Affinage

SEC62

Translocation protein SEC62 · UniProt Q99442

Length
399 aa
Mass
45.9 kDa
Annotated
2026-06-10
61 papers in source corpus 22 papers cited in narrative 22 extracted findings
Cross-family judge vs UniProt: tie faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SEC62 encodes a two-pass ER transmembrane protein with cytosolic N- and C-termini that functions as an accessory component of the Sec61 translocon, originally defined in yeast as a membrane-intrinsic factor required for post-translational import of secretory precursors into the ER (PMID:2687286). In mammalian cells, SEC62 acts together with SEC63 to drive the post-translational, SRP-independent translocation pathway—selectively required for signal-peptide-containing precursors, particularly small proteins (≤100 aa) with slowly gating signal peptides and downstream positively charged residues, in an ATP-dependent manner—while SEC61 itself serves both co- and post-translational routes (PMID:22375059, PMID:22648169, PMID:32133789). Cryo-EM structures show that SEC63 first partially opens the Sec61 lateral gate and SEC62 then displaces the plug domain to open the translocation pore, with SEC62 binding altering lateral-gate, plug, and pore dynamics (PMID:33398175). SEC62 engagement with the translocon is governed by the nascent chain and is regulated by CK2 phosphorylation of SEC63 (which enhances SEC62–SEC63 binding) and by the SRP receptor, whose SRα charged linker displaces SEC62 to switch the channel to cotranslational mode (PMID:23287549, PMID:25801167, PMID:26634806). Independently of translocation, SEC62 serves as an ER-resident autophagy receptor during recovery from ER stress (recovER-phagy): a conserved C-terminal cytosolic LC3-interacting region selectively delivers ER components to autolysosomes, a function dispensable for its translocation role (PMID:27749824). SEC62 also directly binds the Sec61 complex in a Ca2+-sensitive manner to limit ER Ca2+ leak (PMID:24304694). SEC62 (TLOC1) is amplified at 3q26 and required for proliferation of amplified cell lines, conferring anchorage-independent growth via DDX3X binding, and promotes cancer progression through interactions including β-catenin (Wnt activation) and LC3II-driven autophagy (PMID:23764425, PMID:33858476, PMID:35165763).

Mechanistic history

Synthesis pass · year-by-year structured walk · 15 steps
  1. 1989 High

    Established SEC62 as a membrane-intrinsic factor required for protein import into the ER, defining the post-translational translocation problem.

    Evidence In vitro translocation assays with mutant vs. wild-type yeast membranes and cytosol; sequence analysis predicting two TM domains

    PMID:2687286

    Open questions at the time
    • Did not define the molecular partners or mechanism of channel gating
    • Mammalian relevance unaddressed
  2. 2000 Medium

    Showed the mammalian translocon includes ribosome-free Sec61 complexes associated with Sec62 and Sec63, extending the yeast paradigm to humans.

    Evidence Biochemical fractionation and co-isolation of ribosome-free Sec61 complexes with homology analysis

    PMID:10799540

    Open questions at the time
    • Functional roles of the mammalian complex not yet dissected
    • Stoichiometry and architecture undefined
  3. 2012 High

    Dissected pathway specificity, establishing SEC62 as selectively required for post-translational translocation of signal-peptide precursors, especially small (≤100 aa) ATP-dependent substrates, distinct from SEC61 and SEC63 roles.

    Evidence siRNA knockdown in human cells with substrate-specific in vitro translocation assays and size-class analysis

    PMID:22375059 PMID:22648169

    Open questions at the time
    • Structural basis of substrate selection not yet resolved
    • Signal peptide features determining SEC62 dependence not yet defined
  4. 2012 Medium

    Identified CK2 phosphorylation of SEC63 as a regulatory input enhancing SEC62–SEC63 binding required for functional translocation.

    Evidence CK2 phosphosite mapping with deletion/peptide approaches plus reciprocal Co-IP

    PMID:23287549

    Open questions at the time
    • In vivo consequences of phosphosite mutation on translocation flux not quantified
    • Single lab
  5. 2013 Medium

    Revealed a Ca2+-sensitive direct SEC62–Sec61 interaction controlling ER Ca2+ leak, linking the translocon accessory to Ca2+ homeostasis.

