 0030527 | molecular_function | structural constituent of chromatin |
B | 0046982 | molecular_function | protein heterodimerization activity |
C | 0000786 | cellular_component | nucleosome |
C | 0003677 | molecular_function | DNA binding |
C | 0030527 | molecular_function | structural constituent of chromatin |
C | 0046982 | molecular_function | protein heterodimerization activity |
D | 0000786 | cellular_component | nucleosome |
D | 0003677 | molecular_function | DNA binding |
D | 0030527 | molecular_function | structural constituent of chromatin |
D | 0046982 | molecular_function | protein heterodimerization activity |
E | 0000786 | cellular_component | nucleosome |
E | 0003677 | molecular_function | DNA binding |
E | 0030527 | molecular_function | structural constituent of chromatin |
E | 0046982 | molecular_function | protein heterodimerization activity |
F | 0003677 | molecular_function | DNA binding |
F | 0030527 | molecular_function | structural constituent of chromatin |
F | 0046982 | molecular_function | protein heterodimerization activity |
G | 0000786 | cellular_component | nucleosome |
G | 0003677 | molecular_function | DNA binding |
G | 0030527 | molecular_function | structural constituent of chromatin |
G | 0046982 | molecular_function | protein heterodimerization activity |
H | 0000786 | cellular_component | nucleosome |
H | 0003677 | molecular_function | DNA binding |
H | 0030527 | molecular_function | structural constituent of chromatin |
H | 0046982 | molecular_function | protein heterodimerization activity |
Functional Information from PROSITE/UniProt
site_id | PS00046 |
Number of Residues | 7 |
Details | HISTONE_H2A Histone H2A signature. AGLqFPV |
Chain | Residue | Details |
C | ALA21-VAL27 |
site_id | PS00357 |
Number of Residues | 23 |
Details | HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG |
Chain | Residue | Details |
D | ARG89-GLY111 |
site_id | PS00959 |
Number of Residues | 9 |
Details | HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI |
Chain | Residue | Details |
A | PRO66-ILE74 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | CARBOHYD: O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 |
Chain | Residue | Details |
D | SER109 | |
H | SER109 | |
G | LYS9 | |
G | LYS95 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0C1H4 |
Chain | Residue | Details |
D | LYS117 | |
G | LYS36 | |
H | LYS117 | |
F | LYS91 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 |
Chain | Residue | Details |
C | LYS74 | |
C | LYS75 | |
G | LYS74 | |
G | LYS75 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N5-methylglutamine => ECO:0000250 |
Chain | Residue | Details |
C | GLN104 | |
G | GLN104 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 |
Chain | Residue | Details |
C | LYS118 | |
G | LYS118 | |
F | TYR51 | |
F | TYR88 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 |
Chain | Residue | Details |
C | LYS13 | |
A | THR107 | |
C | LYS15 | |
G | LYS13 | |
G | LYS15 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
A | SER86 | |
E | SER86 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | LYS115 | |
E | LYS115 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | LYS122 | |
E | LYS122 | |
F | LYS91 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | CYS110 | |
E | CYS110 |