8XBW
The cryo-EM structure of the RAD51 N-terminal lobe domain bound to the histone H4 tail of the nucleosome
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 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 | 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 | 0061644 | biological_process | protein localization to CENP-A containing chromatin |
| F | 0070062 | cellular_component | extracellular exosome |
| L | 0000150 | molecular_function | DNA strand exchange activity |
| L | 0000152 | cellular_component | nuclear ubiquitin ligase complex |
| L | 0000228 | cellular_component | nuclear chromosome |
| L | 0000722 | biological_process | telomere maintenance via recombination |
| L | 0000724 | biological_process | double-strand break repair via homologous recombination |
| L | 0000730 | biological_process | DNA recombinase assembly |
| L | 0000781 | cellular_component | chromosome, telomeric region |
| L | 0000785 | cellular_component | chromatin |
| L | 0000793 | cellular_component | condensed chromosome |
| L | 0000794 | cellular_component | condensed nuclear chromosome |
| L | 0000800 | cellular_component | lateral element |
| L | 0001673 | cellular_component | male germ cell nucleus |
| L | 0001932 | biological_process | regulation of protein phosphorylation |
| L | 0003677 | molecular_function | DNA binding |
| L | 0003682 | molecular_function | chromatin binding |
| L | 0003690 | molecular_function | double-stranded DNA binding |
| L | 0003697 | molecular_function | single-stranded DNA binding |
| L | 0005515 | molecular_function | protein binding |
| L | 0005524 | molecular_function | ATP binding |
| L | 0005634 | cellular_component | nucleus |
| L | 0005654 | cellular_component | nucleoplasm |
| L | 0005694 | cellular_component | chromosome |
| L | 0005730 | cellular_component | nucleolus |
| L | 0005737 | cellular_component | cytoplasm |
| L | 0005739 | cellular_component | mitochondrion |
| L | 0005759 | cellular_component | mitochondrial matrix |
| L | 0005813 | cellular_component | centrosome |
| L | 0005829 | cellular_component | cytosol |
| L | 0005856 | cellular_component | cytoskeleton |
| L | 0006268 | biological_process | DNA unwinding involved in DNA replication |
| L | 0006281 | biological_process | DNA repair |
| L | 0006310 | biological_process | DNA recombination |
| L | 0006312 | biological_process | mitotic recombination |
| L | 0006974 | biological_process | DNA damage response |
| L | 0007131 | biological_process | reciprocal meiotic recombination |
| L | 0008094 | molecular_function | ATP-dependent activity, acting on DNA |
| L | 0010569 | biological_process | regulation of double-strand break repair via homologous recombination |
| L | 0010833 | biological_process | telomere maintenance via telomere lengthening |
| L | 0016605 | cellular_component | PML body |
| L | 0017116 | molecular_function | single-stranded DNA helicase activity |
| L | 0019899 | molecular_function | enzyme binding |
| L | 0031297 | biological_process | replication fork processing |
| L | 0032200 | biological_process | telomere organization |
| L | 0032991 | cellular_component | protein-containing complex |
| L | 0035861 | cellular_component | site of double-strand break |
| L | 0036297 | biological_process | interstrand cross-link repair |
| L | 0042148 | biological_process | DNA strand invasion |
| L | 0042802 | molecular_function | identical protein binding |
| L | 0048471 | cellular_component | perinuclear region of cytoplasm |
| L | 0051106 | biological_process | positive regulation of DNA ligation |
| L | 0051321 | biological_process | meiotic cell cycle |
| L | 0070182 | molecular_function | DNA polymerase binding |
| L | 0070192 | biological_process | chromosome organization involved in meiotic cell cycle |
| L | 0071312 | biological_process | cellular response to alkaloid |
| L | 0071479 | biological_process | cellular response to ionizing radiation |
| L | 0072711 | biological_process | cellular response to hydroxyurea |
| L | 0072757 | biological_process | cellular response to camptothecin |
| L | 0099182 | cellular_component | presynaptic intermediate filament cytoskeleton |
| L | 1990414 | biological_process | replication-born double-strand break repair via sister chromatid exchange |
| L | 1990918 | biological_process | double-strand break repair involved in meiotic recombination |
| L | 2000001 | biological_process | regulation of DNA damage checkpoint |
Functional Information from PROSITE/UniProt
| site_id | PS00322 |
| Number of Residues | 7 |
| Details | HISTONE_H3_1 Histone H3 signature 1. KAPRKQL |
| Chain | Residue | Details |
| E | LYS14-LEU20 |
| site_id | PS00959 |
| Number of Residues | 9 |
| Details | HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI |
| Chain | Residue | Details |
| E | PRO66-ILE74 |
| site_id | PS00047 |
| Number of Residues | 5 |
| Details | HISTONE_H4 Histone H4 signature. GAKRH |
| Chain | Residue | Details |
| F | GLY14-HIS18 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| L | GLY127 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:22814378 |
| Chain | Residue | Details |
| L | ALA2 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by CK2 => ECO:0000269|PubMed:22325354, ECO:0000269|PubMed:26811421 |
| Chain | Residue | Details |
| L | THR13 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PLK1 => ECO:0000269|PubMed:22325354, ECO:0000269|PubMed:26811421 |
| Chain | Residue | Details |
| L | SER14 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine; by ABL1 => ECO:0000269|PubMed:9461559 |
| Chain | Residue | Details |
| L | TYR54 | |
| F | LYS16 | |
| F | LYS44 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by CHEK1 => ECO:0000269|PubMed:15665856 |
| Chain | Residue | Details |
| L | THR309 | |
| F | LYS31 | |
| F | LYS77 | |
| F | LYS91 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:23393192 |
| Chain | Residue | Details |
| L | LYS58 | |
| L | LYS64 |
| 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 |
| F | 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 |
| F | TYR51 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 |
| Chain | Residue | Details |
| F | LYS59 | |
| E | LYS56 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62806 |
| Chain | Residue | Details |
| F | LYS79 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P62806 |
| Chain | Residue | Details |
| F | THR80 | |
| E | LYS64 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| F | TYR88 |
| 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 |
| F | 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 |
| E | LYS27 | |
| F | 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 |
| 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 UFM1); alternate => ECO:0000269|PubMed:30886146 |
| Chain | Residue | Details |
| F | LYS31 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-methyllysine => ECO:0000269|PubMed:15983376 |
| Chain | Residue | Details |
| E | LYS37 |
| site_id | SWS_FT_FI19 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:19783980 |
| Chain | Residue | Details |
| E | TYR41 |
| site_id | SWS_FT_FI20 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:20850016 |
| Chain | Residue | Details |
| E | SER57 |
| site_id | SWS_FT_FI21 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:29211711 |
| Chain | Residue | Details |
| E | LYS79 |
| site_id | SWS_FT_FI22 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:20850016 |
| Chain | Residue | Details |
| E | THR80 |
| site_id | SWS_FT_FI23 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243 |
| Chain | Residue | Details |
| E | SER86 |
| site_id | SWS_FT_FI24 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 |
| Chain | Residue | Details |
| E | THR107 |
| site_id | SWS_FT_FI25 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 |
| Chain | Residue | Details |
| E | LYS115 |
| site_id | SWS_FT_FI26 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229 |
| Chain | Residue | Details |
| E | LYS122 |
| site_id | SWS_FT_FI27 |
| Number of Residues | 1 |
| Details | LIPID: N6-decanoyllysine => ECO:0000269|PubMed:35939806 |
| Chain | Residue | Details |
| E | LYS18 |
