9OG0
Cryo-EM structure of OS9-SEL1L-HRD1 dimer
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000836 | cellular_component | Hrd1p ubiquitin ligase complex |
| A | 0000839 | cellular_component | Hrd1p ubiquitin ligase ERAD-L complex |
| A | 0002327 | biological_process | immature B cell differentiation |
| A | 0005515 | molecular_function | protein binding |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005790 | cellular_component | smooth endoplasmic reticulum |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0012505 | cellular_component | endomembrane system |
| A | 0016020 | cellular_component | membrane |
| A | 0016567 | biological_process | protein ubiquitination |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030970 | biological_process | retrograde protein transport, ER to cytosol |
| A | 0036503 | biological_process | ERAD pathway |
| A | 0036513 | cellular_component | Derlin-1 retrotranslocation complex |
| A | 0043161 | biological_process | proteasome-mediated ubiquitin-dependent protein catabolic process |
| A | 0044322 | cellular_component | endoplasmic reticulum quality control compartment |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050821 | biological_process | protein stabilization |
| A | 0051082 | molecular_function | unfolded protein binding |
| A | 0051087 | molecular_function | protein-folding chaperone binding |
| A | 0051117 | molecular_function | ATPase binding |
| A | 0061630 | molecular_function | ubiquitin protein ligase activity |
| A | 0070936 | biological_process | protein K48-linked ubiquitination |
| A | 0140297 | molecular_function | DNA-binding transcription factor binding |
| A | 1902236 | biological_process | negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway |
| A | 1904380 | biological_process | endoplasmic reticulum mannose trimming |
| A | 1990381 | molecular_function | ubiquitin-specific protease binding |
| B | 0000836 | cellular_component | Hrd1p ubiquitin ligase complex |
| B | 0000839 | cellular_component | Hrd1p ubiquitin ligase ERAD-L complex |
| B | 0002327 | biological_process | immature B cell differentiation |
| B | 0005515 | molecular_function | protein binding |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0005790 | cellular_component | smooth endoplasmic reticulum |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0012505 | cellular_component | endomembrane system |
| B | 0016020 | cellular_component | membrane |
| B | 0016567 | biological_process | protein ubiquitination |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030970 | biological_process | retrograde protein transport, ER to cytosol |
| B | 0036503 | biological_process | ERAD pathway |
| B | 0036513 | cellular_component | Derlin-1 retrotranslocation complex |
| B | 0043161 | biological_process | proteasome-mediated ubiquitin-dependent protein catabolic process |
| B | 0044322 | cellular_component | endoplasmic reticulum quality control compartment |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050821 | biological_process | protein stabilization |
| B | 0051082 | molecular_function | unfolded protein binding |
| B | 0051087 | molecular_function | protein-folding chaperone binding |
| B | 0051117 | molecular_function | ATPase binding |
| B | 0061630 | molecular_function | ubiquitin protein ligase activity |
| B | 0070936 | biological_process | protein K48-linked ubiquitination |
| B | 0140297 | molecular_function | DNA-binding transcription factor binding |
| B | 1902236 | biological_process | negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway |
| B | 1904380 | biological_process | endoplasmic reticulum mannose trimming |
| B | 1990381 | molecular_function | ubiquitin-specific protease binding |
Functional Information from PROSITE/UniProt
| site_id | PS00023 |
| Number of Residues | 42 |
| Details | FN2_1 Fibronectin type-II collagen-binding domain signature. ChfPFlFldkeydeCtsdgredgrlWCattyDYktdekWgFC |
| Chain | Residue | Details |
| C | CYS123-CYS164 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 90 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 240 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 136 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 500 |
| Details | Region: {"description":"Involved in FAM8A1 interaction","evidences":[{"source":"PubMed","id":"28827405","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 166 |
| Details | Region: {"description":"Necessary and sufficient for SEL1L interaction","evidences":[{"source":"PubMed","id":"28827405","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 96 |
| Details | Domain: {"description":"Fibronectin type-II","evidences":[{"source":"PROSITE-ProRule","id":"PRU00479","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 70 |
| Details | Repeat: {"description":"Sel1-like 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 70 |
| Details | Repeat: {"description":"Sel1-like 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 70 |
| Details | Repeat: {"description":"Sel1-like 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 70 |
| Details | Repeat: {"description":"Sel1-like 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 72 |
| Details | Repeat: {"description":"Sel1-like 5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 72 |
| Details | Repeat: {"description":"Sel1-like 6"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 70 |
| Details | Repeat: {"description":"Sel1-like 7"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 70 |
| Details | Repeat: {"description":"Sel1-like 8"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 70 |
| Details | Repeat: {"description":"Sel1-like 9"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 70 |
| Details | Repeat: {"description":"Sel1-like 10"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 70 |
| Details | Repeat: {"description":"Sel1-like 11"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 370 |
| Details | Region: {"description":"Important for homodimerization and oligomerization","evidences":[{"source":"PubMed","id":"27064360","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 160 |
| Details | Region: {"description":"Interaction with SYVN1","evidences":[{"source":"PubMed","id":"27064360","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 12 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 244 |
| Details | Domain: {"description":"MRH","evidences":[{"source":"PROSITE-ProRule","id":"PRU01262","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 28 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI23 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21172656","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3AIH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
