8ETV
Class2 of the INO80-Hexasome complex
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 | 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 | 0005694 | cellular_component | chromosome |
B | 0006334 | biological_process | nucleosome assembly |
B | 0030527 | molecular_function | structural constituent of chromatin |
B | 0046982 | molecular_function | protein heterodimerization activity |
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 | 0005634 | cellular_component | nucleus |
E | 0005654 | cellular_component | nucleoplasm |
E | 0005694 | cellular_component | chromosome |
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 | 0005694 | cellular_component | chromosome |
F | 0006334 | biological_process | nucleosome assembly |
F | 0030527 | molecular_function | structural constituent of chromatin |
F | 0046982 | molecular_function | protein heterodimerization activity |
Functional Information from PROSITE/UniProt
site_id | PS00046 |
Number of Residues | 7 |
Details | HISTONE_H2A Histone H2A signature. AGLqFPV |
Chain | Residue | Details |
C | ALA22-VAL28 |
site_id | PS00047 |
Number of Residues | 5 |
Details | HISTONE_H4 Histone H4 signature. GAKRH |
Chain | Residue | Details |
B | GLY15-HIS19 |
site_id | PS00322 |
Number of Residues | 7 |
Details | HISTONE_H3_1 Histone H3 signature 1. KAPRKQL |
Chain | Residue | Details |
A | LYS15-LEU21 |
site_id | PS00357 |
Number of Residues | 23 |
Details | HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG |
Chain | Residue | Details |
D | ARG90-GLY112 |
site_id | PS00959 |
Number of Residues | 9 |
Details | HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI |
Chain | Residue | Details |
A | PRO67-ILE75 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: Asymmetric dimethylarginine; by PRMT6 => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
A | ARG3 | |
D | LYS10 | |
D | LYS13 | |
D | LYS18 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by HASPIN => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
A | THR4 | |
F | SER2 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
A | LYS5 | |
F | ARG4 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: 5-glutamyl serotonin; alternate => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
A | GLN6 | |
F | LYS6 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by PKC => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
A | THR7 | |
A | THR12 | |
B | LYS45 | |
B | LYS80 | |
F | LYS9 | |
F | LYS17 | |
F | LYS45 | |
F | LYS80 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N6-methylated lysine => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
A | LYS10 | |
A | LYS65 | |
F | LYS13 | |
F | LYS21 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
A | SER11 | |
B | LYS92 | |
F | LYS32 | |
F | LYS92 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P68433 |
Chain | Residue | Details |
A | LYS15 | |
F | SER48 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Asymmetric dimethylarginine => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
A | ARG18 | |
B | TYR89 | |
F | TYR52 | |
F | TYR89 |
site_id | SWS_FT_FI10 |
Number of Residues | 3 |
Details | MOD_RES: N6-methylated lysine; alternate => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
A | LYS19 | |
A | LYS28 | |
A | LYS37 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
A | LYS24 | |
F | LYS78 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
A | TYR42 | |
F | LYS32 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84244 |
Chain | Residue | Details |
A | LYS57 | |
A | LYS80 | |
F | LYS92 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
A | SER58 | |
E | SER87 |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
A | THR81 |
site_id | SWS_FT_FI16 |
Number of Residues | 1 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
A | LYS116 |
site_id | SWS_FT_FI17 |
Number of Residues | 1 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
A | LYS123 |
site_id | SWS_FT_FI18 |
Number of Residues | 2 |
Details | MOD_RES: Citrulline; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
E | ARG3 | |
E | ARG18 |
site_id | SWS_FT_FI19 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by HASPIN and VRK1 => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
E | THR4 |
site_id | SWS_FT_FI20 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:12138181 |
Chain | Residue | Details |
E | LYS5 |
site_id | SWS_FT_FI21 |
Number of Residues | 1 |
Details | MOD_RES: 5-glutamyl serotonin; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
E | GLN6 |
site_id | SWS_FT_FI22 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by PKC => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
E | THR7 | |
E | THR12 |
site_id | SWS_FT_FI23 |
Number of Residues | 1 |
Details | MOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250 |
Chain | Residue | Details |
E | ARG9 |
site_id | SWS_FT_FI24 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000305|PubMed:12138181 |
Chain | Residue | Details |
E | LYS10 |
site_id | SWS_FT_FI25 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
E | SER11 |
site_id | SWS_FT_FI26 |
Number of Residues | 1 |
Details | MOD_RES: N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P84228 |
Chain | Residue | Details |
E | LYS15 |
site_id | SWS_FT_FI27 |
Number of Residues | 5 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
E | LYS19 | |
E | LYS24 | |
E | LYS28 | |
E | LYS37 | |
E | LYS65 |
site_id | SWS_FT_FI28 |
Number of Residues | 1 |
Details | MOD_RES: Citrulline => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
E | ARG27 |
site_id | SWS_FT_FI29 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
E | SER29 |
site_id | SWS_FT_FI30 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
E | LYS38 |
site_id | SWS_FT_FI31 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
E | TYR42 |
site_id | SWS_FT_FI32 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 |
Chain | Residue | Details |
E | LYS57 | |
E | LYS80 |
site_id | SWS_FT_FI33 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
E | SER58 |
site_id | SWS_FT_FI34 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
E | THR81 | |
E | THR108 |
site_id | SWS_FT_FI35 |
Number of Residues | 1 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
E | LYS116 |
site_id | SWS_FT_FI36 |
Number of Residues | 1 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
E | LYS123 |
site_id | SWS_FT_FI37 |
Number of Residues | 1 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
E | ALA111 |