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Cryo-EM structure of HRD1-SEL1LX3-XTP3B complex in C1 symmetry

Functional Information from GO Data
ChainGOidnamespacecontents
A0000836cellular_componentHrd1p ubiquitin ligase complex
A0000839cellular_componentHrd1p ubiquitin ligase ERAD-L complex
A0002327biological_processimmature B cell differentiation
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005790cellular_componentsmooth endoplasmic reticulum
A0005886cellular_componentplasma membrane
A0006511biological_processubiquitin-dependent protein catabolic process
A0008270molecular_functionzinc ion binding
A0012505cellular_componentendomembrane system
A0016020cellular_componentmembrane
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0030970biological_processretrograde protein transport, ER to cytosol
A0036503biological_processERAD pathway
A0036513cellular_componentDerlin-1 retrotranslocation complex
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0044322cellular_componentendoplasmic reticulum quality control compartment
A0046872molecular_functionmetal ion binding
A0050821biological_processprotein stabilization
A0051082molecular_functionunfolded protein binding
A0051087molecular_functionprotein-folding chaperone binding
A0051117molecular_functionATPase binding
A0061630molecular_functionubiquitin protein ligase activity
A0070936biological_processprotein K48-linked ubiquitination
A0140297molecular_functionDNA-binding transcription factor binding
A1902236biological_processnegative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway
A1904380biological_processendoplasmic reticulum mannose trimming
A1990381molecular_functionubiquitin-specific protease binding
B0000836cellular_componentHrd1p ubiquitin ligase complex
B0000839cellular_componentHrd1p ubiquitin ligase ERAD-L complex
B0002327biological_processimmature B cell differentiation
B0005515molecular_functionprotein binding
B0005654cellular_componentnucleoplasm
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005790cellular_componentsmooth endoplasmic reticulum
B0005886cellular_componentplasma membrane
B0006511biological_processubiquitin-dependent protein catabolic process
B0008270molecular_functionzinc ion binding
B0012505cellular_componentendomembrane system
B0016020cellular_componentmembrane
B0016567biological_processprotein ubiquitination
B0016740molecular_functiontransferase activity
B0030970biological_processretrograde protein transport, ER to cytosol
B0036503biological_processERAD pathway
B0036513cellular_componentDerlin-1 retrotranslocation complex
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0044322cellular_componentendoplasmic reticulum quality control compartment
B0046872molecular_functionmetal ion binding
B0050821biological_processprotein stabilization
B0051082molecular_functionunfolded protein binding
B0051087molecular_functionprotein-folding chaperone binding
B0051117molecular_functionATPase binding
B0061630molecular_functionubiquitin protein ligase activity
B0070936biological_processprotein K48-linked ubiquitination
B0140297molecular_functionDNA-binding transcription factor binding
B1902236biological_processnegative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway
B1904380biological_processendoplasmic reticulum mannose trimming
B1990381molecular_functionubiquitin-specific protease binding
E0030968biological_processendoplasmic reticulum unfolded protein response
E0036503biological_processERAD pathway
F0030968biological_processendoplasmic reticulum unfolded protein response
F0036503biological_processERAD pathway
Functional Information from PROSITE/UniProt
site_idPS00023
Number of Residues42
DetailsFN2_1 Fibronectin type-II collagen-binding domain signature. ChfPFlFldkeydeCtsdgredgrlWCattyDYkadekWgFC
ChainResidueDetails
DCYS127-CYS168

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues90
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues240
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues136
DetailsTopological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues500
DetailsRegion: {"description":"Involved in FAM8A1 interaction","evidences":[{"source":"PubMed","id":"28827405","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues166
DetailsRegion: {"description":"Necessary and sufficient for SEL1L interaction","evidences":[{"source":"PubMed","id":"28827405","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues70
DetailsRepeat: {"description":"Sel1-like 1"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues70
DetailsRepeat: {"description":"Sel1-like 2"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues70
DetailsRepeat: {"description":"Sel1-like 3"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues70
DetailsRepeat: {"description":"Sel1-like 4"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues70
DetailsRepeat: {"description":"Sel1-like 8"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues70
DetailsRepeat: {"description":"Sel1-like 9"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues70
DetailsRepeat: {"description":"Sel1-like 10"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues70
DetailsRepeat: {"description":"Sel1-like 11"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues160
DetailsRegion: {"description":"Interaction with SYVN1","evidences":[{"source":"UniProtKB","id":"Q9Z2G6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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