SEC23A is one of two human paralogs of SEC23, the GTPase-activating subunit of the COPII inner coat. In the cytosol it forms a heterodimer with a SEC24 isoform (SEC24A-D); SAR1-GTP on the ER membrane recruits SEC23-SEC24 to ER exit sites, where SEC24 (and to a lesser extent SEC23) captures cargo, SEC23 binds SEC13-SEC31 outer-coat PPP motifs through its C-terminal gelsolin-like domain, and SEC23 stimulates SAR1 GTP hydrolysis to control coat turnover. Together these drive cargo concentration and budding of COPII carriers for ER-to-Golgi transport. The same gelsolin-like domain binds PPP motifs in the proline-rich domains of the procollagen export receptor TANGO1 (MIA3) and cTAGE5 (MIA2) at ER exit sites. SEC23A is a zinc-binding protein (N-terminal Sec23/Sec24-type zinc finger) of about 85 kDa, ubiquitously expressed, cycling between cytosol, the cytoplasmic face of the transitional ER and COPII vesicles. A homozygous F382L substitution impairs SEC13-SEC31 recruitment and causes cranio-lenticulo-sutural dysplasia, with ER distension and defective collagen secretion.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000139 Golgi membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Golgi membrane, transferred by orthology from mouse Sec23a. Reason: SEC23 is shed largely before COPII carriers fuse, but residual SEC23 on tethered carriers engages TRAPP at the cis-Golgi/ERGIC (Reactome R-HSA-5694439). A Golgi-membrane location is therefore peripheral to the ER exit site, where SEC23A acts; no human data place it in Golgi membranes. Supporting Evidence: Reactome:R-HSA-203973 SAR1:GTPase activity may result in partial uncoating of the emerging vesicle, allowing SEC23 to be exposed for subsequent TRAPPCII binding. |
| GO:0005096 GTPase activator activity | IBA GO_REF:0000033 | ACCEPT | Summary: SAR1 GTPase-activating activity, inferred by PAINT from node PTN000124617 with yeast Sec23 experimental donors. Reason: Sec23 is the GAP for Sar1 in the COPII coat; the activity was established for yeast Sec23p and placed by PAINT at the ancestral SEC23 node, from which human SEC23A (PTHR11141:SF7) descends. Human SEC23A binds SAR1A/SAR1B directly (PMID:32358066) and Reactome models Sec23-stimulated Sar1 GTP hydrolysis. In this review the GAP activity of human SEC23A specifically rests on this phylogenetic inference plus the conserved SAR1-binding interface; no cached human GAP assay was found. Supporting Evidence: PMID:36594468 SEC23 also functions as the GTPase-activating protein for SAR1 and stimulates SAR1 GTP hydrolysis. Reactome:R-HSA-5694527 Sar1p-GTP hydrolysis is increased 15-30-fold by Sec23p. PMID:32358066 We found that the latter cluster confers to SAR1B a binding preference for SEC23A that is stronger than that of SAR1A for SEC23A. |
| GO:0005515 protein binding | IPI PMID:10075675 Sec24 proteins and sorting at the endoplasmic reticulum. | REMOVE | Summary: Interaction of SEC23A with SEC24B reported by co-immunoprecipitation of human SEC24 isoforms with hSec23A. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:10075675 Sec24 proteins and sorting at the endoplasmic reticulum. | REMOVE | Summary: Interaction of SEC23A with SEC24C reported by co-immunoprecipitation of human SEC24 isoforms with hSec23A. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:16091426 PCTAIRE protein kinases interact directly with the COPII com... | MODIFY | Summary: Direct interaction of SEC23 with PCTAIRE kinase CDK16 (PCTAIRE-1) shown by two-hybrid, direct binding and immunoprecipitation. Reason: The partner is a protein kinase and the interaction is direct; protein kinase binding is more informative than generic protein binding. The regulatory significance for COPII function is modest and non-core. Proposed replacements: protein kinase binding Supporting Evidence: PMID:16091426 Here we show that the Sec23p subunit of COPII interacts with PCTAIRE protein kinases. This interaction is shown using two-hybrid screening, direct binding and immunoprecipitation. |
| GO:0005515 protein binding | IPI PMID:17499046 The transport signal on Sec22 for packaging into COPII-coate... | MODIFY | Summary: Crystal structure of human Sec23a/Sec24a bound to SEC22B (SEC22B); SEC22B binds at the Sec23/24 interface via a folded conformational transport signal. Reason: The interaction is a specific SNARE-cargo recognition event by the Sec23/24 inner coat, so SNARE binding is the informative MF. Binding requires the Sec23/24 heterodimer interface rather than SEC23A alone, which is noted here but does not change the term choice. Proposed replacements: SNARE binding Supporting Evidence: PMID:17499046 The SNARE protein Sec22 contains a signal that binds the COPII subcomplex Sec23/24 and specifies its endoplasmic reticulum (ER) exit as an unassembled SNARE. PMID:17499046 The 200 kDa crystal structure of Sec22 bound to Sec23/24 reveals that the transport signal is a folded epitope rather than a conventional short peptide sequence. |
