9OGD
Cryo-EM structure of human exportin-1 conjugated with selinexor and bound to human ASB8(R197A)-ELOB/C
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000054 | biological_process | ribosomal subunit export from nucleus |
| A | 0000055 | biological_process | ribosomal large subunit export from nucleus |
| A | 0000056 | biological_process | ribosomal small subunit export from nucleus |
| A | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
| A | 0000776 | cellular_component | kinetochore |
| A | 0005049 | molecular_function | nuclear export signal receptor activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005635 | cellular_component | nuclear envelope |
| A | 0005642 | cellular_component | annulate lamellae |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005730 | cellular_component | nucleolus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006406 | biological_process | mRNA export from nucleus |
| A | 0006611 | biological_process | protein export from nucleus |
| A | 0006913 | biological_process | nucleocytoplasmic transport |
| A | 0009410 | biological_process | response to xenobiotic stimulus |
| A | 0015030 | cellular_component | Cajal body |
| A | 0016020 | cellular_component | membrane |
| A | 0019904 | molecular_function | protein domain specific binding |
| A | 0032434 | biological_process | regulation of proteasomal ubiquitin-dependent protein catabolic process |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0042254 | biological_process | ribosome biogenesis |
| A | 0071401 | biological_process | cellular response to triglyceride |
| A | 0140297 | molecular_function | DNA-binding transcription factor binding |
| A | 1902075 | biological_process | cellular response to salt |
| A | 1990904 | cellular_component | ribonucleoprotein complex |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0016567 | biological_process | protein ubiquitination |
| F | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
| F | 0000151 | cellular_component | ubiquitin ligase complex |
| F | 0001222 | molecular_function | transcription corepressor binding |
| F | 0005515 | molecular_function | protein binding |
| F | 0005634 | cellular_component | nucleus |
| F | 0005654 | cellular_component | nucleoplasm |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005829 | cellular_component | cytosol |
| F | 0006367 | biological_process | transcription initiation at RNA polymerase II promoter |
| F | 0006368 | biological_process | transcription elongation by RNA polymerase II |
| F | 0016567 | biological_process | protein ubiquitination |
| F | 0030891 | cellular_component | VCB complex |
| F | 0031462 | cellular_component | Cul2-RING ubiquitin ligase complex |
| F | 0031466 | cellular_component | Cul5-RING ubiquitin ligase complex |
| F | 0031625 | molecular_function | ubiquitin protein ligase binding |
| F | 0032436 | biological_process | positive regulation of proteasomal ubiquitin-dependent protein catabolic process |
| F | 0043161 | biological_process | proteasome-mediated ubiquitin-dependent protein catabolic process |
| F | 0065003 | biological_process | protein-containing complex assembly |
| F | 0070449 | cellular_component | elongin complex |
| F | 0140627 | biological_process | ubiquitin-dependent protein catabolic process via the C-end degron rule pathway |
| F | 0140958 | biological_process | target-directed miRNA degradation |
| F | 1990116 | biological_process | ribosome-associated ubiquitin-dependent protein catabolic process |
| F | 2000104 | biological_process | negative regulation of DNA-templated DNA replication |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | Repeat: {"description":"HEAT 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 38 |
| Details | Repeat: {"description":"HEAT 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 37 |
| Details | Repeat: {"description":"HEAT 5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 37 |
| Details | Repeat: {"description":"HEAT 6"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 38 |
| Details | Repeat: {"description":"HEAT 7"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 31 |
| Details | Repeat: {"description":"HEAT 8"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 37 |
| Details | Repeat: {"description":"HEAT 9"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 37 |
| Details | Repeat: {"description":"HEAT 10"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | Region: {"description":"Necessary for HTLV-1 Rex multimerization"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 20 |
| Details | Region: {"description":"Interaction with HIV-1 Rev"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q80U96","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q80U96","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q80U96","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| 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_FI15 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 28 |
| Details | Repeat: {"description":"ANK 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 29 |
| Details | Repeat: {"description":"ANK 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 29 |
| Details | Repeat: {"description":"ANK 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 53 |
| Details | Domain: {"description":"SOCS box","evidences":[{"source":"PROSITE-ProRule","id":"PRU00194","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 65 |
| Details | Domain: {"description":"Ubiquitin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62869","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