    Evidence Biacore SPR Ca2+-sensitive binding, Ca2+ imaging, siRNA silencing, mutant SEC62 expression

    PMID:24304694

    Open questions at the time
    • Structural detail of the Ca2+-binding motif unresolved
    • Relationship to translocation gating unclear
  6. 2013 Medium

    Connected SEC62 to oncogenesis, showing it is required for proliferation of 3q26-amplified cells and drives transformation through DDX3X binding.

    Evidence Loss/gain-of-function genetic screens, proteomic binding studies, anchorage-independent growth assays

    PMID:23764425

    Open questions at the time
    • Mechanism linking translocon function to transformation not defined
    • DDX3X-dependent downstream pathway unmapped
  7. 2014 Medium

    Extended SEC62-SEC63 function to membrane-protein topogenesis, showing the complex facilitates C-terminal translocation of single- and multi-spanning proteins in yeast.

    Evidence Systematic yeast mutant analysis of membrane substrates with varying hydrophobicity, charge, and TM orientation

    PMID:23632075 PMID:25097231

    Open questions at the time
    • Mammalian conservation of topogenic role untested
    • Single lab
  8. 2015 High

    Demonstrated that SEC62/63 engagement is dynamically controlled by the nascent chain and that the SRP receptor displaces SEC62 to switch the channel from post- to cotranslational mode.

    Evidence Ribosome-nascent chain isolation, MS, crosslinking, SRα truncation analysis and translocation assays

    PMID:25801167 PMID:26634806

    Open questions at the time
    • Kinetics of the mode switch in living cells not quantified
    • Generality across substrate classes incomplete
  9. 2016 High

    Defined a translocation-independent role for SEC62 as an ER-phagy receptor during ER stress recovery via a C-terminal LIR motif.

    Evidence Autophagy flux assays, LC3-IP, LIR mutagenesis separating ER-phagy from translocation, live-cell imaging

    PMID:27749824

    Open questions at the time
    • Signals triggering recovER-phagy onset not fully defined
    • Cargo selectivity mechanism within the ER unclear
  10. 2020 Medium

    Defined the signal-peptide features that dictate SEC62/SEC63 dependence, linking longer/less hydrophobic H-regions and downstream positive charges to slow channel gating and BiP requirement.

    Evidence Unbiased proteomics in intact human cells with SEC62/SEC63 knockdown and signal-peptide analysis of validated substrates

    PMID:32133789

    Open questions at the time
    • Predictive rules not validated across full secretome
    • Single lab
  11. 2021 High

    Provided atomic mechanism for stepwise channel activation: SEC63 partially opens the lateral gate, SEC62 displaces the plug to open the pore.

    Evidence Cryo-EM structures of multiple Sec61-Sec62-Sec63 variants with MD simulations and mutagenesis

    PMID:33398175

    Open questions at the time
    • Dynamic transition states captured only computationally
    • Mammalian complex structure not resolved here
  12. 2021 Medium

    Expanded SEC62's autophagy/cancer roles, showing β-catenin stabilization (Wnt activation) and ATG9A-dependent recruitment to ER-phagy.

    Evidence GST pull-down, Co-IP, knockdown and in vivo cancer assays; ATG9A interactome in mouse models

    PMID:33858476 PMID:33870132

    Open questions at the time
    • Connection between translocon and Wnt functions of SEC62 unclear
    • ATG9A acetylation-to-recruitment mechanism not fully resolved
  13. 2022 Medium

    Linked SEC62-driven autophagy to cancer metastasis via LC3II binding and PERK/ATF4 UPR signaling, and computationally refined how SEC62 binding shifts channel conformational dynamics.

    Evidence Co-IP, autophagy flux reporters, xenografts; MD simulations from cryo-EM structures

    PMID:35165763 PMID:36116515

    Open questions at the time
    • MD predictions of gate widening not experimentally validated in that work
    • Causality between autophagy and invasion incompletely separated
  14. 2025 Medium

    Identified disease-relevant SEC62 protein interactions: ATAD3B at mitochondria-associated membranes (driving MASH via defective mitophagy) and TRPM4 (whose degradation SEC62 promotes), the latter a druggable target of cinobufagin.

    Evidence Co-IP, hepatocyte-specific overexpression/knockout mice, MST/CETSA/SPR binding assays, ubiquitination assays

    PMID:40839992 PMID:42001994

    Open questions at the time
    • How these interactions relate to canonical translocon/ER-phagy roles unclear
    • Single lab per interaction
  15. 2026 Medium

    Showed neuronal SEC62-mediated ER-phagy alleviates Alzheimer's pathology, linking ER-phagy receptor function to neurodegeneration.