| GO:0005515 protein binding | IPI PMID:18692470 Structural basis for cargo regulation of COPII coat assembly... | REMOVE | Summary: Interaction of SEC23A with SEC24C reported by COPII coat reconstitution with purified Sec23-24 and Sec13-31. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:18843296 Structural basis of cargo membrane protein discrimination by... | REMOVE | Summary: Interaction of SEC23A with SEC24D reported by structural and biochemical studies of human Sec23/Sec24 isoform complexes. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:20946353 Receptor-mediated ER export of human MHC class I molecules i... | MODIFY | Summary: Binding of the Sec23/24 complex to the C-terminal export signal of MHC class I heavy chain (HLA-A). Reason: The cited abstract identifies binding of the MHC-I C-terminal ER export signal to Sec23/24, an informative cargo-recognition interaction; MHC class I protein binding is the precise MF. Abstract-only cache; the abstract states the binding directly. Proposed replacements: MHC class I protein binding Supporting Evidence: PMID:20946353 These amino acids, conserved in nearly all known human MHC-I alleles, serve as the ER export signal by binding to the Sec23/24 complex, a structural component of coat protein complex II (COPII) vesicles that mediate ER-to-Golgi trafficking. |
| GO:0005515 protein binding | IPI PMID:27018634 Quantitative Mass Spectrometry Identifies Novel Host Binding... | REMOVE | Summary: Interaction of SEC23A with SEC24B, Q12959, Q8XAJ5 reported by a quantitative proteomics screen for pathogen effector partners. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:27551091 TANGO1/cTAGE5 receptor as a polyvalent template for assembly... | MODIFY | Summary: SEC23A binds the proline-rich domain of the ER-exit-site cargo receptor MIA3/TANGO1 through PPP motifs recognised by its gelsolin-like domain (crystal structures and mutagenesis, Ma & Goldberg 2016; pull-down, Maeda et al. 2017). Reason: The structural and mutational data define a specific binding mode: the SEC23A gelsolin-like domain recognises PPP motifs in the TANGO1/cTAGE5 proline-rich domains (and in SEC31). Proline-rich region binding captures this informatively. Proposed replacements: proline-rich region binding Supporting Evidence: PMID:27551091 The affinity for Sec23 is concentrated in the proline-rich domains (PRDs) of TANGO1 and cTAGE5, but Sec23 recognizes merely a PPP motif. PMID:27551091 difference electron density reveals just a three-residue peptide element bound to a site on the gelsolin-like domain of Sec23a |
| GO:0005515 protein binding | IPI PMID:27551091 TANGO1/cTAGE5 receptor as a polyvalent template for assembly... | MODIFY | Summary: SEC23A binds the proline-rich domain of the ER-exit-site cargo receptor MIA2/cTAGE5 isoform through PPP motifs recognised by its gelsolin-like domain (crystal structures and mutagenesis, Ma & Goldberg 2016; pull-down, Maeda et al. 2017). Reason: The structural and mutational data define a specific binding mode: the SEC23A gelsolin-like domain recognises PPP motifs in the TANGO1/cTAGE5 proline-rich domains (and in SEC31). Proline-rich region binding captures this informatively. Proposed replacements: proline-rich region binding Supporting Evidence: PMID:27551091 The affinity for Sec23 is concentrated in the proline-rich domains (PRDs) of TANGO1 and cTAGE5, but Sec23 recognizes merely a PPP motif. PMID:27551091 difference electron density reveals just a three-residue peptide element bound to a site on the gelsolin-like domain of Sec23a |
| GO:0005515 protein binding | IPI PMID:28442536 TANGO1 recruits Sec16 to coordinately organize ER exit sites... | MODIFY | Summary: SEC23A binds the proline-rich domain of the ER-exit-site cargo receptor MIA3/TANGO1 through PPP motifs recognised by its gelsolin-like domain (crystal structures and mutagenesis, Ma & Goldberg 2016; pull-down, Maeda et al. 2017). Reason: The structural and mutational data define a specific binding mode: the SEC23A gelsolin-like domain recognises PPP motifs in the TANGO1/cTAGE5 proline-rich domains (and in SEC31). Proline-rich region binding captures this informatively. Proposed replacements: proline-rich region binding Supporting Evidence: PMID:28442536 Because TANGO1’s PRD has also been reported to interact with Sec23 (Saito et al., 2009; Ma and Goldberg, 2016), we next tested the interaction with Sec23 (Fig. S3). PMID:27551091 The affinity for Sec23 is concentrated in the proline-rich domains (PRDs) of TANGO1 and cTAGE5, but Sec23 recognizes merely a PPP motif. |
