1HJB
CRYSTAL STRUCTURE OF RUNX-1/AML1/CBFALPHA RUNT DOMAIN AND C/EBPBETA BZIP HOMODIMER BOUND TO A DNA FRAGMENT FROM THE CSF-1R PROMOTER
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| A | 0006351 | biological_process | DNA-templated transcription |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0006351 | biological_process | DNA-templated transcription |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0003677 | molecular_function | DNA binding |
| C | 0003700 | molecular_function | DNA-binding transcription factor activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0003700 | molecular_function | DNA-binding transcription factor activity |
| D | 0006351 | biological_process | DNA-templated transcription |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| E | 0003700 | molecular_function | DNA-binding transcription factor activity |
| E | 0006351 | biological_process | DNA-templated transcription |
| E | 0006355 | biological_process | regulation of DNA-templated transcription |
| F | 0003677 | molecular_function | DNA binding |
| F | 0003700 | molecular_function | DNA-binding transcription factor activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005634 | cellular_component | nucleus |
| F | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00399 |
| Chain | Residue | Details |
| C | ASN112 | |
| C | GLU116 | |
| C | ARG139 | |
| C | VAL170 | |
| F | ASN112 | |
| F | GLU116 | |
| F | ARG139 | |
| F | VAL170 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by PKC/PRKCA => ECO:0000305|PubMed:9374525 |
| Chain | Residue | Details |
| A | SER288 | |
| B | SER288 | |
| D | SER288 | |
| E | SER288 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by CaMK2 => ECO:0000250|UniProtKB:P28033 |
| Chain | Residue | Details |
| A | SER325 | |
| B | SER325 | |
| D | SER325 | |
| E | SER325 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| A | LYS260 | |
| B | LYS260 | |
| D | LYS260 | |
| E | LYS260 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| E | LYS262 | |
| E | LYS332 | |
| A | LYS262 | |
| A | LYS332 | |
| B | LYS262 | |
| B | LYS332 | |
| D | LYS262 | |
| D | LYS332 |