    Evidence AAV-mediated SEC62 overexpression in 5×FAD mice, Aβ and cognitive readouts, iPSC-derived neuron analysis

    PMID:42026868

    Open questions at the time
    • Mechanistic link between ER-phagy and Aβ clearance not fully defined
    • Single model system

Open questions

Synthesis pass · forward-looking unresolved questions
  • How SEC62's translocation, ER-phagy, Ca2+-regulation, and disease-associated interactions are integrated and switched within a single protein remains unresolved.
  • No unified regulatory model coordinating SEC62's distinct functions
  • Mammalian translocon structural architecture not solved
  • Whether oncogenic interactions depend on translocon vs. ER-phagy activity unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 4 GO:0060090 molecular adaptor activity 2 GO:0140313 molecular sequestering activity 1
Localization
GO:0005783 endoplasmic reticulum 3 GO:0005739 mitochondrion 1
Pathway
R-HSA-392499 Metabolism of proteins 3 R-HSA-9609507 Protein localization 3 R-HSA-9612973 Autophagy 3
Partners
ATAD3BATG9ACTNNB1DDX3XMAP1LC3BSEC61SEC63TRPM4
Complex memberships
Sec61-Sec62-Sec63 translocon complex

Evidence

Reading pass · 22 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1989 SEC62 encodes a membrane protein required for post-translational translocation of secretory precursor proteins into the yeast ER lumen; membranes from sec62 mutant cells display low and labile translocation activity, while cytosol from mutant cells supports normal translocation, demonstrating the defect is membrane-intrinsic. In vitro translocation assay with membranes/cytosol from mutant and wild-type yeast; DNA sequence analysis predicting two transmembrane domains and cytoplasmic N- and C-terminal domains The Journal of cell biology High 2687286
2000 Mammalian Sec61 exists in ribosome-free complexes associated with Sec62 and Sec63 (homologs of yeast Sec62p/Sec63p), forming a higher-order translocon complex in the ER membrane. Biochemical fractionation, primary sequence homology analysis, co-isolation of ribosome-free Sec61 complexes The Journal of biological chemistry Medium 10799540
2010 Human Sec62 has gained an evolutionary function absent in yeast: it interacts with the ribosomal tunnel exit and supports cotranslational protein transport into the ER. Sec62 is associated with ribosomes in human cells and interacts with Sec63. Ribosome co-sedimentation, co-immunoprecipitation of Sec62 with Sec63 and ribosomes, comparison with yeast ortholog Molecular biology of the cell Medium 20071467
2012 Silencing SEC62 in human cells specifically inhibits post-translational transport of signal-peptide-containing precursor proteins into the ER, whereas silencing SEC61A1 inhibits both co- and post-translational transport; Sec63 depletion affects the initial phase of co-translational transport. siRNA knockdown in HeLa cells, in vitro translocation assay with semi-permeabilized cells, substrate-specific analysis Journal of cell science High 22375059
2012 Sec62 is required for efficient post-translational translocation of small proteins (≤100 amino acids) with N-terminal signal sequences in mammalian cells; this Sec62-dependent pathway operates via the Sec61 translocon and requires ATP, functioning as a fail-safe mechanism independent of SRP. siRNA knockdown of Sec62 and SRP pathway components, in vitro translocation assays, size-class analysis of substrates Molecular biology of the cell High 22648169
2012 CK2 phosphorylates Sec63 at serine residues 574, 576, and 748, and this phosphorylation enhances the binding of Sec63 to Sec62, a prerequisite for functional ER protein translocation. CK2 phosphorylation mapping with deletion mutants and peptide library; pull-down assays and co-immunoprecipitation of Sec63 with Sec62 Biochimica et biophysica acta Medium 23287549
2013 SEC62 (TLOC1) is selectively required for proliferation of cell lines with 3q26 amplification; increased TLOC1 expression induces anchorage-independent growth; TLOC1 binds DDX3X, which is essential for TLOC1-induced cellular transformation. Loss- and gain-of-function genetic screens, proteomic binding studies identifying DDX3X interaction, anchorage-independent growth assays Cancer discovery Medium 23764425
2013 Sec62 directly interacts with the Sec61 complex in a Ca2+-sensitive manner; a Ca2+-binding motif in Sec62 is essential for its molecular function in regulating Ca2+ leakage through Sec61; SEC62 silencing elevates cytosolic Ca2+ and increases ER Ca2+ leakage after thapsigargin treatment. Biacore surface plasmon resonance (Ca2+-sensitive interaction assay), Ca2+ imaging, siRNA silencing, mutant SEC62 expression BMC cancer Medium 24304694
2013 In yeast, mutations in the N-terminal cytosolic domain of Sec62 impair its interaction with Sec63 and cause defects in membrane insertion and translocation of the C-terminus of membrane proteins, revealing a role for Sec62-Sec63 in topogenesis of membrane proteins. Yeast mutant analysis, systematic analysis of membrane proteins with varying hydrophobicity and topology, in vivo translocation assays The Journal of biological chemistry Medium 23632075
2014 The Sec62-Sec63 complex facilitates translocation of the C-terminus of membrane proteins in yeast; mutations in the N-terminal cytosolic domain of Sec62 disrupt Sec62-Sec63 interaction and impair C-terminal translocation of single- and multi-spanning membrane proteins. Systematic analysis of single and multi-spanning membrane proteins with varying hydrophobicity, flanking charges, and TM orientation in yeast sec62 mutant strains Journal of cell science Medium 25097231
2015 Blocking cotranslational translocation by passenger domain folding stabilizes an alternate translocon complex containing Sec61, Sec62, and Sec63; Sec62/63 stabilization within the translocon also occurs for native endogenous substrates (e.g., prion protein) and correlates with a delay in translocation initiation, demonstrating that Sec62/63 engagement is controlled by the nascent chain. Ribosome-nascent chain isolation, mass spectrometry of translocon complexes, crosslinking, cotranslational translocation assays with preprolactin and prion protein as substrates Molecular cell High 25801167
2015 The SRP receptor (SR) switches the Sec61 translocon from Sec62-dependent to SRP-dependent translocation by displacing Sec62 from Sec61; the charged linker region of SRα mediates this displacement, while a separate conserved element promotes ribosome binding. Truncation variant analysis of SRα, crosslinking assays, in vitro translocation assays demonstrating Sec62 displacement Nature communications Medium 26634806
2016 Sec62 functions as an ER-resident autophagy receptor during recovery from ER stress (recovER-phagy), selectively delivering ER components to autolysosomes; this requires a conserved LC3-interacting region (LIR) in the C-terminal cytosolic domain of Sec62, which is dispensable for protein translocation function. Autophagy flux assays, LC3-IP, LIR motif mutagenesis, live-cell imaging, fractionation, loss-of-function experiments in mammalian cells Nature cell biology High 27749824
2020 Human Sec62/Sec63 substrates share signal peptides with longer but less hydrophobic hydrophobic regions and lower C-region polarity; a slowly gating signal peptide combined with a downstream positively charged amino acid cluster is decisive for Sec62/Sec63 requirement, and these features also correlate with BiP requirement and sensitivity to the Sec61-channel inhibitor CAM741. Unbiased proteomics approach in intact human cells, siRNA knockdown of SEC62/SEC63, substrate signal peptide analysis of 22 newly identified substrates The FEBS journal Medium 32133789
2021 Cryo-EM structures of Sec61-Sec62-Sec63 complexes from yeast show that Sec63 and Sec62 stepwise activate Sec61 for post-translational translocation: Sec63 first partially opens the lateral gate via cytosolic and luminal domain interactions with Sec61, then Sec62 is required to displace the plug domain to open the translocation pore; Sec62 may also prevent lipids from entering the channel through the open lateral gate. Cryo-EM structure determination of multiple complex variants, molecular dynamics simulations, functional mutagenesis analysis Nature structural & molecular biology High 33398175
2021 Sec62 promotes stemness and chemoresistance of colorectal cancer cells by binding to β-catenin, inhibiting its degradation, and competitively disrupting the interaction between β-catenin and APC, thereby inhibiting β-catenin destruction complex assembly and activating Wnt signaling. GST pull-down, co-immunoprecipitation, western blot, siRNA knockdown, in vitro and in vivo functional experiments Journal of experimental & clinical cancer research : CR Medium 33858476
2021 ATG9A engages SEC62 (and FAM134B) on the cytosolic side of the ER to induce reticulophagy; this engagement depends on the acetylation status of ATG9A in the ER lumen, linking luminal acetylation to cytosolic ER-phagy receptor recruitment. ATG9A interactome analysis in two mouse models of AT-1 dysregulation (AT-1 sTg and AT-1S113R/+), co-immunoprecipitation iScience Medium 33870132
2022 Molecular dynamics simulations starting from cryo-EM structures show that Sec62 binding to Sec61 alters the conformational dynamics of the lateral gate, plug, and pore region: the luminal lateral gate adopts a wider (open) conformation when Sec62 is bound, while it closes in the apo state; the signal peptide stabilizes the active state conformation during post-translational translocation. Molecular dynamics simulations from cryo-EM structures of Sec61 with and without Sec62 Biochimica et biophysica acta. Biomembranes Low 36116515
2022 Sec62 promotes gastric cancer metastasis by binding LC3II and activating autophagy via the UPR-related PERK/ATF4 pathway with concomitant upregulation of FIP200/Beclin-1/Atg5; autophagy activation in turn alters TIMP-1/MMP2/9 balance to promote migration and invasion. Co-immunoprecipitation of Sec62 with LC3II, transmission electron microscopy for autophagy, mRFP-GFP-LC3 adenovirus reporter, siRNA knockdown, xenograft models Cellular and molecular life sciences : CMLS Medium 35165763
2025 SEC62 interacts directly with ATAD3B at mitochondria-associated membranes (MAMs), leading to downregulation of ATAD3B expression, defective mitophagy, increased mitochondrial ROS, and inflammatory responses; hepatocyte-specific SEC62 overexpression worsens and SEC62 knockout ameliorates MASH pathology. Co-immunoprecipitation of SEC62 with ATAD3B, hepatocyte-specific overexpression and knockout mouse models, mitophagy and ROS assays Metabolism: clinical and experimental Medium 42001994
2025 Cinobufagin directly binds SEC62 (validated by MST and CETSA); SEC62 interacts with TRPM4 (validated by SPR) and promotes its ubiquitination and proteasomal degradation; cinobufagin disrupts the SEC62/TRPM4 interaction, stabilizing TRPM4 and enabling NECSO cell death in bortezomib-resistant multiple myeloma cells. LiP-MS, molecular docking, MST and CETSA binding assays, SPR for SEC62-TRPM4 interaction, immunoprecipitation for ubiquitination, SEC62 knockdown rescue experiments Phytomedicine Medium 40839992
2026 SEC62-mediated ER-phagy activation in neurons alleviates Alzheimer's disease pathology (Aβ plaque deposition, neuroinflammation, cognitive impairment) in 5×FAD mice; ER-phagy receptor expression including SEC62 is decreased in AD patient iPSC-derived neurons and 5×FAD samples. AAV-mediated overexpression of SEC62 in 5×FAD mouse brain via intrathecal injection, Aβ plaque quantification, cognitive behavioral tests, iPSC-derived neuron analysis Molecular therapy Medium 42026868

