6UPK
Structure of FACT_subnucleosome complex 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 | 0010467 | biological_process | gene expression |
A | 0016020 | cellular_component | membrane |
A | 0030527 | molecular_function | structural constituent of chromatin |
A | 0032200 | biological_process | telomere organization |
A | 0032991 | cellular_component | protein-containing complex |
A | 0040029 | biological_process | epigenetic regulation of gene expression |
A | 0043229 | cellular_component | intracellular organelle |
A | 0045296 | molecular_function | cadherin binding |
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 | 0003674 | molecular_function | molecular_function |
C | 0003677 | molecular_function | DNA binding |
C | 0005515 | molecular_function | protein binding |
C | 0005634 | cellular_component | nucleus |
C | 0005654 | cellular_component | nucleoplasm |
C | 0005694 | cellular_component | chromosome |
C | 0008285 | biological_process | negative regulation of cell population proliferation |
C | 0030527 | molecular_function | structural constituent of chromatin |
C | 0031492 | molecular_function | nucleosomal DNA binding |
C | 0031507 | biological_process | heterochromatin formation |
C | 0043229 | cellular_component | intracellular organelle |
C | 0046982 | molecular_function | protein heterodimerization activity |
C | 0070062 | cellular_component | extracellular exosome |
D | 0000786 | cellular_component | nucleosome |
D | 0002227 | biological_process | innate immune response in mucosa |
D | 0003677 | molecular_function | DNA binding |
D | 0005515 | molecular_function | protein binding |
D | 0005615 | cellular_component | extracellular space |
D | 0005634 | cellular_component | nucleus |
D | 0005654 | cellular_component | nucleoplasm |
D | 0005694 | cellular_component | chromosome |
D | 0005829 | cellular_component | cytosol |
D | 0006334 | biological_process | nucleosome assembly |
D | 0019731 | biological_process | antibacterial humoral response |
D | 0030527 | molecular_function | structural constituent of chromatin |
D | 0042742 | biological_process | defense response to bacterium |
D | 0042802 | molecular_function | identical protein binding |
D | 0043229 | cellular_component | intracellular organelle |
D | 0046982 | molecular_function | protein heterodimerization activity |
D | 0050830 | biological_process | defense response to Gram-positive bacterium |
D | 0061844 | biological_process | antimicrobial humoral immune response mediated by antimicrobial peptide |
D | 0070062 | cellular_component | extracellular exosome |
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 | 0010467 | biological_process | gene expression |
E | 0016020 | cellular_component | membrane |
E | 0030527 | molecular_function | structural constituent of chromatin |
E | 0032200 | biological_process | telomere organization |
E | 0032991 | cellular_component | protein-containing complex |
E | 0040029 | biological_process | epigenetic regulation of gene expression |
E | 0043229 | cellular_component | intracellular organelle |
E | 0045296 | molecular_function | cadherin binding |
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 | 0035101 | cellular_component | FACT complex |
H | 0003677 | molecular_function | DNA binding |
H | 0003682 | molecular_function | chromatin binding |
H | 0003723 | molecular_function | RNA binding |
H | 0005515 | molecular_function | protein binding |
H | 0005634 | cellular_component | nucleus |
H | 0005654 | cellular_component | nucleoplasm |
H | 0005694 | cellular_component | chromosome |
H | 0005730 | cellular_component | nucleolus |
H | 0006260 | biological_process | DNA replication |
H | 0006281 | biological_process | DNA repair |
H | 0006334 | biological_process | nucleosome assembly |
H | 0006337 | biological_process | nucleosome disassembly |
H | 0031491 | molecular_function | nucleosome binding |
H | 0035101 | cellular_component | FACT complex |
H | 0042393 | molecular_function | histone binding |
H | 1902275 | biological_process | regulation of chromatin organization |
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 | 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 | ARG92-GLY114 |
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 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 68 |
Details | DNA_BIND: HMG box => ECO:0000255|PROSITE-ProRule:PRU00267 |
Chain | Residue | Details |
H | PRO547-GLU615 | |
F | LYS16-LYS20 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | SITE: Cleavage; by caspase-3 and/or caspase-7 |
Chain | Residue | Details |
H | ASP450 | |
G | LYS196 | |
G | LYS223 | |
G | LYS732 | |
G | LYS786 | |
G | LYS904 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylalanine => ECO:0000269|Ref.3, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378 |
Chain | Residue | Details |
H | ALA2 | |
D | LYS11 | |
D | LYS15 | |
D | LYS16 | |
D | LYS20 | |
D | LYS23 | |
D | LYS43 | |
D | LYS85 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231 |
Chain | Residue | Details |
H | THR170 | |
G | SER658 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
H | LYS233 | |
H | LYS413 | |
B | LYS44 | |
F | LYS8 | |
F | LYS16 | |
F | LYS44 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
Chain | Residue | Details |
H | SER437 | |
B | LYS31 | |
B | LYS77 | |
B | LYS91 | |
F | LYS12 | |
F | LYS31 | |
F | LYS77 | |
F | LYS91 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q08943 |
Chain | Residue | Details |
H | TYR441 | |
H | TYR452 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
H | SER444 | |
D | LYS116 | |
D | LYS120 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
H | SER471 | |
C | LYS119 | |
C | LYS125 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by CK2 => ECO:0000305|PubMed:15659405 |
Chain | Residue | Details |
H | SER510 | |
G | LYS647 | |
E | LYS14 | |
E | LYS56 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q08943 |
Chain | Residue | Details |
H | LYS542 | |
D | LYS108 |
site_id | SWS_FT_FI12 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
H | LYS90 | |
C | LYS119 | |
H | LYS296 | |
H | LYS364 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | MOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08 |
Chain | Residue | Details |
D | ARG79 | |
F | TYR88 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | MOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 |
Chain | Residue | Details |
D | ARG86 | |
D | ARG92 |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q00729 |
Chain | Residue | Details |
D | THR115 | |
B | LYS91 | |
F | LYS91 |
site_id | SWS_FT_FI16 |
Number of Residues | 1 |
Details | CARBOHYD: O-linked (GlcNAc) serine => ECO:0000269|PubMed:22121020 |
Chain | Residue | Details |
D | SER112 | |
B | LYS59 | |
B | LYS79 | |
F | LYS20 | |
F | LYS59 | |
F | LYS79 |
site_id | SWS_FT_FI17 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P58876 |
Chain | Residue | Details |
D | LYS5 | |
F | LYS31 |
site_id | SWS_FT_FI18 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:16713563, ECO:0000269|PubMed:22121020 |
Chain | Residue | Details |
A | LYS37 | |
D | LYS120 |
site_id | SWS_FT_FI19 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:Q5QNW6 |
Chain | Residue | Details |
D | LYS20 | |
E | TYR41 |
site_id | SWS_FT_FI20 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:21726816 |
Chain | Residue | Details |
D | LYS34 | |
E | SER57 |
site_id | SWS_FT_FI21 |
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_FI22 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:20850016 |
Chain | Residue | Details |
A | THR80 | |
E | THR80 |
site_id | SWS_FT_FI23 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
A | SER86 | |
E | SER86 |
site_id | SWS_FT_FI24 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | THR107 | |
E | THR107 |
site_id | SWS_FT_FI25 |
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_FI26 |
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_FI27 |
Number of Residues | 2 |
Details | LIPID: N6-decanoyllysine => ECO:0000269|PubMed:35939806 |
Chain | Residue | Details |
A | LYS18 | |
E | LYS18 |