7CMR
The Crystal Structure of human MYST1 from Biortus.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000123 | cellular_component | histone acetyltransferase complex |
| A | 0000776 | cellular_component | kinetochore |
| A | 0003713 | molecular_function | transcription coactivator activity |
| A | 0004402 | molecular_function | histone acetyltransferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005694 | cellular_component | chromosome |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0006325 | biological_process | chromatin organization |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009048 | biological_process | dosage compensation by inactivation of X chromosome |
| A | 0010485 | molecular_function | histone H4 acetyltransferase activity |
| A | 0010506 | biological_process | regulation of autophagy |
| A | 0010719 | biological_process | negative regulation of epithelial to mesenchymal transition |
| A | 0016363 | cellular_component | nuclear matrix |
| A | 0016407 | molecular_function | acetyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0019899 | molecular_function | enzyme binding |
| A | 0022008 | biological_process | neurogenesis |
| A | 0030097 | biological_process | hemopoiesis |
| A | 0030099 | biological_process | myeloid cell differentiation |
| A | 0031981 | cellular_component | nuclear lumen |
| A | 0032480 | biological_process | negative regulation of type I interferon production |
| A | 0035166 | biological_process | post-embryonic hemopoiesis |
| A | 0035267 | cellular_component | NuA4 histone acetyltransferase complex |
| A | 0040029 | biological_process | epigenetic regulation of gene expression |
| A | 0043995 | molecular_function | histone H4K5 acetyltransferase activity |
| A | 0043996 | molecular_function | histone H4K8 acetyltransferase activity |
| A | 0044545 | cellular_component | NSL complex |
| A | 0045595 | biological_process | regulation of cell differentiation |
| A | 0045815 | biological_process | transcription initiation-coupled chromatin remodeling |
| A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046972 | molecular_function | histone H4K16 acetyltransferase activity |
| A | 0048477 | biological_process | oogenesis |
| A | 0050684 | biological_process | regulation of mRNA processing |
| A | 0051241 | biological_process | negative regulation of multicellular organismal process |
| A | 0060261 | biological_process | positive regulation of transcription initiation by RNA polymerase II |
| A | 0061629 | molecular_function | RNA polymerase II-specific DNA-binding transcription factor binding |
| A | 0061733 | molecular_function | protein-lysine-acetyltransferase activity |
| A | 0061920 | molecular_function | protein propionyltransferase activity |
| A | 0071339 | cellular_component | MLL1 complex |
| A | 0072487 | cellular_component | MSL complex |
| A | 0140297 | molecular_function | DNA-binding transcription factor binding |
| A | 1902726 | biological_process | positive regulation of skeletal muscle satellite cell differentiation |
| A | 1903108 | biological_process | regulation of mitochondrial transcription |
| A | 1990841 | molecular_function | promoter-specific chromatin binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 25 |
| Details | Zinc finger: {"description":"C2HC MYST-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01063","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"21217699","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27768893","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"33657400","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21217699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21691301","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27382063","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29321206","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2007","submissionDatabase":"PDB data bank","title":"MYST histone acetyltransferase 1.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2GIV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PQ8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Y0M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QAH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TOA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TOB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4DNC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J8C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J8F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5WCI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29321206","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5WCI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21217699","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2007","submissionDatabase":"PDB data bank","title":"MYST histone acetyltransferase 1.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2GIV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Y0M","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21217699","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2Y0M","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"21217699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21691301","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22547026","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22918831","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27382063","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2007","submissionDatabase":"PDB data bank","title":"MYST histone acetyltransferase 1.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2GIV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
