The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
Human EMC2 encodes a cytosolic-facing subunit of the endoplasmic reticulum (ER) membrane protein complex (EMC), a conserved machine that promotes membrane protein biogenesis. The best-supported primary function of EMC2 is architectural/assembly scaffolding of the EMC cytosolic “basket,” positioning other EMC elements (notably the EMC3/EMC6 membrane vestibule and EMC3 cytosolic loop) that directly execute insertase and topology-control activities for selected membrane proteins. Recent work (2023–2024) has refined EMC mechanisms for selectivity filtering (preventing misinsertion and enforcing topogenesis rules) and post-translational topology rectification for multipass clients; these advances update how EMC2’s scaffold role is interpreted in pathway context. (pleiner2020structuralbasisfor pages 1-3, pleiner2023aselectivityfilter pages 8-10, wu2024emcrectifiesthe pages 7-9)
Authoritative EMC structural and mechanistic papers explicitly identify human EMC2 as a ~35 kDa, cytosolic EMC subunit (also called TTC35) that is part of the ER membrane protein complex. This matches the provided UniProt identity (Q15006: “ER membrane protein complex subunit 2”; synonyms TTC35/KIAA0103) and places the protein in ER membrane protein biogenesis rather than in an unrelated pathway. (chitwood2019theroleof pages 2-4, pleiner2020structuralbasisfor pages 1-3)
The EMC is a multi-subunit ER complex implicated in insertion, folding, and assembly of membrane proteins. It has an established insertase role for certain transmembrane domains (TMDs) and additional roles in later steps of membrane protein maturation. (hegde2022thefunctionstructure pages 4-6, odonnell2020thearchitectureof pages 1-2)
EMC2 is cytosolic-facing and resides as part of the ER-resident EMC, rather than acting as a free cytosolic chaperone. In the human EMC cryo-EM model, EMC2 sits in the cytosolic region adjacent to other cytosolic and membrane subunits that create the substrate-entry vestibule. (pleiner2020structuralbasisfor pages 1-3, hegde2022thefunctionstructure pages 4-6)
Human EMC contains cytosolic subunits EMC2 plus EMC8 and/or EMC9. Structural/biochemical work indicates EMC2 forms stable complexes with EMC8/9 that can be mutually exclusive in assembly contexts, consistent with functional substitution by paralogs in some settings. (pleiner2020structuralbasisfor pages 7-11, odonnell2020thearchitectureof pages 2-4)
High-resolution structural work indicates EMC2 is an architectural scaffold that organizes the cytosolic portion of EMC. In the human EMC cryo-EM structure, EMC2 “acts as an architectural scaffold for EMC8 and the cytosolic regions of EMC3, 5, and 1,” consistent with EMC2 being central for EMC integrity. (pleiner2020structuralbasisfor pages 1-3)
Mechanistically, EMC2:
* forms an α-solenoid that binds the three-helix bundle formed by the coiled-coil and C-terminus of EMC3; (pleiner2020structuralbasisfor pages 1-3)
* clamps around EMC8 via an extensive hydrophobic surface; (pleiner2020structuralbasisfor pages 1-3)
* contributes to composite interfaces that accommodate the C-terminal tail of EMC5, which traverses through the center of EMC2 to the cytosolic face. (pleiner2020structuralbasisfor pages 1-3)
Mutations at EMC2 interfaces disrupt subunit binding/assembly in vitro, supporting a non-redundant structural role. (pleiner2020structuralbasisfor pages 1-3, pleiner2020structuralbasisfor pages 7-11)
In the architecture model, the cytosolic vestibule that initially receives TMDs includes EMC2 (in complex with EMC8/9). EMC2 contributes conserved basic residues at the entry region (e.g., Arg26, Arg91) that may participate in substrate filtering, disfavoring passage of highly basic segments toward the intramembrane groove and thereby contributing to selectivity. (odonnell2020thearchitectureof pages 14-15)
The EMC is described as a co- and post-translational insertase at the ER. In the human structure, the membrane insertion pathway proceeds via an enclosed hydrophilic vestibule within the membrane formed by EMC3 and EMC6, with a methionine-rich cytosolic loop implicated in substrate capture. EMC2 scaffolding helps position these elements within a functional assembly. (pleiner2020structuralbasisfor pages 1-3)
Proteomics and ribosome profiling indicate EMC engages a range of multipass membrane proteins cotranslationally, with enrichment for transporters and other challenging substrates (e.g., TMDs with charged residues). This is a complex-level activity, but EMC2 depletion can destabilize EMC subunits, consistent with EMC2 being required for these functions by maintaining complex integrity. (shurtleff2018theermembrane pages 8-10, chitwood2019theroleof pages 2-4)
Pleiner et al. (Journal of Cell Biology; May 2023) report that EMC limits misinsertion at the ER via a positively charged, hydrophilic vestibule that functions as a selectivity filter. Charge repulsion disfavors translocation of positively charged segments and contributes to enforcing “positive-inside” topology rules; altering key EMC3 residues can increase misinsertion (e.g., mislocalization of RHOT1). The work used split-GFP topology reporters, glycosylation assays, and crosslinking approaches to map substrate contacts through the vestibule. (pleiner2023aselectivityfilter pages 8-10, pleiner2023aselectivityfilter pages 2-4)
Importantly for EMC2 annotation, the study ties correct assembly/biogenesis of the insertase-competent module to cytosolic-domain interactions: deletion of EMC4’s cytosolic EMC2-binding site impaired biogenesis of a canonical EMC-dependent TA client (SQS/FDFT1), supporting the functional importance of EMC2-mediated assembly interfaces even when the “catalytic” insertion module is primarily EMC3/6. (pleiner2023aselectivityfilter pages 4-6)
Wu et al. (Nature Structural & Molecular Biology; Nov 2024) report that EMC can mediate post-translational insertion/rectification of certain TMDs near the C-terminus of multipass membrane proteins, exemplified by the final TMD insertion of SOAT1. The authors propose that some substrates are released from the ribosome–translocon in an incompletely inserted state and require EMC to rectify topology and evade quality control. The paper estimates ~250 new putative EMC substrates, indicating broader client scope than previously recognized for this topology-rectification role. (wu2024emcrectifiesthe pages 7-9)
O’Keefe et al. (Communications Biology; Jul 2021) show that type III single-pass membrane proteins (including viral HIV Vpu) can integrate into the ER via an EMC-mediated pathway that is resistant to Sec61 inhibitors such as ipomoeassin F (Ipom-F) and mycolactone. In their assays, multiple type III TMPs retained N-glycosylation in 1 µM Ipom-F, and siRNA knockdown of EMC2 (and EMC5) was used to probe EMC’s contribution and destabilized the wider EMC without broadly disrupting OST activity. This provides a practical strategy used in cell biology/pharmacology: combining Sec61 inhibitors with EMC depletion to separate Sec61- versus EMC-dependent membrane insertion routes. (o’keefe2021analternativepathway pages 1-2, o’keefe2021analternativepathway pages 2-3)
A 2024 review of ER involvement in flavivirus infection summarizes evidence that dengue virus multipass proteins NS4A/NS4B depend on EMC for biogenesis: EMC interacts with NS4B during ER translocation and supports its folding/correct topology, with context dependence on upstream NS4A. The review also notes an EMC4 role in phosphatidylserine transfer at ER–endosome contacts, impacting entry steps (fusion/RNA release). While this review discusses “EMC” rather than EMC2 specifically, EMC2 is required for complex integrity and thus is part of the host machinery underlying these phenotypes. (verhaegen2024theendoplasmicreticulum pages 3-4, chitwood2019theroleof pages 2-4)
These studies provide an empirical scope estimate: EMC dependence is substantial but not universal across the transmembrane proteome, and specific client features (e.g., polar/charged TMD residues) contribute to dependence. (tian2019proteomicanalysisidentifies pages 1-3)
Wu et al. (2024) estimate that their sequential co-/post-translational mechanism may apply to ~250 diverse multipass proteins, including pentameric ion channel family subunits relevant for neurotransmission. (wu2024emcrectifiesthe pages 7-9)
Open Targets lists association evidence linking EMC2 (ENSG00000104412) to traits/diseases including neurodegenerative disease, asthma, and gastroesophageal reflux disease, among others. These are association-level signals and should not be interpreted as definitive causal mechanisms without gene-level functional validation and variant-to-function mapping. (OpenTargets Search: -EMC2)
Given that EMC supports the biogenesis/topology of many multipass membrane proteins—many of which are receptors, channels, and transporters—perturbations of EMC integrity (including EMC2 disruption) plausibly impact signaling and homeostasis broadly via membrane proteostasis failure; however, the most reliable gene-level statements for EMC2 remain those tied to complex assembly/stability and substrate handling demonstrated in structural and depletion studies. (chitwood2019theroleof pages 2-4, pleiner2020structuralbasisfor pages 1-3)
EMC2 (Q15006) is best annotated as a cytosolic scaffold subunit of the ER membrane protein complex (EMC) that is required for EMC assembly and organization of the cytosolic vestibule. Through this architectural role, EMC2 enables EMC’s insertase/topogenesis functions that promote the correct insertion, topology, and stability of subsets of TA, type III, and multipass membrane proteins, including those with challenging biophysical features (e.g., low hydrophobicity or polar/charged residues in TMDs). (pleiner2020structuralbasisfor pages 1-3, odonnell2020thearchitectureof pages 14-15, tian2019proteomicanalysisidentifies pages 1-3)
The EMC architecture and EMC2’s cytosolic placement/interfaces within the human complex are illustrated in the Pleiner et al. (Science 2020) cryo-EM figures. (pleiner2020structuralbasisfor media 452a27e0, pleiner2020structuralbasisfor media afa23ddb, pleiner2020structuralbasisfor media 9fea6c09)
| Aspect | Key findings | Supporting citations |
|---|---|---|
| Identity / aliases | Human EMC2 encodes ER membrane protein complex subunit 2, also known as TTC35/KIAA0103; literature consistently identifies it as a cytosolic EMC subunit in the human ER membrane protein complex, matching UniProt Q15006. It is ~35 kDa and part of the conserved EMC core. | (chitwood2019theroleof pages 2-4, pleiner2020structuralbasisfor pages 1-3, hegde2022thefunctionstructure pages 4-6) |
| Localization | EMC2 is cytosolic-facing but tightly associated with the ER-resident EMC rather than being a free soluble factor. It sits in the cytosolic domain/vestibule of the complex adjacent to membrane subunits that form the insertase core. | (pleiner2020structuralbasisfor pages 1-3, odonnell2020thearchitectureof pages 14-15, odonnell2020thearchitectureof pages 1-2) |
| Complex membership | Human EMC is a 9-10 subunit complex depending on annotation/study context; EMC2 associates with membrane subunits plus EMC8 or EMC9 in a mutually exclusive or paralog-substitutable manner. EMC2 knockdown destabilizes other EMC components, supporting a core assembly role. | (odonnell2020thearchitectureof pages 2-4, odonnell2020thearchitectureof pages 1-2, chitwood2019theroleof pages 2-4) |
| Structural role | EMC2 forms an α-solenoid/TPR-like helical scaffold that organizes the cytosolic region. It contacts EMC3, EMC5, EMC1, and EMC8/9, and mutations at these interfaces disrupt assembly, showing EMC2 is primarily an architectural scaffold rather than the membrane-embedded catalytic insertase element. | (pleiner2020structuralbasisfor pages 1-3, pleiner2020structuralbasisfor pages 7-11) |
| Mechanistic role in insertion | EMC as a whole is a co- and post-translational insertase for selected low/moderate-hydrophobicity TMDs; EMC2 helps form the cytosolic vestibule that initially receives substrate TMDs before transfer to the EMC3/EMC6 hydrophilic vestibule in the membrane. Conserved basic residues at/near the EMC2-containing vestibule likely contribute to substrate filtering against positively charged segments. | (pleiner2020structuralbasisfor pages 1-3, odonnell2020thearchitectureof pages 14-15, odonnell2020thearchitectureof pages 1-2) |
| Recent 2023-2024 developments | 2023: EMC was shown to contain a selectivity filter that limits ER misinsertion, using a positively charged vestibule and methionine-rich capture loops; EMC4’s EMC2-binding site was functionally important for assembly. 2024: EMC was shown to rectify topology post-translationally for some multipass proteins, with an estimated ~250 new putative substrates. | (pleiner2023aselectivityfilter pages 8-10, pleiner2023aselectivityfilter pages 4-6, wu2024emcrectifiesthe pages 7-9) |
| Known client protein classes / examples | EMC-dependent proteins are enriched for multipass transporters, ATPases, some tail-anchored proteins, and selected type III membrane proteins. Example clients/contexts include SQS/FDFT1, ATP6V0A1, FZD family proteins, CB5, SGPL1, and viral or host type III TMPs such as HIV Vpu, SMAGP, BCMA, Syt1; flaviviral NS4A/NS4B biogenesis also depends on EMC contextually. | (chitwood2019theroleof pages 2-4, tian2019proteomicanalysisidentifies pages 5-6, o’keefe2021analternativepathway pages 1-2, verhaegen2024theendoplasmicreticulum pages 3-4) |
| Quantitative stats | In unbiased mammalian proteomics, 36 of 971 transmembrane proteins were classified as EMC-dependent (~3.7%), while 171 of 971 were EMC-independent (~17.6%). Tian et al. identified 5,570 proteins total, retained 4,446 for analysis, with 81 significantly changed in EMC6-KO vs WT (17 up, 64 down). Shurtleff et al. found 37 decreased proteins, and among 11 proteins decreased ≥2-fold in both EMC2- and EMC4-depleted cells, 10 were transmembrane proteins. | (tian2019proteomicanalysisidentifies pages 5-6, tian2019proteomicanalysisidentifies pages 3-5, shurtleff2018theermembrane pages 8-10) |
| Experimental systems | EMC2/EMC function has been studied using cryo-EM, mutagenesis, co-immunoprecipitation, SEC-MALS, site-specific crosslinking, reconstituted proteoliposome insertion assays, split-GFP topology reporters, glycosylation assays, SILAC/TMT proteomics, ribosome profiling, and siRNA/CRISPRi depletion in human cell systems plus in vitro rough microsomes/reticulocyte lysates. | (pleiner2020structuralbasisfor pages 1-3, pleiner2023aselectivityfilter pages 2-4, shurtleff2018theermembrane pages 8-10, tian2019proteomicanalysisidentifies pages 3-5, o’keefe2021analternativepathway pages 1-2) |
| Disease / phenotype associations | Direct, gene-specific human disease causality for EMC2 remains limited relative to complex-level biology, but EMC perturbation affects membrane-protein homeostasis, ER stress, and client stability. Experimental evidence links EMC biology to viral infection (e.g., DENV NS4A/NS4B, HIV Vpu), proteostasis, and cancer-related phenotypes in broader EMC studies; Open Targets lists low-to-moderate evidence associations for EMC2 to traits/diseases such as neurodegenerative disease, asthma, and gastroesophageal reflux disease, which should be interpreted cautiously as association-level rather than definitive mechanism. | (chitwood2019theroleof pages 2-4, OpenTargets Search: -EMC2, verhaegen2024theendoplasmicreticulum pages 3-4) |
Table: This table summarizes the verified identity, localization, structural role, mechanism, recent advances, client scope, quantitative data, methods, and disease relevance of human EMC2 (UniProt Q15006). It is useful as a compact evidence map linking EMC2 specifically to the ER membrane protein complex and membrane-protein biogenesis.
References
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(tian2019proteomicanalysisidentifies pages 1-3): Songhai Tian, Quan Wu, Bo Zhou, Mei Yuk Choi, Bo Ding, Wei Yang, and Min Dong. Proteomic analysis identifies membrane proteins dependent on the er membrane protein complex. Cell reports, 28:2517-2526.e5, Sep 2019. URL: https://doi.org/10.1016/j.celrep.2019.08.006, doi:10.1016/j.celrep.2019.08.006. This article has 79 citations and is from a highest quality peer-reviewed journal.
(OpenTargets Search: -EMC2): Open Targets Query (-EMC2, 5 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.
(pleiner2020structuralbasisfor media 452a27e0): Tino Pleiner, Giovani Pinton Tomaleri, Kurt Januszyk, Alison J. Inglis, Masami Hazu, and Rebecca M. Voorhees. Structural basis for membrane insertion by the human er membrane protein complex. Jul 2020. URL: https://doi.org/10.1126/science.abb5008, doi:10.1126/science.abb5008. This article has 192 citations and is from a highest quality peer-reviewed journal.
(pleiner2020structuralbasisfor media afa23ddb): Tino Pleiner, Giovani Pinton Tomaleri, Kurt Januszyk, Alison J. Inglis, Masami Hazu, and Rebecca M. Voorhees. Structural basis for membrane insertion by the human er membrane protein complex. Jul 2020. URL: https://doi.org/10.1126/science.abb5008, doi:10.1126/science.abb5008. This article has 192 citations and is from a highest quality peer-reviewed journal.
(pleiner2020structuralbasisfor media 9fea6c09): Tino Pleiner, Giovani Pinton Tomaleri, Kurt Januszyk, Alison J. Inglis, Masami Hazu, and Rebecca M. Voorhees. Structural basis for membrane insertion by the human er membrane protein complex. Jul 2020. URL: https://doi.org/10.1126/science.abb5008, doi:10.1126/science.abb5008. This article has 192 citations and is from a highest quality peer-reviewed journal.