5B1L
The mouse nucleosome structure containing H3t
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 | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005694 | cellular_component | chromosome |
A | 0006325 | biological_process | chromatin organization |
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 | 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 |
C | 0070828 | biological_process | heterochromatin organization |
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 | 0005515 | molecular_function | protein binding |
E | 0005634 | cellular_component | nucleus |
E | 0005654 | cellular_component | nucleoplasm |
E | 0005694 | cellular_component | chromosome |
E | 0006325 | biological_process | chromatin organization |
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 | 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 |
G | 0070828 | biological_process | heterochromatin organization |
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 PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | binding site for residue CL A 301 |
Chain | Residue |
A | PRO121 |
A | LYS122 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue CL C 301 |
Chain | Residue |
C | GLY44 |
C | GLY46 |
C | ALA47 |
D | THR90 |
D | SER91 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue MN D 301 |
Chain | Residue |
D | HOH402 |
D | HOH409 |
E | ASP77 |
E | HOH412 |
C | HOH409 |
D | VAL48 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue CL E 301 |
Chain | Residue |
E | PRO121 |
E | LYS122 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue CL G 301 |
Chain | Residue |
G | GLY44 |
G | GLY46 |
G | ALA47 |
H | SER91 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue MN I 301 |
Chain | Residue |
I | DG121 |
I | HOH406 |
I | HOH435 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue MN I 302 |
Chain | Residue |
I | HOH414 |
I | HOH441 |
J | HOH511 |
J | HOH538 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue MN I 303 |
Chain | Residue |
I | DG134 |
I | HOH432 |
I | HOH437 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue MN I 304 |
Chain | Residue |
I | DG68 |
I | HOH409 |
J | HOH517 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue MN I 305 |
Chain | Residue |
I | HOH419 |
J | HOH540 |
site_id | AD2 |
Number of Residues | 1 |
Details | binding site for residue MN I 306 |
Chain | Residue |
I | DA17 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue MN J 401 |
Chain | Residue |
J | DG267 |
J | HOH505 |
J | HOH532 |
J | HOH537 |
J | HOH545 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue MN J 402 |
Chain | Residue |
J | DG185 |
J | DG186 |
J | HOH522 |
J | HOH530 |
J | HOH531 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue MN J 403 |
Chain | Residue |
J | DG280 |
J | HOH519 |
J | HOH544 |
site_id | AD6 |
Number of Residues | 2 |
Details | binding site for residue MN J 404 |
Chain | Residue |
J | DT183 |
J | HOH541 |
site_id | AD7 |
Number of Residues | 2 |
Details | binding site for residue MN J 405 |
Chain | Residue |
J | DG217 |
J | HOH502 |
site_id | AD8 |
Number of Residues | 1 |
Details | binding site for residue MN J 406 |
Chain | Residue |
J | HOH542 |
Functional Information from PROSITE/UniProt
site_id | PS00322 |
Number of Residues | 7 |
Details | HISTONE_H3_1 Histone H3 signature 1. KAPRKQL |
Chain | Residue | Details |
A | LYS14-LEU20 |
site_id | PS00959 |
Number of Residues | 9 |
Details | HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI |
Chain | Residue | Details |
A | PRO66-ILE74 |
site_id | PS00357 |
Number of Residues | 23 |
Details | HISTONE_H2B Histone H2B signature. REVQTavRlLLpGELaKHAVSEG |
Chain | Residue | Details |
D | ARG92-GLY114 |
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 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoarginine; alternate => ECO:0000305 |
Chain | Residue | Details |
A | ARG2 | |
E | ARG2 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610 |
Chain | Residue | Details |
A | THR3 | |
E | THR3 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:11747826, ECO:0000269|PubMed:17194708 |
Chain | Residue | Details |
E | LYS4 | |
A | LYS4 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594 |
Chain | Residue | Details |
D | LYS85 | |
H | LYS11 | |
H | LYS15 | |
H | LYS16 | |
H | LYS20 | |
H | LYS85 | |
A | GLN5 | |
E | GLN5 | |
D | LYS16 | |
D | LYS20 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by PKC => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
B | LYS44 | |
A | THR6 | |
E | THR6 | |
F | LYS8 | |
F | LYS16 | |
F | LYS44 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000269|PubMed:15485929 |
Chain | Residue | Details |
G | LYS74 | |
G | LYS75 | |
A | ARG8 | |
E | ARG8 |
site_id | SWS_FT_FI7 |
Number of Residues | 6 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:13678296, ECO:0000269|PubMed:17194708 |
Chain | Residue | Details |
A | LYS36 | |
E | LYS9 | |
E | LYS27 | |
E | LYS36 | |
A | LYS9 | |
A | LYS27 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:15735677, ECO:0000269|PubMed:15870105 |
Chain | Residue | Details |
A | SER10 | |
E | SER10 | |
G | LYS118 | |
C | LYS125 | |
G | LYS119 | |
G | LYS125 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by PKC and CHEK1 => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
A | THR11 | |
E | THR11 | |
H | LYS34 | |
H | LYS116 |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
A | LYS14 | |
A | LYS122 | |
E | LYS14 | |
E | LYS122 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: Citrulline; alternate => ECO:0000269|PubMed:15339660 |
Chain | Residue | Details |
A | ARG17 | |
E | ARG17 | |
G | LYS119 |
site_id | SWS_FT_FI12 |
Number of Residues | 4 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:17194708 |
Chain | Residue | Details |
E | LYS18 | |
A | LYS18 | |
A | LYS23 | |
E | LYS23 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | MOD_RES: Citrulline => ECO:0000269|PubMed:15339660 |
Chain | Residue | Details |
A | ARG26 | |
E | ARG26 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11441012, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:15684425, ECO:0000269|PubMed:15735677, ECO:0000269|PubMed:15870105 |
Chain | Residue | Details |
E | SER28 | |
A | SER28 |
site_id | SWS_FT_FI15 |
Number of Residues | 4 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
F | LYS12 | |
F | LYS20 | |
F | LYS59 | |
F | LYS79 | |
A | LYS37 | |
A | LYS64 | |
E | LYS37 | |
E | LYS64 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
F | LYS91 | |
E | TYR41 | |
A | TYR41 |
site_id | SWS_FT_FI17 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 |
Chain | Residue | Details |
A | LYS56 | |
A | LYS79 | |
E | LYS56 | |
E | LYS79 |
site_id | SWS_FT_FI18 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
A | SER57 | |
E | SER57 |
site_id | SWS_FT_FI19 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
A | THR80 | |
E | THR80 |
site_id | SWS_FT_FI20 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
H | LYS120 | |
A | SER86 | |
E | SER86 |
site_id | SWS_FT_FI21 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | THR107 | |
E | THR107 |
site_id | SWS_FT_FI22 |
Number of Residues | 2 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
A | LYS115 | |
E | LYS115 |
site_id | SWS_FT_FI23 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoarginine => ECO:0000305 |
Chain | Residue | Details |
A | ARG128 | |
A | ARG129 | |
E | ARG128 | |
E | ARG129 |
site_id | SWS_FT_FI24 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoarginine => ECO:0000255 |
Chain | Residue | Details |
A | ARG131 | |
E | ARG131 |
site_id | SWS_FT_FI25 |
Number of Residues | 2 |
Details | LIPID: N6-decanoyllysine => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
A | LYS18 | |
E | LYS18 |