3GUT
Crystal structure of a higher-order complex of p50:RelA bound to the HIV-1 LTR
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0005737 | cellular_component | cytoplasm |
| 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 | 0005737 | cellular_component | cytoplasm |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0003677 | molecular_function | DNA binding |
| D | 0003700 | molecular_function | DNA-binding transcription factor activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| E | 0003677 | molecular_function | DNA binding |
| E | 0003700 | molecular_function | DNA-binding transcription factor activity |
| E | 0005737 | cellular_component | cytoplasm |
| 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 | 0005737 | cellular_component | cytoplasm |
| F | 0006355 | biological_process | regulation of DNA-templated transcription |
| G | 0003677 | molecular_function | DNA binding |
| G | 0003700 | molecular_function | DNA-binding transcription factor activity |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0006355 | biological_process | regulation of DNA-templated transcription |
| H | 0003677 | molecular_function | DNA binding |
| H | 0003700 | molecular_function | DNA-binding transcription factor activity |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from PROSITE/UniProt
| site_id | PS01204 |
| Number of Residues | 7 |
| Details | REL_1 NF-kappa-B/Rel/dorsal domain signature. FRYvCEG |
| Chain | Residue | Details |
| B | PHE355-GLY361 | |
| A | PHE34-GLY40 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"S-nitrosocysteine; alternate","evidences":[{"source":"UniProtKB","id":"Q04207","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"(Microbial infection) Phosphoserine","evidences":[{"source":"PubMed","id":"24807716","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine; by PCAF and EP300; alternate","evidences":[{"source":"PubMed","id":"12419806","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"12456660","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"14690596","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine; by RPS6KA4 and RPS6KA5","evidences":[{"source":"PubMed","id":"12628924","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15516339","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3)","evidences":[{"source":"PubMed","id":"22649547","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 12 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3); alternate"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"S-nitrosocysteine; alternate","evidences":[{"source":"PubMed","id":"8710491","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine; by PKA","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | Lipidation: {"description":"S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternate","evidences":[{"source":"PubMed","id":"11466314","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 8 |
| 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 |
