6IEG
Crystal structure of human MTR4
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000176 | cellular_component | nuclear exosome (RNase complex) |
| A | 0000178 | cellular_component | exosome (RNase complex) |
| A | 0000398 | biological_process | mRNA splicing, via spliceosome |
| A | 0000460 | biological_process | maturation of 5.8S rRNA |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0003724 | molecular_function | RNA helicase activity |
| A | 0004386 | molecular_function | helicase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005681 | cellular_component | spliceosomal complex |
| A | 0005730 | cellular_component | nucleolus |
| A | 0006364 | biological_process | rRNA processing |
| A | 0006397 | biological_process | mRNA processing |
| A | 0006401 | biological_process | RNA catabolic process |
| A | 0006974 | biological_process | DNA damage response |
| A | 0008380 | biological_process | RNA splicing |
| A | 0016076 | biological_process | snRNA catabolic process |
| A | 0016607 | cellular_component | nuclear speck |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0031499 | cellular_component | TRAMP complex |
| A | 0062141 | cellular_component | nuclear exosome targeting complex |
| A | 0071013 | cellular_component | catalytic step 2 spliceosome |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000176 | cellular_component | nuclear exosome (RNase complex) |
| B | 0000178 | cellular_component | exosome (RNase complex) |
| B | 0000398 | biological_process | mRNA splicing, via spliceosome |
| B | 0000460 | biological_process | maturation of 5.8S rRNA |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0003723 | molecular_function | RNA binding |
| B | 0003724 | molecular_function | RNA helicase activity |
| B | 0004386 | molecular_function | helicase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005681 | cellular_component | spliceosomal complex |
| B | 0005730 | cellular_component | nucleolus |
| B | 0006364 | biological_process | rRNA processing |
| B | 0006397 | biological_process | mRNA processing |
| B | 0006401 | biological_process | RNA catabolic process |
| B | 0006974 | biological_process | DNA damage response |
| B | 0008380 | biological_process | RNA splicing |
| B | 0016076 | biological_process | snRNA catabolic process |
| B | 0016607 | cellular_component | nuclear speck |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0031499 | cellular_component | TRAMP complex |
| B | 0062141 | cellular_component | nuclear exosome targeting complex |
| B | 0071013 | cellular_component | catalytic step 2 spliceosome |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 156 |
| Details | Domain: {"description":"Helicase ATP-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 172 |
| Details | Domain: {"description":"Helicase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00542","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Motif: {"description":"DEIH box"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31358741","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6RO1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29844170","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31358741","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6C90","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6RO1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| 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 |
