5KDM
Crystal structure of EBV tegument protein BNRF1 in complex with histone chaperone DAXX and histones H3.3-H4
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000775 | cellular_component | chromosome, centromeric region |
| A | 0000781 | cellular_component | chromosome, telomeric region |
| A | 0000785 | cellular_component | chromatin |
| A | 0000786 | cellular_component | nucleosome |
| A | 0000939 | cellular_component | inner kinetochore |
| A | 0000978 | molecular_function | RNA polymerase II cis-regulatory region sequence-specific DNA binding |
| A | 0000979 | molecular_function | RNA polymerase II core promoter sequence-specific DNA binding |
| A | 0001556 | biological_process | oocyte maturation |
| A | 0001649 | biological_process | osteoblast differentiation |
| A | 0001740 | cellular_component | Barr body |
| 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 | 0006334 | biological_process | nucleosome assembly |
| A | 0006997 | biological_process | nucleus organization |
| A | 0007283 | biological_process | spermatogenesis |
| A | 0007286 | biological_process | spermatid development |
| A | 0007338 | biological_process | single fertilization |
| A | 0007566 | biological_process | embryo implantation |
| A | 0008283 | biological_process | cell population proliferation |
| A | 0008584 | biological_process | male gonad development |
| A | 0030307 | biological_process | positive regulation of cell growth |
| A | 0030527 | molecular_function | structural constituent of chromatin |
| A | 0031492 | molecular_function | nucleosomal DNA binding |
| A | 0031508 | biological_process | pericentric heterochromatin formation |
| A | 0031509 | biological_process | subtelomeric heterochromatin formation |
| A | 0032200 | biological_process | telomere organization |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0035264 | biological_process | multicellular organism growth |
| A | 0042692 | biological_process | muscle cell differentiation |
| A | 0043229 | cellular_component | intracellular organelle |
| A | 0046982 | molecular_function | protein heterodimerization activity |
| A | 0048477 | biological_process | oogenesis |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0090230 | biological_process | regulation of centromere complex assembly |
| A | 1902340 | biological_process | negative regulation of chromosome condensation |
| 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 | 0042393 | molecular_function | histone binding |
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 | 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 | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| C | SER178 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
| Chain | Residue | Details |
| C | SER213 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate => ECO:0000250|UniProtKB:P62806 |
| Chain | Residue | Details |
| B | ARG3 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 |
| Chain | Residue | Details |
| B | LYS5 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | MOD_RES: N6-propionyllysine; alternate => ECO:0000269|PubMed:17267393 |
| Chain | Residue | Details |
| B | LYS8 | |
| B | LYS16 | |
| B | LYS44 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 |
| Chain | Residue | Details |
| B | LYS91 | |
| B | LYS12 | |
| B | LYS31 | |
| B | LYS77 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:15964846, ECO:0000269|PubMed:17967882, ECO:0000269|PubMed:27338793 |
| Chain | Residue | Details |
| B | LYS20 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PAK2 => ECO:0000269|PubMed:21724829, ECO:0007744|PubMed:17081983, 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 |
| B | SER47 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:20068231 |
| Chain | Residue | Details |
| B | TYR51 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 |
| Chain | Residue | Details |
| B | LYS59 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62806 |
| Chain | Residue | Details |
| A | LYS56 | |
| B | LYS79 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P62806 |
| Chain | Residue | Details |
| B | THR80 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| B | TYR88 | |
| A | LYS64 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447 |
| Chain | Residue | Details |
| B | LYS12 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:19818714 |
| Chain | Residue | Details |
| A | ARG26 | |
| B | LYS91 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 3 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| B | LYS59 | |
| B | LYS79 | |
| B | LYS20 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 1 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000269|PubMed:30886146 |
| Chain | Residue | Details |
| B | LYS31 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:15851689, ECO:0000269|PubMed:16185088 |
| Chain | Residue | Details |
| A | SER31 |
| site_id | SWS_FT_FI19 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68431 |
| Chain | Residue | Details |
| A | LYS37 |
| site_id | SWS_FT_FI20 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:19783980 |
| Chain | Residue | Details |
| A | TYR41 |
| site_id | SWS_FT_FI21 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:20850016 |
| Chain | Residue | Details |
| A | SER57 |
| site_id | SWS_FT_FI22 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:29211711 |
| Chain | Residue | Details |
| A | LYS79 |
| site_id | SWS_FT_FI23 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:20850016 |
| Chain | Residue | Details |
| A | THR80 |
| site_id | SWS_FT_FI24 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER86 |
| site_id | SWS_FT_FI25 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 |
| Chain | Residue | Details |
| A | THR107 |
| site_id | SWS_FT_FI26 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 |
| Chain | Residue | Details |
| A | LYS115 |
| site_id | SWS_FT_FI27 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229 |
| Chain | Residue | Details |
| A | LYS122 |
| site_id | SWS_FT_FI28 |
| Number of Residues | 1 |
| Details | LIPID: N6-decanoyllysine => ECO:0000269|PubMed:35939806 |
| Chain | Residue | Details |
| A | LYS18 |
