7OS2
Cryo-EM structure of Brr2 in complex with Jab1/MPN and C9ORF78
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0005524 | molecular_function | ATP binding |
| C | 0000398 | biological_process | mRNA splicing, via spliceosome |
| C | 0000775 | cellular_component | chromosome, centromeric region |
| C | 0003723 | molecular_function | RNA binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005654 | cellular_component | nucleoplasm |
| C | 0005681 | cellular_component | spliceosomal complex |
| C | 0005694 | cellular_component | chromosome |
| C | 0005829 | cellular_component | cytosol |
| C | 0006397 | biological_process | mRNA processing |
| C | 0007059 | biological_process | chromosome segregation |
| C | 0008380 | biological_process | RNA splicing |
| C | 0030623 | molecular_function | U5 snRNA binding |
| C | 0045292 | biological_process | mRNA cis splicing, via spliceosome |
| C | 0060629 | biological_process | regulation of homologous chromosome segregation |
| J | 0000398 | biological_process | mRNA splicing, via spliceosome |
| J | 0005681 | cellular_component | spliceosomal complex |
| J | 0008233 | molecular_function | peptidase activity |
| J | 0008237 | molecular_function | metallopeptidase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 183 |
| Details | Domain: {"description":"Helicase ATP-binding 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 237 |
| Details | Domain: {"description":"Helicase C-terminal 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00542","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 305 |
| Details | Domain: {"description":"SEC63 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 175 |
| Details | Domain: {"description":"Helicase ATP-binding 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 208 |
| Details | Domain: {"description":"Helicase C-terminal 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00542","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 312 |
| Details | Domain: {"description":"SEC63 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Motif: {"description":"DEIH box"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | Motif: {"description":"DEVH box"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23045696","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4F93","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"F1LNJ2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q6P4T2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 53 |
| Details | Region: {"description":"Interaction with SNRNP200","evidences":[{"source":"PubMed","id":"35241646","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7OS2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 131 |
| Details | Domain: {"description":"MPN","evidences":[{"source":"PROSITE-ProRule","id":"PRU01182","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 34 |
| Details | Region: {"description":"Required for interaction with EFTUD2 and SNRNP200","evidences":[{"source":"PubMed","id":"17317632","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
