8AAG
H1-bound palindromic nucleosome, state 1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000786 | cellular_component | nucleosome |
A | 0003677 | molecular_function | DNA binding |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005694 | cellular_component | chromosome |
A | 0006325 | biological_process | chromatin organization |
A | 0006334 | biological_process | nucleosome assembly |
A | 0030527 | molecular_function | structural constituent of chromatin |
A | 0046982 | molecular_function | protein heterodimerization activity |
A | 0070062 | cellular_component | extracellular exosome |
B | 0000781 | cellular_component | chromosome, telomeric region |
B | 0000786 | cellular_component | nucleosome |
B | 0003677 | molecular_function | DNA binding |
B | 0003723 | molecular_function | RNA binding |
B | 0005515 | molecular_function | protein binding |
B | 0005576 | cellular_component | extracellular region |
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 | 0016020 | cellular_component | membrane |
B | 0030527 | molecular_function | structural constituent of chromatin |
B | 0032200 | biological_process | telomere organization |
B | 0032991 | cellular_component | protein-containing complex |
B | 0043505 | cellular_component | CENP-A containing nucleosome |
B | 0045653 | biological_process | negative regulation of megakaryocyte differentiation |
B | 0046982 | molecular_function | protein heterodimerization activity |
B | 0061644 | biological_process | protein localization to CENP-A containing chromatin |
B | 0070062 | cellular_component | extracellular exosome |
C | 0000786 | cellular_component | nucleosome |
C | 0003677 | molecular_function | DNA binding |
C | 0005634 | cellular_component | nucleus |
C | 0005694 | cellular_component | chromosome |
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 | 0005515 | molecular_function | protein binding |
D | 0005634 | cellular_component | nucleus |
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 | 0005515 | molecular_function | protein binding |
E | 0005576 | cellular_component | extracellular region |
E | 0005634 | cellular_component | nucleus |
E | 0005654 | cellular_component | nucleoplasm |
E | 0005694 | cellular_component | chromosome |
E | 0006325 | biological_process | chromatin organization |
E | 0006334 | biological_process | nucleosome assembly |
E | 0030527 | molecular_function | structural constituent of chromatin |
E | 0046982 | molecular_function | protein heterodimerization activity |
E | 0070062 | cellular_component | extracellular exosome |
F | 0000781 | cellular_component | chromosome, telomeric region |
F | 0000786 | cellular_component | nucleosome |
F | 0003677 | molecular_function | DNA binding |
F | 0003723 | molecular_function | RNA binding |
F | 0005515 | molecular_function | protein binding |
F | 0005576 | cellular_component | extracellular region |
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 | 0016020 | cellular_component | membrane |
F | 0030527 | molecular_function | structural constituent of chromatin |
F | 0032200 | biological_process | telomere organization |
F | 0032991 | cellular_component | protein-containing complex |
F | 0043505 | cellular_component | CENP-A containing nucleosome |
F | 0045653 | biological_process | negative regulation of megakaryocyte differentiation |
F | 0046982 | molecular_function | protein heterodimerization activity |
F | 0061644 | biological_process | protein localization to CENP-A containing chromatin |
F | 0070062 | cellular_component | extracellular exosome |
G | 0000786 | cellular_component | nucleosome |
G | 0003677 | molecular_function | DNA binding |
G | 0005634 | cellular_component | nucleus |
G | 0005694 | cellular_component | chromosome |
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 | 0005515 | molecular_function | protein binding |
H | 0005634 | cellular_component | nucleus |
H | 0005694 | cellular_component | chromosome |
H | 0030527 | molecular_function | structural constituent of chromatin |
H | 0046982 | molecular_function | protein heterodimerization activity |
Z | 0000786 | cellular_component | nucleosome |
Z | 0003677 | molecular_function | DNA binding |
Z | 0003690 | molecular_function | double-stranded DNA binding |
Z | 0005634 | cellular_component | nucleus |
Z | 0005694 | cellular_component | chromosome |
Z | 0006334 | biological_process | nucleosome assembly |
