1JEQ
Crystal Structure of the Ku Heterodimer
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0000723 | biological_process | telomere maintenance |
A | 0000725 | biological_process | recombinational repair |
A | 0000781 | cellular_component | chromosome, telomeric region |
A | 0000783 | cellular_component | nuclear telomere cap complex |
A | 0000976 | molecular_function | transcription cis-regulatory region binding |
A | 0002218 | biological_process | activation of innate immune response |
A | 0002376 | biological_process | immune system process |
A | 0002684 | biological_process | positive regulation of immune system process |
A | 0003677 | molecular_function | DNA binding |
A | 0003678 | molecular_function | DNA helicase activity |
A | 0003684 | molecular_function | damaged DNA binding |
A | 0003690 | molecular_function | double-stranded DNA binding |
A | 0003691 | molecular_function | double-stranded telomeric DNA binding |
A | 0003723 | molecular_function | RNA binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0004386 | molecular_function | helicase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005667 | cellular_component | transcription regulator complex |
A | 0005694 | cellular_component | chromosome |
A | 0005730 | cellular_component | nucleolus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005958 | cellular_component | DNA-dependent protein kinase-DNA ligase 4 complex |
A | 0006281 | biological_process | DNA repair |
A | 0006303 | biological_process | double-strand break repair via nonhomologous end joining |
A | 0006310 | biological_process | DNA recombination |
A | 0006974 | biological_process | DNA damage response |
A | 0008094 | molecular_function | ATP-dependent activity, acting on DNA |
A | 0010212 | biological_process | response to ionizing radiation |
A | 0016020 | cellular_component | membrane |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016829 | molecular_function | lyase activity |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0030332 | molecular_function | cyclin binding |
A | 0032991 | cellular_component | protein-containing complex |
A | 0032993 | cellular_component | protein-DNA complex |
A | 0034774 | cellular_component | secretory granule lumen |
A | 0042162 | molecular_function | telomeric DNA binding |
A | 0043564 | cellular_component | Ku70:Ku80 complex |
A | 0044877 | molecular_function | protein-containing complex binding |
A | 0045027 | molecular_function | DNA end binding |
A | 0045087 | biological_process | innate immune response |
A | 0045621 | biological_process | positive regulation of lymphocyte differentiation |
A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
A | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
A | 0048660 | biological_process | regulation of smooth muscle cell proliferation |
A | 0051575 | molecular_function | 5'-deoxyribose-5-phosphate lyase activity |
A | 0070418 | cellular_component | DNA-dependent protein kinase complex |
A | 0070419 | cellular_component | nonhomologous end joining complex |
A | 0071475 | biological_process | cellular hyperosmotic salinity response |
A | 0071480 | biological_process | cellular response to gamma radiation |
A | 0071481 | biological_process | cellular response to X-ray |
A | 0097110 | molecular_function | scaffold protein binding |
A | 0097680 | biological_process | double-strand break repair via classical nonhomologous end joining |
A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
B | 0000723 | biological_process | telomere maintenance |
B | 0003677 | molecular_function | DNA binding |
B | 0003678 | molecular_function | DNA helicase activity |
B | 0003684 | molecular_function | damaged DNA binding |
B | 0005634 | cellular_component | nucleus |
B | 0006303 | biological_process | double-strand break repair via nonhomologous end joining |
B | 0006310 | biological_process | DNA recombination |
B | 0042162 | molecular_function | telomeric DNA binding |
B | 0043564 | cellular_component | Ku70:Ku80 complex |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 207 |
Details | Domain: {"description":"Ku"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 34 |
Details | Domain: {"description":"SAP","evidences":[{"source":"PROSITE-ProRule","id":"PRU00186","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 64 |
Details | Region: {"description":"DNA-binding","evidences":[{"source":"PubMed","id":"15023334","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 109 |
Details | Region: {"description":"Interaction with XRCC5","evidences":[{"source":"PubMed","id":"15023334","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 5 |
Details | Region: {"description":"Interaction with BAX","evidences":[{"source":"PubMed","id":"15023334","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine; by PRKDC","evidences":[{"source":"PubMed","id":"9362500","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 5 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"15023334","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"15023334","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"source":"PubMed","id":"35545041","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI15 |
Number of Residues | 7 |
Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI16 |
Number of Residues | 27 |
Details | Region: {"description":"Leucine-zipper"} |
Chain | Residue | Details |
site_id | SWS_FT_FI17 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |