Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7CZB

The cryo-EM structure of the ERAD retrotranslocation channel formed by human Derlin-1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002020	molecular_function	protease binding
A	0005047	molecular_function	signal recognition particle binding
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005769	cellular_component	early endosome
A	0005770	cellular_component	late endosome
A	0005783	cellular_component	endoplasmic reticulum
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0006511	biological_process	ubiquitin-dependent protein catabolic process
A	0006986	biological_process	response to unfolded protein
A	0010498	biological_process	proteasomal protein catabolic process
A	0015031	biological_process	protein transport
A	0016020	cellular_component	membrane
A	0030968	biological_process	endoplasmic reticulum unfolded protein response
A	0030970	biological_process	retrograde protein transport, ER to cytosol
A	0031398	biological_process	positive regulation of protein ubiquitination
A	0031625	molecular_function	ubiquitin protein ligase binding
A	0031648	biological_process	protein destabilization
A	0033554	biological_process	cellular response to stress
A	0036502	cellular_component	Derlin-1-VIMP complex
A	0036503	biological_process	ERAD pathway
A	0036513	cellular_component	Derlin-1 retrotranslocation complex
A	0038023	molecular_function	signaling receptor activity
A	0042288	molecular_function	MHC class I protein binding
A	0042802	molecular_function	identical protein binding
A	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
A	0044322	cellular_component	endoplasmic reticulum quality control compartment
A	0044877	molecular_function	protein-containing complex binding
A	0045184	biological_process	establishment of protein localization
A	0051117	molecular_function	ATPase binding
A	0071218	biological_process	cellular response to misfolded protein
A	1990381	molecular_function	ubiquitin-specific protease binding
B	0002020	molecular_function	protease binding
B	0005047	molecular_function	signal recognition particle binding
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005769	cellular_component	early endosome
B	0005770	cellular_component	late endosome
B	0005783	cellular_component	endoplasmic reticulum
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0006511	biological_process	ubiquitin-dependent protein catabolic process
B	0006986	biological_process	response to unfolded protein
B	0010498	biological_process	proteasomal protein catabolic process
B	0015031	biological_process	protein transport
B	0016020	cellular_component	membrane
B	0030968	biological_process	endoplasmic reticulum unfolded protein response
B	0030970	biological_process	retrograde protein transport, ER to cytosol
B	0031398	biological_process	positive regulation of protein ubiquitination
B	0031625	molecular_function	ubiquitin protein ligase binding
B	0031648	biological_process	protein destabilization
B	0033554	biological_process	cellular response to stress
B	0036502	cellular_component	Derlin-1-VIMP complex
B	0036503	biological_process	ERAD pathway
B	0036513	cellular_component	Derlin-1 retrotranslocation complex
B	0038023	molecular_function	signaling receptor activity
B	0042288	molecular_function	MHC class I protein binding
B	0042802	molecular_function	identical protein binding
B	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
B	0044322	cellular_component	endoplasmic reticulum quality control compartment
B	0044877	molecular_function	protein-containing complex binding
B	0045184	biological_process	establishment of protein localization
B	0051117	molecular_function	ATPase binding
B	0071218	biological_process	cellular response to misfolded protein
B	1990381	molecular_function	ubiquitin-specific protease binding
C	0002020	molecular_function	protease binding
C	0005047	molecular_function	signal recognition particle binding
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005769	cellular_component	early endosome
C	0005770	cellular_component	late endosome
C	0005783	cellular_component	endoplasmic reticulum
C	0005789	cellular_component	endoplasmic reticulum membrane
C	0006511	biological_process	ubiquitin-dependent protein catabolic process
C	0006986	biological_process	response to unfolded protein
C	0010498	biological_process	proteasomal protein catabolic process
C	0015031	biological_process	protein transport
C	0016020	cellular_component	membrane
C	0030968	biological_process	endoplasmic reticulum unfolded protein response
C	0030970	biological_process	retrograde protein transport, ER to cytosol
C	0031398	biological_process	positive regulation of protein ubiquitination
C	0031625	molecular_function	ubiquitin protein ligase binding
C	0031648	biological_process	protein destabilization
C	0033554	biological_process	cellular response to stress
C	0036502	cellular_component	Derlin-1-VIMP complex
C	0036503	biological_process	ERAD pathway
C	0036513	cellular_component	Derlin-1 retrotranslocation complex
C	0038023	molecular_function	signaling receptor activity
C	0042288	molecular_function	MHC class I protein binding
C	0042802	molecular_function	identical protein binding
C	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
C	0044322	cellular_component	endoplasmic reticulum quality control compartment
C	0044877	molecular_function	protein-containing complex binding
C	0045184	biological_process	establishment of protein localization
C	0051117	molecular_function	ATPase binding
C	0071218	biological_process	cellular response to misfolded protein
C	1990381	molecular_function	ubiquitin-specific protease binding
D	0002020	molecular_function	protease binding
D	0005047	molecular_function	signal recognition particle binding
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005769	cellular_component	early endosome
D	0005770	cellular_component	late endosome
D	0005783	cellular_component	endoplasmic reticulum
D	0005789	cellular_component	endoplasmic reticulum membrane
D	0006511	biological_process	ubiquitin-dependent protein catabolic process
D	0006986	biological_process	response to unfolded protein
D	0010498	biological_process	proteasomal protein catabolic process
D	0015031	biological_process	protein transport
D	0016020	cellular_component	membrane
D	0030968	biological_process	endoplasmic reticulum unfolded protein response
D	0030970	biological_process	retrograde protein transport, ER to cytosol
D	0031398	biological_process	positive regulation of protein ubiquitination
D	0031625	molecular_function	ubiquitin protein ligase binding
D	0031648	biological_process	protein destabilization
D	0033554	biological_process	cellular response to stress
D	0036502	cellular_component	Derlin-1-VIMP complex
D	0036503	biological_process	ERAD pathway
D	0036513	cellular_component	Derlin-1 retrotranslocation complex
D	0038023	molecular_function	signaling receptor activity
D	0042288	molecular_function	MHC class I protein binding
D	0042802	molecular_function	identical protein binding
D	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
D	0044322	cellular_component	endoplasmic reticulum quality control compartment
D	0044877	molecular_function	protein-containing complex binding
D	0045184	biological_process	establishment of protein localization
D	0051117	molecular_function	ATPase binding
D	0071218	biological_process	cellular response to misfolded protein
D	1990381	molecular_function	ubiquitin-specific protease binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	60
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"33658201","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	184
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"33658201","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	76
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"33658201","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	80
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"33658201","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	80
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"33658201","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	56
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"33658201","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	44
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"33658201","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	72
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"33658201","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)