Affinage

SEC62

Translocation protein SEC62 · UniProt Q99442

Length
399 aa
Mass
45.9 kDa
Annotated
2026-04-28
61 papers in source corpus 25 papers cited in narrative 25 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SEC62 is a conserved ER membrane protein that functions as a core component of the Sec61–Sec62–Sec63 post-translational translocation channel and as an ER-phagy receptor, linking ER protein import to ER quality control. In the translocation channel, Sec62 opens the Sec61 pore by displacing its plug domain in a hierarchical mechanism with Sec63, and is specifically required for post-translational import of substrates with less hydrophobic signal peptides, including small secretory proteins; the SRP receptor switches the translocon from Sec62-dependent to SRP-dependent mode by physically displacing Sec62 from Sec61 (PMID:33398175, PMID:22375059, PMID:26634806). Independent of its translocation role, Sec62 acts as a selective ER-phagy (recovER-phagy) receptor during ER stress recovery through a C-terminal LC3-interacting region that recruits autophagic machinery, a function with physiological consequences in atherosclerosis, neurodegeneration, and liver disease (PMID:27749824, PMID:39930135, PMID:42026868). SEC62 additionally regulates ER Ca²⁺ leak through Ca²⁺-sensitive interaction with Sec61 and promotes oncogenic signaling by stabilizing β-catenin against destruction-complex-mediated degradation and by activating the MAPK/JNK pathway (PMID:24304694, PMID:33858476, PMID:36200182).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 1989 High

    Identification of SEC62 as an ER membrane component required for post-translational protein translocation established its fundamental cellular role, resolving whether the translocation defect was membrane-intrinsic or cytosolic.

    Evidence In vitro translocation assay with sec62 mutant membranes/cytosol fractionation in yeast

    PMID:2687286

    Open questions at the time
    • No structural information on SEC62
    • Mammalian ortholog not yet identified
    • Mechanism of SEC62 action at the translocon unknown
  2. 2000 High

    Demonstration that mammalian Sec62 physically associates with Sec61 and Sec63 in a ribosome-free complex established the conservation of the post-translational translocation machinery from yeast to mammals.

    Evidence Reciprocal co-immunoprecipitation and biochemical fractionation of mammalian ER membranes

    PMID:10799540

    Open questions at the time
    • Substrate specificity of the mammalian complex unknown
    • Whether Sec62 has gained new functions in mammals unclear
  3. 2010 Medium

    Discovery that human Sec62 can interact with the ribosomal tunnel exit raised the possibility that mammalian Sec62 has acquired cotranslational roles beyond its conserved post-translational function.

    Evidence Co-immunoprecipitation of Sec62 with ribosomes in human cells

    PMID:20071467

    Open questions at the time
    • Functional significance of ribosome interaction for cotranslational transport not demonstrated
    • No structural detail of this interface
  4. 2012 High

    Systematic substrate analysis established that Sec62 is specifically required for post-translational (not cotranslational) ER import in mammalian cells, particularly for small secretory proteins with N-terminal signal sequences, revealing SEC62 as a fail-safe for the SRP pathway.

    Evidence siRNA knockdown in HeLa cells with in vitro translocation assays across multiple substrate classes; SRP pathway impairment combined with SEC62 RNAi

    PMID:22375059 PMID:22648169

    Open questions at the time
    • Full client proteome not defined
    • Signal peptide features dictating Sec62 dependence not characterized
  5. 2012 Medium

    CK2 phosphorylation of Sec63 was shown to enhance its binding to Sec62, revealing a regulatory input that controls assembly of the functional translocon.

    Evidence Phosphorylation mapping with CK2 and co-immunoprecipitation of Sec62–Sec63

    PMID:23287549

    Open questions at the time
    • In vivo relevance of CK2-mediated regulation not tested
    • Whether phosphorylation affects translocation efficiency directly unknown
  6. 2013 Medium

    Two discoveries expanded SEC62's roles: Sec62 was found to regulate signal anchor protein orientation during membrane insertion, and to regulate ER Ca²⁺ leak through a Ca²⁺-sensitive direct interaction with Sec61.

    Evidence Yeast Sec62 mutant analysis with model membrane proteins of varying topology; SPR interaction analysis and Ca²⁺ imaging with SEC62 siRNA depletion in human cells

    PMID:23632075 PMID:24304694

    Open questions at the time
    • Structural basis of Ca²⁺-sensitive Sec62–Sec61 interaction unknown
    • Whether Ca²⁺ regulation and translocation functions are separable unclear
  7. 2015 High

    The SRP receptor was shown to physically displace Sec62 from Sec61, establishing the molecular switch mechanism between post-translational and cotranslational translocation modes, and Sec62/63 were found to be recruited when translocation initiation is delayed.

    Evidence Crosslinking and translocation assays with SRα truncation variants; ribosome-nascent chain complex isolation with co-IP of translocon components

    PMID:25801167 PMID:26634806

    Open questions at the time
    • Structural basis of SRα-mediated Sec62 displacement not resolved
    • How translocation kinetics regulate Sec62/63 recruitment mechanistically unclear
  8. 2016 High

    The discovery that Sec62 functions as a selective ER-phagy receptor (recovER-phagy) through its C-terminal LIR motif — independent of its translocation role — revealed a second major function for this protein in ER homeostasis.

    Evidence LIR motif mutagenesis separating translocation and autophagy functions; autophagy flux assays during ER stress recovery

    PMID:27749824

    Open questions at the time
    • Cargo selectivity mechanism for ER-phagy not defined
    • How SEC62-mediated ER-phagy is initiated and terminated unclear
  9. 2020 High

    Unbiased proteomics identified the signal peptide code for Sec62/Sec63 dependence — longer, less hydrophobic h-regions plus downstream positively charged residues — defining the substrate selection rules for this translocation pathway.

    Evidence In-cell protein import assay with siRNA knockdown; signal peptide mutagenesis across 22 novel substrates

    PMID:32789789

    Open questions at the time
    • How signal peptide features mechanistically engage Sec62/Sec63 to open Sec61 not resolved at atomic level
  10. 2021 High

    Cryo-EM structures of the Sec61–Sec62–Sec63 complex revealed the stepwise gating mechanism: Sec63 first partially opens the Sec61 lateral gate, then Sec62 displaces the plug domain to open the pore, resolving the long-standing question of how post-translational translocation is activated.

    Evidence Cryo-EM structures from S. cerevisiae and T. lanuginosus with mutagenesis validation and MD simulations

    PMID:33398175

    Open questions at the time
    • Structure of a substrate-engaged complex not available
    • Lipid-blocking role of Sec62 at the lateral gate not experimentally validated
  11. 2021 Medium

    Multiple studies established SEC62 as an oncogenic factor acting through diverse signaling pathways: binding and stabilizing β-catenin to activate Wnt signaling, activating MAPK/JNK to drive metastasis, and interacting with DDX3X to promote cellular transformation.

    Evidence GST pulldown and co-IP for β-catenin interaction; JNK inhibitor rescue and ChIP assays; proteomic identification of DDX3X interaction with transformation assays

    PMID:23764425 PMID:33858476 PMID:36200182

    Open questions at the time
    • How an ER membrane protein accesses cytoplasmic/nuclear β-catenin mechanistically unresolved
    • Whether oncogenic functions depend on translocation or ER-phagy activities unknown
    • Single-lab findings for each pathway
  12. 2025 Medium

    SEC62-mediated ER-phagy was shown to have broad pathophysiological relevance: promoting atherosclerosis in endothelial cells, being deficient in Alzheimer's disease neurons (where its restoration reduces Aβ pathology), and interacting with ATAD3B at MAMs to suppress mitophagy and drive MASH.

    Evidence Endothelial-specific SEC62 KO in APOE−/− mice; AAV-SEC62 overexpression in 5×FAD mice; hepatocyte-specific SEC62 KO and overexpression with mitophagy assays

    PMID:39930135 PMID:42001994 PMID:42026868

    Open questions at the time
    • Whether MAM localization represents a distinct pool from ER-phagy receptor pool unclear
    • Upstream signals controlling SEC62 expression in disease contexts incompletely mapped
    • Single-lab studies for each disease model
  13. 2025 Medium

    SEC62 was found to promote TRPM4 ubiquitination and proteasomal degradation through direct interaction, linking SEC62 to ion channel proteostasis and drug resistance in myeloma.

    Evidence SPR, MST, and CETSA target engagement assays; ubiquitination immunoprecipitation; SEC62 knockdown

    PMID:40839992

    Open questions at the time
    • E3 ligase mediating TRPM4 ubiquitination through SEC62 not identified
    • Whether this represents a general SEC62 function in membrane protein quality control unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include: the structure of a substrate-engaged Sec61–Sec62–Sec63 complex, how SEC62 transitions between its translocation and ER-phagy receptor functions, the mechanism by which an ER membrane protein activates cytoplasmic signaling pathways (Wnt, MAPK/JNK), and the structural basis by which SEC62's intrinsically disordered regions drive ER membrane fragmentation during ER-phagy.
  • No substrate-engaged cryo-EM structure
  • Functional switching mechanism between translocation and ER-phagy roles uncharacterized
  • Structural basis of ER fragmentation by SEC62 IDRs not peer-review validated

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 5 GO:0038024 cargo receptor activity 3 GO:0098772 molecular function regulator activity 3
Localization
GO:0005783 endoplasmic reticulum 5 GO:0005886 plasma membrane 2
Pathway
R-HSA-9609507 Protein localization 6 R-HSA-9612973 Autophagy 5 R-HSA-392499 Metabolism of proteins 3 R-HSA-162582 Signal Transduction 2
Partners
ATAD3BATG9ACTNNB1DDX3XLC3SEC61A1SEC63TRPM4
Complex memberships
Sec61-Sec62-Sec63 translocon

Evidence

Reading pass · 25 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1989 Yeast SEC62 encodes a membrane protein required for post-translational translocation of secretory precursor proteins into the ER lumen; the defect is membrane-specific (not cytosolic), and the protein is predicted to have two transmembrane domains with cytoplasmic N- and C-terminal domains including a C-terminal basic amphipathic helix for protein–protein interactions. In vitro translocation assay with sec62 mutant membranes/cytosol fractionation; DNA sequence analysis The Journal of cell biology High 2687286
2000 Mammalian Sec62 physically associates with Sec61 and Sec63 in a ribosome-free complex in the ER membrane, forming a mammalian counterpart of the yeast Sec61p–Sec62p–Sec63p post-translational translocation complex. Biochemical fractionation, co-immunoprecipitation, primary sequence homology analysis The Journal of biological chemistry High 10799540
2010 Human Sec62 interacts with Sec63 (conserved from yeast) and additionally has gained the ability to interact with the ribosomal tunnel exit, supporting cotranslational protein transport into the ER—a function not present in yeast Sec62. Co-immunoprecipitation of Sec62 with ribosomes; interaction assays between Sec62 and Sec63 Molecular biology of the cell Medium 20071467
2012 Silencing SEC62 in human cells specifically inhibits post-translational (but not co-translational) transport of signal-peptide-containing precursor proteins into the ER, demonstrating a substrate-specific role for Sec62 in mammalian post-translational translocation. siRNA knockdown in HeLa cells; in vitro translocation assay with semi-permeabilized cells Journal of cell science High 22375059
2012 Mammalian Sec62-dependent translocation occurs post-translationally via the Sec61 translocon, requires ATP, and is specifically required for efficient secretion of small proteins (≤100 amino acids) with N-terminal signal sequences, serving as a fail-safe for the SRP pathway. SRP pathway impairment combined with SEC62 RNAi; in vitro translocation assays categorizing substrates by size Molecular biology of the cell High 22648169
2012 Protein kinase CK2 phosphorylates human Sec63 at serine residues 574, 576, and 748, and this phosphorylation enhances Sec63 binding to Sec62, which is a prerequisite for a functional ER protein translocon. CK2 phosphorylation mapping with deletion mutants and peptide library; pull-down and co-immunoprecipitation assays Biochimica et biophysica acta Medium 23287549
2013 Sec62 mediates membrane insertion and orientation of moderately hydrophobic signal anchor proteins in the ER; defects in Sec62 selectively reduce translocation of type II (N-in, C-out) membrane topology, indicating a role in regulating signal sequence orientation during early translocation. Yeast Sec62 mutant strains; systematic analysis of model proteins with varying hydrophobicity and topology The Journal of biological chemistry Medium 23632075
2013 Sec62 protein directly and Ca2+-sensitively interacts with the Sec61 complex (major ER Ca2+ leak channel), and a Ca2+-binding motif in Sec62 is essential for this function; SEC62 silencing leads to elevated cytosolic Ca2+ and increased ER Ca2+ leakage, and Sec62 is required for tumor cell migration. Biacore surface plasmon resonance interaction analysis; Ca2+ imaging; siRNA depletion with migration assays; Ca2+-binding motif mutagenesis BMC cancer Medium 24304694
2014 The Sec62–Sec63 complex in yeast facilitates translocation of the C-terminus of membrane proteins; mutations in the N-terminal cytosolic domain of Sec62 impair its interaction with Sec63 and cause defects in membrane insertion and C-terminal translocation of both single- and multi-spanning membrane proteins. Yeast Sec62 N-terminal domain mutants; co-IP to assess Sec62–Sec63 interaction; systematic analysis of single and multi-spanning membrane proteins Journal of cell science Medium 25097231
2015 The SRP receptor (SRα) switches the Sec61 translocase from Sec62-dependent to SRP-dependent translocation by physically displacing Sec62 from Sec61; the charged linker region of SRα (between longin and GTPase domains) mediates this displacement. Truncation variants of SRα; crosslinking; in vitro translocation assays; co-immunoprecipitation Nature communications High 26634806
2015 Sec62 and Sec63 are stabilized within the Sec61 translocon when the nascent polypeptide encounters a delay in translocation initiation (e.g., by passenger domain folding); the engaged nascent chain controls translocon composition, with Sec62/63-containing complexes forming when translocation initiation is slow. Ribosome-nascent chain complex isolation; co-immunoprecipitation of translocon components at defined translocation stages using model substrate preprolactin Molecular cell High 25801167
2016 Sec62 acts as an ER-resident autophagy receptor (recovER-phagy receptor) during recovery from ER stress, selectively delivering excess ER components to the autolysosomal system; this function requires a conserved LC3-interacting region (LIR) in the C-terminal cytosolic domain of Sec62, which is dispensable for its protein translocation function. Live-cell imaging; loss-of-function studies; LIR motif mutagenesis; autophagy flux assays in ER stress recovery conditions Nature cell biology High 27749824
2020 Human Sec62/Sec63-dependent ER import substrates share signal peptides with longer but less hydrophobic h-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, which may involve Sec62/Sec63 supporting Sec61-channel opening via direct interaction with the N-terminal cytosolic peptide of Sec61α or via BiP recruitment to ER-lumenal loop 7. Unbiased proteomics (in-cell protein import assay); siRNA knockdown; signal peptide mutagenesis; identification of 22 novel substrates The FEBS journal High 32133789
2021 Cryo-EM structures of Sec61-Sec62-Sec63 complexes from S. cerevisiae and T. lanuginosus show that Sec62 and Sec63 activate Sec61 for post-translational translocation in a stepwise/hierarchical manner: Sec63 first partially opens the Sec61 lateral gate through cytosolic and luminal domain interactions, then Sec62 opens the translocation pore by displacing the plug domain; Sec62 may also prevent lipid invasion through the open lateral gate. Cryo-electron microscopy structure determination; molecular dynamics simulations; mutagenesis of Sec61–Sec63 interface residues Nature structural & molecular biology High 33398175
2021 ATG9A acetylation status in the ER lumen controls induction of reticulophagy, and this requires ATG9A to engage SEC62 (as well as FAM134B) on the cytosolic side of the ER membrane. ATG9A interactome analysis in two mouse models of AT-1 dysregulation; co-immunoprecipitation iScience Medium 33870132
2021 Sec62 promotes gastric cancer metastasis by binding to LC3II and activating autophagy via the PERK/ATF4 pathway, with concomitant FIP200/Beclin-1/Atg5 activation; autophagy blockage abolishes Sec62-driven cell migration and invasion. Co-immunoprecipitation of Sec62 with LC3II; Western blot for UPR/autophagy markers; transwell migration/invasion assays; xenograft models; autophagy inhibitor rescue experiments Cellular and molecular life sciences : CMLS Medium 35165763
2021 SEC62 binds DDX3X, and DDX3X is essential for TLOC1/SEC62-induced oncogenic transformation (anchorage-independent growth); this interaction was identified by proteomic studies. Proteomic interaction studies (pulldown/MS); loss-of-function genetic screen; gain-of-function transformation assays Cancer discovery Medium 23764425
2021 SEC62 binds β-catenin and inhibits its degradation by competitively disrupting the interaction between β-catenin and APC, thereby preventing assembly of the β-catenin destruction complex and activating Wnt/β-catenin signaling in colorectal cancer cells. GST pull-down; co-immunoprecipitation; Western blot for β-catenin destruction complex components; siRNA loss-of-function with phenotypic readouts Journal of experimental & clinical cancer research : CR Medium 33858476
2022 SEC62 activates the MAPK/JNK signaling pathway, leading to ATF2-mediated transcriptional upregulation of the lncRNA UCA1, which promotes colorectal cancer metastasis; blocking or activating JNK suppresses or enhances Sec62-mediated metastasis. RNA sequencing; rescue experiments with JNK inhibitor/agonist; luciferase reporter assay; ChIP assay; transwell/wound healing assays Cell proliferation Medium 36200182
2022 Molecular dynamics simulations starting from cryo-EM structures show that the presence of Sec62 alters the conformational dynamics of the Sec61 lateral gate, plug, and pore region; without Sec62, the luminal side of the lateral gate closes toward the apo state, while with Sec62 bound it adopts a wider (active) conformation. Molecular dynamics simulations based on cryo-EM structures of Sec61 with/without Sec62 Biochimica et biophysica acta. Biomembranes Low 36116515
2025 SEC62 directly interacts with TRPM4 and promotes TRPM4 ubiquitination and proteasomal degradation; the compound cinobufagin binds SEC62 and disrupts the SEC62–TRPM4 interaction, thereby stabilizing TRPM4 and inducing necrosis by sodium overload in bortezomib-resistant myeloma cells. LiP-MS, molecular docking, MST and CETSA target engagement assays; SPR for SEC62–TRPM4 interaction; immunoprecipitation for ubiquitination; SEC62 knockdown validation Phytomedicine Medium 40839992
2025 SEC62-dependent ER-phagy in vascular endothelial cells promotes monocyte–endothelial cell adhesion and atherosclerosis; apelin-13 upregulates SEC62 to induce ER-phagy, and vascular endothelial cell-specific SEC62 deletion reduces atherosclerotic plaques in APOE-/- mice. Mechanistically, UBL4A mediates ubiquitin-like modification of ALDH1L1 at lysine-812, promoting ALDH1L1 insertion into the ER membrane and SEC62-dependent ER-phagy. siRNA knockdown; cell-specific knockout in APOE-/- mice with high-fat diet; co-immunoprecipitation; ubiquitination assay with lysine mutant Acta pharmacologica Sinica Medium 39930135
2026 SEC62 at mitochondria-associated membranes (MAMs) interacts directly with ATAD3B and suppresses ATAD3B expression, causing defective mitophagy, increased mitochondrial ROS, and inflammation, thereby driving MASH progression; hepatocyte-specific SEC62 overexpression worsens and SEC62 knockout ameliorates MASH phenotypes. Co-immunoprecipitation (SEC62–ATAD3B interaction); hepatocyte-specific KO and overexpression mouse models; mitophagy and ROS assays Metabolism: clinical and experimental Medium 42001994
2026 SEC62-mediated ER-phagy is deficient in Alzheimer's disease neurons; AAV-driven overexpression of SEC62 in 5×FAD mouse brains reduces Aβ plaque deposition, neuroinflammation, and cognitive impairment, establishing SEC62 ER-phagy as a mechanism for ER quality control relevant to AD pathology. Intrathecal AAV injection in 5×FAD mice; behavioral assays; immunostaining for Aβ and neuroinflammation markers; iPSC-derived neurons from AD patients Molecular therapy Medium 42026868
2024 The intrinsically disordered regions (IDRs) of SEC62 exposed at the cytoplasmic face of the ER membrane (not its transmembrane domains) drive ER fragmentation during ER-phagy; the transmembrane domains determine sub-compartmental distribution but are dispensable for fragmentation. Domain swap experiments; live-cell imaging of ER fragmentation; loss-of-function and gain-of-function constructs for IDR and transmembrane domains bioRxivpreprint Low bio_10.1101_2024.06.18.599470

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 374 27749824
2000 Mammalian Sec61 is associated with Sec62 and Sec63. The Journal of biological chemistry 158 10799540
2021 Sec62 promotes stemness and chemoresistance of human colorectal cancer through activating Wnt/β-catenin pathway. Journal of experimental & clinical cancer research : CR 156 33858476
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 137 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 133 22375059
2005 HTP-1 coordinates synaptonemal complex assembly with homolog alignment during meiosis in C. elegans. Genes & development 124 16291647
2019 MiR-4429 prevented gastric cancer progression through targeting METTL3 to inhibit m6A-caused stabilization of SEC62. Biochemical and biophysical research communications 118 31395342
2012 Efficient secretion of small proteins in mammalian cells relies on Sec62-dependent posttranslational translocation. Molecular biology of the cell 99 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 75 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 71 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 47 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 26 34884562
2012 CK2 phosphorylation of human Sec63 regulates its interaction with Sec62. Biochimica et biophysica acta 20 23287549
2021 Sec62 Regulates Endoplasmic Reticulum Stress and Autophagy Balance to Affect Foot-and-Mouth Disease Virus Replication. Frontiers in cellular and infection microbiology 19 34532300
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
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
2021 ATG9A regulates proteostasis through reticulophagy receptors FAM134B and SEC62 and folding chaperones CALR and HSPB1. iScience 14 33870132
2022 PRP8-Induced CircMaml2 Facilitates the Healing of the Intestinal Mucosa via Recruiting PTBP1 and Regulating Sec62. Cells 12 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) 10 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
2018 Sec62/Ki67 dual staining in cervical cytology specimens: a new marker for high-grade dysplasia. Archives of gynecology and obstetrics 8 30498965
2024 Mild endoplasmic reticulum stress alleviates FB1-triggered intestinal pyroptosis via the Sec62-PERK pathway. Cell biology and toxicology 7 38769285
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
2022 Effect of Sec62 on the conformation of the Sec61 channel in yeast. Biochimica et biophysica acta. Biomembranes 3 36116515
2025 Cinobufagin overcomes bortezomib resistance in multiple myeloma strains by targeting SEC62/TRPM4-mediated NECSO. Phytomedicine : international journal of phytotherapy and phytopharmacology 2 40839992
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
2026 Sec62 restricts ER-replicating positive-strand RNA virus infections via UPR-dependent ER-phagy. The Plant cell 1 41592053
2023 Expression of 3q Oncogene SEC62 Predicts Survival in Head and Neck Squamous Cell Carcinoma Patients Treated with Primary Chemoradiation. Cancers 1 38201525
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