Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Towards a proteome-scale map of the human protein-protein interaction network.
Defining the membrane proteome of NK cells.
Defining human ERAD networks through an integrative mapping strategy.
A human interactome in three quantitative dimensions organized by stoichiometries and abundances.
Architecture of the human interactome defines protein communities and disease networks.
The ER membrane protein complex is a transmembrane domain insertase.
The ER membrane protein complex interacts cotranslationally to enable biogenesis of multipass membrane proteins.
Histone Interaction Landscapes Visualized by Crosslinking Mass Spectrometry in Intact Cell Nuclei.
EMC Is Required to Initiate Accurate Membrane Protein Topogenesis.
A reference map of the human binary protein interactome.
Structural basis for membrane insertion by the human ER membrane protein complex.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
OpenCell: Endogenous tagging for the cartography of human cellular organization.
EMC chaperone-Ca(V) structure reveals an ion channel assembly intermediate.
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Cryo-EM of human EMC bound to a CaV1.2-CaVbeta3 assembly intermediate; EMC8 forms a specific cytosolic client-docking interface ("Cyto dock"/"EMC8 site", ~962 A^2 centered on the last helix of EMC8) with CaVbeta3, binding two CaVbeta loops and ordering an otherwise disordered CaVbeta region, demonstrating an EMC8-specific chaperone/assembly role beyond generic insertion.
The architecture of EMC reveals a path for membrane protein insertion.
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EMC2 forms an alpha-solenoid that clamps around EMC8 in the cytosolic basket; EMC8 is a ~23 kDa monomer ~44% identical to EMC9, and EMC8 and EMC9 are mutually exclusive subunits (no ternary EMC2-EMC8-EMC9 complex forms), supporting EMC8 as a structural assembly/scaffold subunit of the cytosolic module.
The Function, Structure, and Origins of the ER Membrane Protein Complex.
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Authoritative review of EMC function, structure, and evolution; places EMC2, EMC8, and EMC9 as the cytosolic subunits and EMC8/EMC9 as mutually exclusive paralogs of the cytosolic cradle that engages membrane-protein clients before insertion.
Structural insights into human EMC and its interaction with VDAC.
UniProt entry O43402 (EMC8_HUMAN), ER membrane protein complex subunit 8
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EMC8 is a cytosolic, peripheral subunit (cytoplasmic side) of the ER membrane protein complex (EMC), an energy-independent TMD insertase for newly synthesized membrane proteins; mediates cotranslational multipass and post-translational tail-anchored insertion. EMC8 and EMC9 are mutually exclusive subunits; EMC8 belongs to the EMC8/EMC9 family and contains an MPN domain.