3GB8
Crystal structure of CRM1/Snurportin-1 complex
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 | 0003723 | molecular_function | RNA binding |
| 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 | 0006886 | biological_process | intracellular protein transport |
| A | 0006913 | biological_process | nucleocytoplasmic transport |
| A | 0009410 | biological_process | response to xenobiotic stimulus |
| A | 0015030 | cellular_component | Cajal body |
| A | 0015031 | biological_process | protein transport |
| A | 0016020 | cellular_component | membrane |
| A | 0019904 | molecular_function | protein domain specific binding |
| A | 0031267 | molecular_function | small GTPase 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 | 0051028 | biological_process | mRNA transport |
| 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 | 0000339 | molecular_function | RNA cap binding |
| B | 0003723 | molecular_function | RNA binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005643 | cellular_component | nuclear pore |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006404 | biological_process | RNA import into nucleus |
| B | 0006606 | biological_process | protein import into nucleus |
| B | 0007010 | biological_process | cytoskeleton organization |
| B | 0051259 | biological_process | protein complex oligomerization |
| B | 0051262 | biological_process | protein tetramerization |
| B | 0061015 | biological_process | snRNA import into nucleus |
| B | 0061608 | molecular_function | nuclear import signal receptor activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 23 |
| Details | Repeat: {"description":"HEAT 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | Repeat: {"description":"HEAT 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 38 |
| Details | Repeat: {"description":"HEAT 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 37 |
| Details | Repeat: {"description":"HEAT 5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 37 |
| Details | Repeat: {"description":"HEAT 6"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 38 |
| Details | Repeat: {"description":"HEAT 7"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 31 |
| Details | Repeat: {"description":"HEAT 8"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 37 |
| Details | Repeat: {"description":"HEAT 9"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 37 |
| Details | Repeat: {"description":"HEAT 10"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 3 |
| Details | Region: {"description":"Necessary for HTLV-1 Rex multimerization"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 20 |
| Details | Region: {"description":"Interaction with HIV-1 Rev"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q80U96","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q80U96","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q80U96","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| 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_FI16 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 64 |
| Details | Region: {"description":"Necessary for interaction with KPNB1 and m3G-cap U1 and U5 snRNP import receptor activity","evidences":[{"source":"PubMed","id":"18187419","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9670026","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 41 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 2 |
| Details | Region: {"description":"Interaction with m3G-cap structure","evidences":[{"source":"PubMed","id":"15920472","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XK5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 15 |
| Details | Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 3 |
| Details | Site: {"description":"Interaction with m3G-cap structure","evidences":[{"source":"PubMed","id":"15920472","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XK5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
