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 | 0000785 | cellular_component | chromatin |
| A | 0003682 | molecular_function | chromatin binding |
| A | 0003712 | molecular_function | transcription coregulator activity |
| 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 | 0006338 | biological_process | chromatin remodeling |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
| 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 | 0016746 | molecular_function | acyltransferase activity |
| A | 0019899 | molecular_function | enzyme binding |
| A | 0022008 | biological_process | neurogenesis |
| A | 0030099 | biological_process | myeloid cell differentiation |
| 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 | 0043995 | molecular_function | histone H4K5 acetyltransferase activity |
| A | 0043996 | molecular_function | histone H4K8 acetyltransferase activity |
| A | 0044545 | cellular_component | NSL complex |
| 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 | 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 | peptide-lysine-N-acetyltransferase activity |
| A | 0061920 | molecular_function | protein propionyltransferase activity |
| A | 0071339 | cellular_component | MLL1 complex |
| A | 0072487 | cellular_component | MSL complex |
| A | 1902726 | biological_process | positive regulation of skeletal muscle satellite cell differentiation |
| A | 1903108 | biological_process | regulation of mitochondrial transcription |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 25 |
| Details | ZN_FING: C2HC MYST-type => ECO:0000255|PROSITE-ProRule:PRU01063, ECO:0000269|PubMed:22020126 |
| Chain | Residue | Details |
| A | LEU207-TRP232 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:21217699, ECO:0000305|PubMed:27768893, ECO:0000305|PubMed:33657400 |
| Chain | Residue | Details |
| A | GLU350 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|PubMed:21691301, ECO:0000269|PubMed:22020126, ECO:0000269|PubMed:27382063, ECO:0000269|PubMed:29321206, ECO:0000269|Ref.33, ECO:0007744|PDB:2GIV, ECO:0007744|PDB:2PQ8, ECO:0007744|PDB:2Y0M, ECO:0007744|PDB:3QAH, ECO:0007744|PDB:3TOA, ECO:0007744|PDB:3TOB, ECO:0007744|PDB:4DNC, ECO:0007744|PDB:5J8C, ECO:0007744|PDB:5J8F, ECO:0007744|PDB:5WCI |
| Chain | Residue | Details |
| A | CYS230 | |
| A | CYS210 | |
| A | CYS213 | |
| A | HIS226 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29321206, ECO:0007744|PDB:5WCI |
| Chain | Residue | Details |
| A | THR319 | |
| A | ARG325 | |
| A | GLY329 | |
| A | LYS330 | |
| A | SER354 | |
| A | SER363 | |
| A | ILE317 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|Ref.33, ECO:0007744|PDB:2GIV, ECO:0007744|PDB:2Y0M |
| Chain | Residue | Details |
| A | ARG326 | |
| A | GLY327 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21217699, ECO:0007744|PDB:2Y0M |
| Chain | Residue | Details |
| A | LYS432 | |
| A | TYR408 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378 |
| Chain | Residue | Details |
| A | ALA2 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q5XI06 |
| Chain | Residue | Details |
| A | SER42 | |
| A | SER37 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS113 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:21217699, ECO:0000269|PubMed:21691301, ECO:0000269|PubMed:22020126, ECO:0000269|PubMed:22547026, ECO:0000269|PubMed:22918831, ECO:0000269|PubMed:27382063, ECO:0000269|Ref.33, ECO:0007744|PDB:2GIV |
| Chain | Residue | Details |
| A | ALY274 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER348 |
