2IO5
Crystal structure of the CIA- histone H3-H4 complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005634 | cellular_component | nucleus |
A | 0006325 | biological_process | chromatin organization |
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 | 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 | 0005515 | molecular_function | protein binding |
C | 0005634 | cellular_component | nucleus |
C | 0005694 | cellular_component | chromosome |
C | 0006334 | biological_process | nucleosome assembly |
C | 0030527 | molecular_function | structural constituent of chromatin |
C | 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 |
C | GLY14-HIS18 |
site_id | PS00322 |
Number of Residues | 7 |
Details | HISTONE_H3_1 Histone H3 signature 1. KAPRKQL |
Chain | Residue | Details |
B | LYS14-LEU20 |
site_id | PS00959 |
Number of Residues | 9 |
Details | HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI |
Chain | Residue | Details |
B | PRO66-ILE74 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | DNA_BIND: |
Chain | Residue | Details |
C | ARG17-VAL21 | |
B | LYS18 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
C | GLY2 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
C | GLY4 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
C | GLY6 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
C | GLY9 | |
C | ARG17 | |
C | ARG45 | |
C | THR80 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
C | GLY13 | |
C | VAL21 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
C | PRO32 | |
C | ARG92 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
C | GLY48 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
C | GLU52 | |
C | ALA89 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
C | VAL60 | |
B | ALA24 | |
B | SER28 | |
B | LYS37 | |
B | LEU65 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
C | ARG78 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
C | PRO32 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
B | PRO38 | |
C | ARG92 |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
B | ARG42 |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 |
Chain | Residue | Details |
B | SER57 | |
B | THR80 |
site_id | SWS_FT_FI16 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
B | THR58 |
site_id | SWS_FT_FI17 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
B | ASP81 | |
B | ASN108 |
site_id | SWS_FT_FI18 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
B | SER87 |
site_id | SWS_FT_FI19 |
Number of Residues | 1 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
B | ARG116 |
site_id | SWS_FT_FI20 |
Number of Residues | 1 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
B | ASP123 |
site_id | SWS_FT_FI21 |
Number of Residues | 1 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
B | ALA111 |