1U35
Crystal structure of the nucleosome core particle containing the histone domain of macroH2A
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 | 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 | 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 | 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 | 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 | LYS414-LEU420 |
site_id | PS00357 |
Number of Residues | 23 |
Details | HISTONE_H2B Histone H2B signature. REVQTavRlLLpGELaKHAVSEG |
Chain | Residue | Details |
D | ARG1289-GLY1311 |
site_id | PS00959 |
Number of Residues | 9 |
Details | HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI |
Chain | Residue | Details |
A | PRO466-ILE474 |
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 |
D | PRO1198 | |
H | PRO1398 | |
G | LYS1009 | |
G | LYS1011 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: ADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:P33778 |
Chain | Residue | Details |
D | GLU1199 | |
H | GLU1399 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: ADP-ribosylserine => ECO:0000250|UniProtKB:P33778 |
Chain | Residue | Details |
D | SER1203 | |
H | SER1403 |
site_id | SWS_FT_FI4 |
Number of Residues | 10 |
Details | MOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 |
Chain | Residue | Details |
D | LYS1208 | |
H | LYS1482 | |
D | LYS1212 | |
D | LYS1213 | |
D | LYS1217 | |
D | LYS1282 | |
H | LYS1408 | |
H | LYS1412 | |
H | LYS1413 | |
H | LYS1417 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-crotonyllysine; alternate => ECO:0000269|PubMed:21925322 |
Chain | Residue | Details |
D | LYS1209 | |
H | LYS1409 | |
B | ARG35 | |
G | LYS1119 | |
F | GLY207 | |
F | ARG235 |
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 |
D | SER1211 | |
H | SER1411 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P33778 |
Chain | Residue | Details |
D | LYS1220 | |
D | LYS1240 | |
H | LYS1420 | |
H | LYS1440 | |
F | ASP268 | |
F | VAL270 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:24681537 |
Chain | Residue | Details |
D | LYS1221 | |
H | LYS1421 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P33778 |
Chain | Residue | Details |
D | LYS1231 | |
D | LYS1313 | |
H | LYS1431 | |
H | LYS1513 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000269|PubMed:32822587 |
Chain | Residue | Details |
D | GLU1232 | |
H | GLU1432 | |
E | ALA615 | |
E | ASP723 |
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 | SER1233 | |
H | SER1433 |
site_id | SWS_FT_FI12 |
Number of Residues | 4 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62807 |
Chain | Residue | Details |
D | LYS1243 | |
D | LYS1305 | |
H | LYS1443 | |
H | LYS1505 |
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 | LYS1254 | |
H | LYS1454 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | MOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08 |
Chain | Residue | Details |
D | ARG1276 | |
H | ARG1476 | |
B | ILE50 | |
B | VAL70 | |
F | ARG203 | |
F | GLY211 | |
F | ILE250 | |
F | VAL270 |
site_id | SWS_FT_FI15 |
Number of Residues | 4 |
Details | MOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 |
Chain | Residue | Details |
D | ARG1283 | |
D | ARG1289 | |
H | ARG1483 | |
H | ARG1489 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q00729 |
Chain | Residue | Details |
D | THR1312 | |
H | THR1512 |
site_id | SWS_FT_FI17 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 |
Chain | Residue | Details |
D | LYS1317 | |
H | LYS1517 | |
E | SER657 | |
E | THR680 |
site_id | SWS_FT_FI18 |
Number of Residues | 2 |
Details | CARBOHYD: O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 |
Chain | Residue | Details |
D | SER1309 | |
H | SER1509 |
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 | LYS1217 | |
H | LYS1417 |
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 |
A | SER487 | |
D | LYS1317 | |
H | LYS1517 |
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 | LYS1231 | |
H | LYS1431 |
site_id | SWS_FT_FI22 |
Number of Residues | 2 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
A | ARG516 | |
E | ARG716 |
site_id | SWS_FT_FI23 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoarginine => ECO:0000305 |
Chain | Residue | Details |
A | ARG529 | |
A | ILE530 | |
E | ARG729 | |
E | ILE730 |
site_id | SWS_FT_FI24 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoarginine => ECO:0000255 |
Chain | Residue | Details |
A | GLY532 | |
E | GLY732 |
site_id | SWS_FT_FI25 |
Number of Residues | 2 |
Details | LIPID: N6-decanoyllysine => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
A | GLN419 | |
E | GLN619 |