Z | 0030261 | biological_process | chromosome condensation |
Z | 0030527 | molecular_function | structural constituent of chromatin |
Z | 0031492 | molecular_function | nucleosomal DNA binding |
Z | 0045910 | biological_process | negative regulation of DNA recombination |
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 | 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 | 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 | 8 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0C1H4 |
Chain | Residue | Details |
D | LYS2 | |
D | LYS9 | |
D | LYS12 | |
D | LYS17 | |
H | LYS2 | |
H | LYS9 | |
H | LYS12 | |
H | LYS17 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:12757711 |
Chain | Residue | Details |
D | SER11 | |
H | SER11 |
site_id | SWS_FT_FI3 |
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 | |
E | LYS18 | |
E | LYS64 |
site_id | SWS_FT_FI4 |
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 |
site_id | SWS_FT_FI5 |
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 | |
F | LYS16 | |
F | LYS44 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N5-methylglutamine => ECO:0000250 |
Chain | Residue | Details |
C | GLN104 | |
G | GLN104 | |
B | LYS77 | |
B | LYS91 | |
F | LYS12 | |
F | LYS31 | |
F | LYS77 | |
F | LYS91 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 |
Chain | Residue | Details |
C | LYS118 | |
G | LYS118 |
site_id | SWS_FT_FI8 |
Number of Residues | 8 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 |
Chain | Residue | Details |
C | LYS13 | |
E | SER10 | |
C | LYS15 | |
C | LYS119 | |
G | LYS13 | |
G | LYS15 | |
G | LYS119 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by PKC => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:22901803 |
Chain | Residue | Details |
A | THR11 | |
E | THR11 |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 |
Chain | Residue | Details |
A | LYS14 | |
A | LYS56 | |
E | LYS14 | |
E | LYS56 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: Citrulline; alternate => ECO:0000269|PubMed:15345777, ECO:0000269|PubMed:16497732, ECO:0000269|PubMed:16567635 |
Chain | Residue | Details |
A | ARG17 | |
E | ARG17 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:17194708 |
Chain | Residue | Details |
A | LYS23 | |
E | LYS23 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | MOD_RES: Citrulline => ECO:0000269|PubMed:16567635 |
Chain | Residue | Details |
A | ARG26 | |
E | ARG26 |
site_id | SWS_FT_FI14 |
Number of Residues | 4 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:17194708 |
Chain | Residue | Details |
A | LYS27 | |
A | LYS36 | |
E | LYS27 | |
E | LYS36 |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:15684425, ECO:0000269|PubMed:16185088 |
Chain | Residue | Details |
A | SER28 | |
E | SER28 | |
F | LYS91 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
A | LYS37 | |
E | LYS37 | |
B | LYS79 | |
F | LYS20 | |
F | LYS59 | |
F | LYS79 |
site_id | SWS_FT_FI17 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:19783980 |
Chain | Residue | Details |
A | TYR41 | |
E | TYR41 |
site_id | SWS_FT_FI18 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:20850016 |
Chain | Residue | Details |
A | SER57 | |
E | SER57 |
site_id | SWS_FT_FI19 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:29211711 |
Chain | Residue | Details |
A | LYS79 | |
E | LYS79 |
site_id | SWS_FT_FI20 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:20850016 |
Chain | Residue | Details |
A | THR80 | |
E | THR80 |
site_id | SWS_FT_FI21 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
A | SER86 | |
E | SER86 |
site_id | SWS_FT_FI22 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332 |
Chain | Residue | Details |
A | THR107 | |
E | THR107 |
site_id | SWS_FT_FI23 |
Number of Residues | 2 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 |
Chain | Residue | Details |
A | LYS115 | |
E | LYS115 |
site_id | SWS_FT_FI24 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229 |
Chain | Residue | Details |
A | LYS122 | |
E | LYS122 |
site_id | SWS_FT_FI25 |
Number of Residues | 2 |
Details | LIPID: N6-decanoyllysine => ECO:0000269|PubMed:35939806 |
Chain | Residue | Details |
A | LYS18 | |
E | LYS18 |
site_id | SWS_FT_FI26 |
Number of Residues | 2 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:21076176 |
Chain | Residue | Details |
A | CYS110 | |
E | CYS110 |