3Q68
Structure of the Vps75-Rtt109 histone chaperone-lysine acetyltransferase complex (Full-length proteins in space group P212121)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000785 | cellular_component | chromatin |
| A | 0003682 | molecular_function | chromatin binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005829 | cellular_component | cytosol |
| A | 0006303 | biological_process | double-strand break repair via nonhomologous end joining |
| A | 0006325 | biological_process | chromatin organization |
| A | 0006334 | biological_process | nucleosome assembly |
| A | 0006335 | biological_process | DNA replication-dependent chromatin assembly |
| A | 0010698 | molecular_function | acetyltransferase activator activity |
| A | 0015031 | biological_process | protein transport |
| A | 0042393 | molecular_function | histone binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0070775 | cellular_component | H3 histone acetyltransferase complex |
| A | 2000617 | biological_process | obsolete positive regulation of histone H3-K9 acetylation |
| B | 0000785 | cellular_component | chromatin |
| B | 0003682 | molecular_function | chromatin binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005829 | cellular_component | cytosol |
| B | 0006303 | biological_process | double-strand break repair via nonhomologous end joining |
| B | 0006325 | biological_process | chromatin organization |
| B | 0006334 | biological_process | nucleosome assembly |
| B | 0006335 | biological_process | DNA replication-dependent chromatin assembly |
| B | 0010698 | molecular_function | acetyltransferase activator activity |
| B | 0015031 | biological_process | protein transport |
| B | 0042393 | molecular_function | histone binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0070775 | cellular_component | H3 histone acetyltransferase complex |
| B | 2000617 | biological_process | obsolete positive regulation of histone H3-K9 acetylation |
| C | 0000785 | cellular_component | chromatin |
| C | 0004402 | molecular_function | histone acetyltransferase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0006325 | biological_process | chromatin organization |
| C | 0006335 | biological_process | DNA replication-dependent chromatin assembly |
| C | 0006338 | biological_process | chromatin remodeling |
| C | 0006351 | biological_process | DNA-templated transcription |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
| C | 0006974 | biological_process | DNA damage response |
| C | 0010468 | biological_process | regulation of gene expression |
| C | 0010484 | molecular_function | histone H3 acetyltransferase activity |
| C | 0010526 | biological_process | transposable element silencing |
| C | 0016740 | molecular_function | transferase activity |
| C | 0032931 | molecular_function | histone H3K56 acetyltransferase activity |
| C | 0033554 | biological_process | cellular response to stress |
| C | 0036408 | molecular_function | histone H3K14 acetyltransferase activity |
| C | 0043007 | biological_process | maintenance of rDNA |
| C | 0043992 | molecular_function | histone H3K9 acetyltransferase activity |
| C | 0043994 | molecular_function | histone H3K23 acetyltransferase activity |
| C | 0044017 | molecular_function | histone H3K27 acetyltransferase activity |
| C | 0061733 | molecular_function | protein-lysine-acetyltransferase activity |
| C | 0070775 | cellular_component | H3 histone acetyltransferase complex |
| C | 1990414 | biological_process | replication-born double-strand break repair via sister chromatid exchange |
| C | 2001032 | biological_process | regulation of double-strand break repair via nonhomologous end joining |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 42 |
| Details | Region: {"description":"Interaction with VPS75","evidences":[{"source":"PubMed","id":"18719104","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21256037","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21454705","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"18707894","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18568037","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18707894","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18719104","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21256037","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ZFN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CZ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3Q33","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3Q35","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QM0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18568037","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3QM0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18568037","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21256037","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3Q33","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3Q35","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QM0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18707894","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18719104","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21256037","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ZFN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CZ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3Q33","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3Q35","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"18568037","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18707894","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18719104","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