Source papers

Stage 0 corpus · 61 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2016 Translocon component Sec62 acts in endoplasmic reticulum turnover during stress recovery. Nature cell biology 379 27749824
2021 Sec62 promotes stemness and chemoresistance of human colorectal cancer through activating Wnt/β-catenin pathway. Journal of experimental & clinical cancer research : CR 159 33858476
2000 Mammalian Sec61 is associated with Sec62 and Sec63. The Journal of biological chemistry 158 10799540
1989 SEC62 encodes a putative membrane protein required for protein translocation into the yeast endoplasmic reticulum. The Journal of cell biology 156 2687286
2017 Let's talk about Secs: Sec61, Sec62 and Sec63 in signal transduction, oncology and personalized medicine. Signal transduction and targeted therapy 140 29263911
2012 Different effects of Sec61α, Sec62 and Sec63 depletion on transport of polypeptides into the endoplasmic reticulum of mammalian cells. Journal of cell science 134 22375059
2005 HTP-1 coordinates synaptonemal complex assembly with homolog alignment during meiosis in C. elegans. Genes & development 126 16291647
2019 MiR-4429 prevented gastric cancer progression through targeting METTL3 to inhibit m6A-caused stabilization of SEC62. Biochemical and biophysical research communications 119 31395342
2012 Efficient secretion of small proteins in mammalian cells relies on Sec62-dependent posttranslational translocation. Molecular biology of the cell 100 22648169
2015 Cotranslational stabilization of Sec62/63 within the ER Sec61 translocon is controlled by distinct substrate-driven translocation events. Molecular cell 86 25801167
2010 Evolutionary gain of function for the ER membrane protein Sec62 from yeast to humans. Molecular biology of the cell 78 20071467
2012 Identification of cyclin B1 and Sec62 as biomarkers for recurrence in patients with HBV-related hepatocellular carcinoma after surgical resection. Molecular cancer 76 22682366
2013 Systematic interrogation of 3q26 identifies TLOC1 and SKIL as cancer drivers. Cancer discovery 72 23764425
2013 Targeting cell migration and the endoplasmic reticulum stress response with calmodulin antagonists: a clinically tested small molecule phenocopy of SEC62 gene silencing in human tumor cells. BMC cancer 72 24304694
2011 Sec62 bridges the gap from 3q amplification to molecular cell biology in non-small cell lung cancer. The American journal of pathology 70 22197383
2011 Silencing of the SEC62 gene inhibits migratory and invasive potential of various tumor cells. International journal of cancer 58 20669223
2006 Genomic and expression analysis of the 3q25-q26 amplification unit reveals TLOC1/SEC62 as a probable target gene in prostate cancer. Molecular cancer research : MCR 52 16547154
2021 Stepwise gating of the Sec61 protein-conducting channel by Sec63 and Sec62. Nature structural & molecular biology 49 33398175
2015 Mammalian SRP receptor switches the Sec61 translocase from Sec62 to SRP-dependent translocation. Nature communications 48 26634806
2020 Identification of signal peptide features for substrate specificity in human Sec62/Sec63-dependent ER protein import. The FEBS journal 46 32133789
2013 Sec62 protein mediates membrane insertion and orientation of moderately hydrophobic signal anchor proteins in the endoplasmic reticulum (ER). The Journal of biological chemistry 40 23632075
2011 Sec62 protein level is crucial for the ER stress tolerance of prostate cancer. The Prostate 36 21557272
2017 Effect of 3q oncogenes SEC62 and SOX2 on lymphatic metastasis and clinical outcome of head and neck squamous cell carcinomas. Oncotarget 35 28002801
2016 Identification of SEC62 as a potential marker for 3q amplification and cellular migration in dysplastic cervical lesions. BMC cancer 31 27553742
2022 Sec62 promotes gastric cancer metastasis through mediating UPR-induced autophagy activation. Cellular and molecular life sciences : CMLS 29 35165763
2014 The Sec62-Sec63 translocon facilitates translocation of the C-terminus of membrane proteins. Journal of cell science 29 25097231
2017 Role of SEC62 in ER maintenance: A link with ER stress tolerance in SEC62-overexpressing tumors? Molecular & cellular oncology 28 28401179
2021 Emerging View on the Molecular Functions of Sec62 and Sec63 in Protein Translocation. International journal of molecular sciences 27 34884562
2021 Sec62 Regulates Endoplasmic Reticulum Stress and Autophagy Balance to Affect Foot-and-Mouth Disease Virus Replication. Frontiers in cellular and infection microbiology 20 34532300
2012 CK2 phosphorylation of human Sec63 regulates its interaction with Sec62. Biochimica et biophysica acta 20 23287549
2020 ERK phosphorylates chromosomal axis component HORMA domain protein HTP-1 to regulate oocyte numbers. Science advances 19 33127680
