7DBH
The mouse nucleosome structure containing H3mm18
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 | 0000786 | cellular_component | nucleosome |
B | 0003677 | molecular_function | DNA binding |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005694 | cellular_component | chromosome |
B | 0006325 | biological_process | chromatin organization |
B | 0006334 | biological_process | nucleosome assembly |
B | 0030527 | molecular_function | structural constituent of chromatin |
B | 0043505 | cellular_component | CENP-A containing nucleosome |
B | 0046982 | molecular_function | protein heterodimerization activity |
B | 0061644 | biological_process | protein localization to CENP-A containing chromatin |
C | 0000786 | cellular_component | nucleosome |
C | 0003677 | molecular_function | DNA binding |
C | 0005634 | cellular_component | nucleus |
C | 0005694 | cellular_component | chromosome |
C | 0006325 | biological_process | chromatin organization |
C | 0030527 | molecular_function | structural constituent of chromatin |
C | 0031492 | molecular_function | nucleosomal DNA binding |
C | 0031507 | biological_process | heterochromatin formation |
C | 0043505 | cellular_component | CENP-A containing nucleosome |
C | 0046982 | molecular_function | protein heterodimerization activity |
C | 0061644 | biological_process | protein localization to CENP-A containing chromatin |
D | 0000786 | cellular_component | nucleosome |
D | 0003677 | molecular_function | DNA binding |
D | 0005634 | cellular_component | nucleus |
D | 0005654 | cellular_component | nucleoplasm |
D | 0005694 | cellular_component | chromosome |
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 | 0000786 | cellular_component | nucleosome |
F | 0003677 | molecular_function | DNA binding |
F | 0005515 | molecular_function | protein binding |
F | 0005634 | cellular_component | nucleus |
F | 0005654 | cellular_component | nucleoplasm |
F | 0005694 | cellular_component | chromosome |
F | 0006325 | biological_process | chromatin organization |
F | 0006334 | biological_process | nucleosome assembly |
F | 0030527 | molecular_function | structural constituent of chromatin |
F | 0043505 | cellular_component | CENP-A containing nucleosome |
F | 0046982 | molecular_function | protein heterodimerization activity |
F | 0061644 | biological_process | protein localization to CENP-A containing chromatin |
G | 0000786 | cellular_component | nucleosome |
G | 0003677 | molecular_function | DNA binding |
G | 0005634 | cellular_component | nucleus |
G | 0005694 | cellular_component | chromosome |
G | 0006325 | biological_process | chromatin organization |
G | 0030527 | molecular_function | structural constituent of chromatin |
G | 0031492 | molecular_function | nucleosomal DNA binding |
G | 0031507 | biological_process | heterochromatin formation |
G | 0043505 | cellular_component | CENP-A containing nucleosome |
G | 0046982 | molecular_function | protein heterodimerization activity |
G | 0061644 | biological_process | protein localization to CENP-A containing chromatin |
H | 0000786 | cellular_component | nucleosome |
H | 0003677 | molecular_function | DNA binding |
H | 0005634 | cellular_component | nucleus |
H | 0005654 | cellular_component | nucleoplasm |
H | 0005694 | cellular_component | chromosome |
H | 0030527 | molecular_function | structural constituent of chromatin |
H | 0046982 | molecular_function | protein heterodimerization activity |
Functional Information from PROSITE/UniProt
site_id | PS00047 |
Number of Residues | 5 |
Details | HISTONE_H4 Histone H4 signature. GAKRH |
Chain | Residue | Details |
B | GLY14-HIS18 |
site_id | PS00322 |
Number of Residues | 7 |
Details | HISTONE_H3_1 Histone H3 signature 1. KAPRKQL |
Chain | Residue | Details |
A | LYS14-LEU20 |
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. REVQTavRlLLpGELaKHAVSEG |
Chain | Residue | Details |
D | ARG92-GLY114 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylproline => ECO:0000250|UniProtKB:P23527 |
Chain | Residue | Details |
H | PRO1 | |
D | PRO1 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: ADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:P33778 |
Chain | Residue | Details |
D | GLU2 | |
H | GLU2 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: ADP-ribosylserine => ECO:0000250|UniProtKB:P33778 |
Chain | Residue | Details |
H | SER6 | |
D | SER6 |
site_id | SWS_FT_FI4 |
Number of Residues | 10 |
Details | MOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 |
Chain | Residue | Details |
D | LYS85 | |
H | LYS11 | |
H | LYS15 | |
H | LYS16 | |
H | LYS20 | |
H | LYS85 | |
D | LYS16 | |
D | LYS20 | |
D | LYS11 | |
D | LYS15 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-crotonyllysine; alternate => ECO:0000269|PubMed:21925322 |
Chain | Residue | Details |
F | LYS16 | |
F | LYS44 | |
F | LYS8 | |
D | LYS12 | |
H | LYS12 | |
B | LYS44 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:15197225, ECO:0000269|PubMed:16039583 |
Chain | Residue | Details |
H | SER14 | |
D | SER14 | |
G | LYS74 | |
G | LYS75 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P33778 |
Chain | Residue | Details |
D | LYS43 | |
H | LYS23 | |
H | LYS43 | |
D | LYS23 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:24681537 |
Chain | Residue | Details |
G | LYS118 | |
G | LYS119 | |
G | LYS125 | |
D | LYS24 | |
H | LYS24 | |
C | LYS125 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P33778 |
Chain | Residue | Details |
D | LYS116 | |
H | LYS34 | |
H | LYS116 | |
D | LYS34 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000269|PubMed:32822587 |
Chain | Residue | Details |
G | LYS13 | |
G | LYS15 | |
D | GLU35 | |
H | GLU35 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by AMPK => ECO:0000269|PubMed:20647423, ECO:0000269|PubMed:32822587 |
Chain | Residue | Details |
D | SER36 | |
H | SER36 | |
G | LYS119 |
site_id | SWS_FT_FI12 |
Number of Residues | 4 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62807 |
Chain | Residue | Details |
D | LYS46 | |
D | LYS108 | |
H | LYS46 | |
H | LYS108 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537 |
Chain | Residue | Details |
D | LYS57 | |
H | LYS57 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | MOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08 |
Chain | Residue | Details |
D | ARG79 | |
H | ARG79 |
site_id | SWS_FT_FI15 |
Number of Residues | 4 |
Details | MOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 |
Chain | Residue | Details |
D | ARG86 | |
D | ARG92 | |
H | ARG86 | |
H | ARG92 | |
F | LYS12 | |
F | LYS20 | |
F | LYS59 | |
F | LYS79 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q00729 |
Chain | Residue | Details |
D | THR115 | |
H | THR115 | |
F | LYS91 |
site_id | SWS_FT_FI17 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 |
Chain | Residue | Details |
D | LYS120 | |
H | LYS120 |
site_id | SWS_FT_FI18 |
Number of Residues | 2 |
Details | CARBOHYD: O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 |
Chain | Residue | Details |
D | SER112 | |
H | SER112 |
site_id | SWS_FT_FI19 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:Q5QNW6 |
Chain | Residue | Details |
D | LYS20 | |
H | LYS20 |
site_id | SWS_FT_FI20 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62808 |
Chain | Residue | Details |
D | LYS120 | |
H | LYS120 |
site_id | SWS_FT_FI21 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P33778 |
Chain | Residue | Details |
D | LYS34 | |
H | LYS34 |