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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8S9S

Structure of the human ER membrane protein complex (EMC) in GDN

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
10072546cellular_componentEMC complex
20005515molecular_functionprotein binding
20005737cellular_componentcytoplasm
20005783cellular_componentendoplasmic reticulum
20005789cellular_componentendoplasmic reticulum membrane
20032977molecular_functionmembrane insertase activity
20042406cellular_componentextrinsic component of endoplasmic reticulum membrane
20045050biological_processprotein insertion into ER membrane by stop-transfer membrane-anchor sequence
20071816biological_processtail-anchored membrane protein insertion into ER membrane
20072546cellular_componentEMC complex
30005515molecular_functionprotein binding
30005789cellular_componentendoplasmic reticulum membrane
30016020cellular_componentmembrane
30032977molecular_functionmembrane insertase activity
30045050biological_processprotein insertion into ER membrane by stop-transfer membrane-anchor sequence
30071816biological_processtail-anchored membrane protein insertion into ER membrane
30072546cellular_componentEMC complex
40005515molecular_functionprotein binding
40005789cellular_componentendoplasmic reticulum membrane
40006915biological_processapoptotic process
40016020cellular_componentmembrane
40032977molecular_functionmembrane insertase activity
40045050biological_processprotein insertion into ER membrane by stop-transfer membrane-anchor sequence
40071816biological_processtail-anchored membrane protein insertion into ER membrane
40072546cellular_componentEMC complex
50000139cellular_componentGolgi membrane
50005515molecular_functionprotein binding
50005737cellular_componentcytoplasm
50005769cellular_componentearly endosome
50005789cellular_componentendoplasmic reticulum membrane
50005794cellular_componentGolgi apparatus
50005886cellular_componentplasma membrane
50006812biological_processmonoatomic cation transport
50006824biological_processcobalt ion transport
50006825biological_processcopper ion transport
50006826biological_processiron ion transport
50015087molecular_functioncobalt ion transmembrane transporter activity
50015093molecular_functionferrous iron transmembrane transporter activity
50015095molecular_functionmagnesium ion transmembrane transporter activity
50015693biological_processmagnesium ion transport
50016020cellular_componentmembrane
50022890molecular_functionobsolete inorganic cation transmembrane transporter activity
50031901cellular_componentearly endosome membrane
50032977molecular_functionmembrane insertase activity
50034755biological_processiron ion transmembrane transport
50045050biological_processprotein insertion into ER membrane by stop-transfer membrane-anchor sequence
50071816biological_processtail-anchored membrane protein insertion into ER membrane
50072546cellular_componentEMC complex
51903830biological_processmagnesium ion transmembrane transport
60000045biological_processautophagosome assembly
60005515molecular_functionprotein binding
60005783cellular_componentendoplasmic reticulum
60005789cellular_componentendoplasmic reticulum membrane
60016020cellular_componentmembrane
60032977molecular_functionmembrane insertase activity
60045050biological_processprotein insertion into ER membrane by stop-transfer membrane-anchor sequence
60071816biological_processtail-anchored membrane protein insertion into ER membrane
60072546cellular_componentEMC complex
61903349cellular_componentomegasome membrane
70030246molecular_functioncarbohydrate binding
80005515molecular_functionprotein binding
80005737cellular_componentcytoplasm
80005783cellular_componentendoplasmic reticulum
80005789cellular_componentendoplasmic reticulum membrane
80005794cellular_componentGolgi apparatus
80016020cellular_componentmembrane
80032977molecular_functionmembrane insertase activity
80045050biological_processprotein insertion into ER membrane by stop-transfer membrane-anchor sequence
80071816biological_processtail-anchored membrane protein insertion into ER membrane
80072546cellular_componentEMC complex
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues164
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"32439656","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues26
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"32439656","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"32439656","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WW7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32439656","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WW7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues33
DetailsRepeat: {"description":"TPR 1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues33
DetailsRepeat: {"description":"TPR 2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues33
DetailsRepeat: {"description":"TPR 3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues65
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"32439656","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues61
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"32459176","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues44
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"32459176","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues6
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"32459176","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32439656","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2025-10-22

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