2018 Treatment of SEC62 over-expressing tumors by Thapsigargin and Trifluoperazine. Biomolecular concepts 19 29779013
2019 Identification of 3q oncogene SEC62 as a marker for distant metastasis and poor clinical outcome in invasive ductal breast cancer. Archives of gynecology and obstetrics 18 30747329
1997 Identification of a human cDNA homologue to the Drosophila translocation protein 1 (Dtrp1). Biochemical and biophysical research communications 17 9020021
2019 Sec62 promotes early recurrence of hepatocellular carcinoma through activating integrinα/CAV1 signalling. Oncogenesis 16 31822656
2021 ATG9A regulates proteostasis through reticulophagy receptors FAM134B and SEC62 and folding chaperones CALR and HSPB1. iScience 15 33870132
2010 Hph1 and Hph2 are novel components of the Sec63/Sec62 posttranslational translocation complex that aid in vacuolar proton ATPase biogenesis. Eukaryotic cell 15 21097665
2022 Endoplasmic reticulum-resident protein Sec62 drives colorectal cancer metastasis via MAPK/ATF2/UCA1 axis. Cell proliferation 14 36200182
2022 The endoplasmic reticulum membrane protein Sec62 as potential therapeutic target in SEC62 overexpressing tumors. Frontiers in physiology 14 36262254
2022 PRP8-Induced CircMaml2 Facilitates the Healing of the Intestinal Mucosa via Recruiting PTBP1 and Regulating Sec62. Cells 13 36359856
2021 Expression of SEC62 Oncogene in Benign, Malignant and Borderline Melanocytic Tumors-Unmasking the Wolf in Sheep's Clothing? Cancers 11 33915997
2021 SEC62 and SEC63 Expression in Hepatocellular Carcinoma and Tumor-Surrounding Liver Tissue. Visceral medicine 11 33977099
2019 Sec62 Suppresses Foot-and-Mouth Disease Virus Proliferation by Promotion of IRE1α-RIG-I Antiviral Signaling. Journal of immunology (Baltimore, Md. : 1950) 11 31167774
2018 Expression of 3q oncogene SEC62 in atypical fibroxanthoma-immunohistochemical analysis of 41 cases and correlation with clinical, viral and histopathologic features. Oncology letters 10 30675236
2022 Antagonizing Sec62 function in intracellular Ca2+ homeostasis represents a novel therapeutic strategy for head and neck cancer. Frontiers in physiology 9 36045752
2021 Sec62 promotes pro-angiogenesis of hepatocellular carcinoma cells under hypoxia. Cell biochemistry and biophysics 9 34120320
2019 Sec62/Ki67 and p16/Ki67 dual-staining immunocytochemistry in vulvar cytology for the identification of vulvar intraepithelial neoplasia and vulvar cancer: a pilot study. Archives of gynecology and obstetrics 9 30607586
2024 Mild endoplasmic reticulum stress alleviates FB1-triggered intestinal pyroptosis via the Sec62-PERK pathway. Cell biology and toxicology 8 38769285
2018 Sec62/Ki67 dual staining in cervical cytology specimens: a new marker for high-grade dysplasia. Archives of gynecology and obstetrics 8 30498965
1997 Cloning the Yarrowia lipolytica homologue of the Saccharomyces cerevisiae SEC62 gene. Current genetics 5 9021129
2025 SEC62-dependent ER-phagy contributes to apelin-13/APJ-induced monocyte-vascular endothelial cell adhesion in atherosclerosis pathogenesis. Acta pharmacologica Sinica 4 39930135
2025 Cinobufagin overcomes bortezomib resistance in multiple myeloma strains by targeting SEC62/TRPM4-mediated NECSO. Phytomedicine : international journal of phytotherapy and phytopharmacology 3 40839992
2022 Effect of Sec62 on the conformation of the Sec61 channel in yeast. Biochimica et biophysica acta. Biomembranes 3 36116515
2023 The 3q Oncogene SEC62 Predicts Response to Neoadjuvant Chemotherapy and Regulates Tumor Cell Migration in Triple Negative Breast Cancer. International journal of molecular sciences 2 37298528
2023 Dual Sec62/Ki67 immunocytochemistry of liquid-based cytological preparations represents a highly valid biomarker for non-invasive detection of head and neck squamous cell carcinomas. Cytopathology : official journal of the British Society for Clinical Cytology 2 37787092
2023 Expression of 3q Oncogene SEC62 Predicts Survival in Head and Neck Squamous Cell Carcinoma Patients Treated with Primary Chemoradiation. Cancers 2 38201525
2026 Sec62 restricts ER-replicating positive-strand RNA virus infections via UPR-dependent ER-phagy. The Plant cell 1 41592053
1999 Fine structure of the human translocation protein 1 (HTP1/TLOC1) gene. IUBMB life 1 10683767
2026 SEC62 at mitochondria-associated membranes drives MASH progression by suppressing ATAD3B-mediated mitochondrial quality control. Metabolism: clinical and experimental 0 42001994
2026 SEC62-mediated ER-phagy activation alleviates Alzheimer's disease pathology and restores cognitive function in 5×FAD mice. Molecular therapy : the journal of the American Society of Gene Therapy 0 42026868
2025 Sec61s and Sec62/Sec63 Genes Are Essential for Survival by Regulating the Gut and Cuticle Development in Locusta migratoria. Insects 0 40558980

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