| GO:0005515 protein binding | IPI PMID:31806350 The ER-Localized Transmembrane Protein TMEM39A/SUSR2 Regulat... | REMOVE | Summary: Interaction of SEC23A with SACM1L reported by co-immunoprecipitation with TMEM39A/SAC1 (abstract-only). Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:31806350 The ER-Localized Transmembrane Protein TMEM39A/SUSR2 Regulat... | REMOVE | Summary: Interaction of SEC23A with TMEM39A reported by co-immunoprecipitation with TMEM39A/SAC1 (abstract-only). Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of SEC23A with A2RRN7 reported by the HuRI binary yeast two-hybrid reference interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of SEC23A with O43557 reported by the HuRI binary yeast two-hybrid reference interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of SEC23A with O75477 reported by the HuRI binary yeast two-hybrid reference interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of SEC23A with O75928-2 reported by the HuRI binary yeast two-hybrid reference interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of SEC23A with SEC24D isoform 2 reported by the HuRI binary yeast two-hybrid reference interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of SEC23A with P30825 reported by the HuRI binary yeast two-hybrid reference interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of SEC23A with P48023 reported by the HuRI binary yeast two-hybrid reference interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of SEC23A with P48165 reported by the HuRI binary yeast two-hybrid reference interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of SEC23A with P50570 reported by the HuRI binary yeast two-hybrid reference interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of SEC23A with Q12983 reported by the HuRI binary yeast two-hybrid reference interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of SEC23A with SEC23B reported by the HuRI binary yeast two-hybrid reference interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of SEC23A with Q15637-4 reported by the HuRI binary yeast two-hybrid reference interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of SEC23A with MIA3/TANGO1 reported by the HuRI binary yeast two-hybrid reference interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of SEC23A with Q6ZMZ0 reported by the HuRI binary yeast two-hybrid reference interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of SEC23A with Q6ZS10 reported by the HuRI binary yeast two-hybrid reference interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of SEC23A with Q86UW9 reported by the HuRI binary yeast two-hybrid reference interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of SEC23A with Q969F0 reported by the HuRI binary yeast two-hybrid reference interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of SEC23A with Q96B21 reported by the HuRI binary yeast two-hybrid reference interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of SEC23A with Q9GZY8-5 reported by the HuRI binary yeast two-hybrid reference interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of SEC23A with Q9P2R7 reported by the HuRI binary yeast two-hybrid reference interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of SEC23A with Q9UPX6 reported by the HuRI binary yeast two-hybrid reference interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of SEC23A with Q9Y282 reported by the HuRI binary yeast two-hybrid reference interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of SEC23A with Q9Y2W2 reported by the HuRI binary yeast two-hybrid reference interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction of SEC23A with SEC23IP reported by the HuRI binary yeast two-hybrid reference interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Interaction of SEC23A with DCTN1 isoform reported by a neurodegenerative-disease interactome screen. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Interaction of SEC23A with SEC24D reported by proteome-scale affinity purification-mass spectrometry networks (BioPlex). Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Interaction of SEC23A with SEC24B reported by proteome-scale affinity purification-mass spectrometry networks (BioPlex). Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Interaction of SEC23A with SEC24C reported by proteome-scale affinity purification-mass spectrometry networks (BioPlex). Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Interaction of SEC23A with SEC23B reported by proteome-scale affinity purification-mass spectrometry networks (BioPlex). Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Interaction of SEC23A with SEC23IP reported by proteome-scale affinity purification-mass spectrometry networks (BioPlex). Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:34349020 Proteolytic processing of secretory pathway kinase Fam20C by... | REMOVE | Summary: Interaction of SEC23A with FAM20C reported by co-immunoprecipitation with FAM20C (abstract-only). Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:34504087 Sequences in the cytoplasmic tail of SARS-CoV-2 Spike facili... | REMOVE | Summary: Interaction of SEC23A with SARS-CoV-2 spike reported by interaction of the SARS-CoV-2 spike cytoplasmic tail with COPII. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Interaction of SEC23A with SEC24D reported by OpenCell endogenous-tagging interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Interaction of SEC23A with SEC24B reported by OpenCell endogenous-tagging interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Interaction of SEC23A with SEC24C reported by OpenCell endogenous-tagging interactome. Reason: Generic protein binding (GO:0005515) is uninformative under the project protein-binding policy. Removal does not dispute the reported interaction; the functionally relevant interactions of SEC23A (SEC24 heterodimerization, SAR1 GAP, SEC31 and TANGO1 PPP-motif recognition, cargo signals) are captured by COPII vesicle coat, GTPase activator activity, proline-rich region binding and cargo loading terms elsewhere in this review. |
| GO:0005783 endoplasmic reticulum | IDA GO_REF:0000052 | ACCEPT | Summary: Endoplasmic reticulum localization from the Human Protein Atlas immunofluorescence screen. Reason: Consistent with the transitional ER/ER exit site localisation of hSec23A by immuno-EM; a broad localisation-screen term that remains correct. Supporting Evidence: PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0005789 endoplasmic reticulum membrane | EXP PMID:8898360 Cloning and functional characterization of mammalian homolog... | ACCEPT | Summary: ER membrane localisation of hSec23A by immunoelectron microscopy (Paccaud et al. 1996). Reason: SEC23A is a peripheral membrane protein on the cytoplasmic face of the transitional ER membrane. Supporting Evidence: PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000120 | ACCEPT | Summary: ER membrane from UniProt subcellular-location mapping. Reason: Consistent with the experimental ER membrane localisation (PMID:8898360). Supporting Evidence: PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-203973 | ACCEPT | Summary: ER membrane location of SEC23A in a Reactome COPII reaction. Reason: Reactome places the SEC23:SEC24 inner coat on the cytoplasmic face of the ER membrane during COPII coat assembly, cargo capture and budding; consistent with immunoelectron microscopy of hSec23A at the transitional ER (PMID:8898360). Supporting Evidence: Reactome:R-HSA-5694522 SAR1:GTP recruits the cytoplasmic SEC23:SEC24 complex. PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-203979 | ACCEPT | Summary: ER membrane location of SEC23A in a Reactome COPII reaction. Reason: Reactome places the SEC23:SEC24 inner coat on the cytoplasmic face of the ER membrane during COPII coat assembly, cargo capture and budding; consistent with immunoelectron microscopy of hSec23A at the transitional ER (PMID:8898360). Supporting Evidence: Reactome:R-HSA-5694522 SAR1:GTP recruits the cytoplasmic SEC23:SEC24 complex. PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-204008 | ACCEPT | Summary: ER membrane location of SEC23A in a Reactome COPII reaction. Reason: Reactome places the SEC23:SEC24 inner coat on the cytoplasmic face of the ER membrane during COPII coat assembly, cargo capture and budding; consistent with immunoelectron microscopy of hSec23A at the transitional ER (PMID:8898360). Supporting Evidence: Reactome:R-HSA-5694522 SAR1:GTP recruits the cytoplasmic SEC23:SEC24 complex. PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-2130731 | ACCEPT | Summary: ER membrane location of SEC23A in a Reactome COPII reaction. Reason: Reactome places the SEC23:SEC24 inner coat on the cytoplasmic face of the ER membrane during COPII coat assembly, cargo capture and budding; consistent with immunoelectron microscopy of hSec23A at the transitional ER (PMID:8898360). Supporting Evidence: Reactome:R-HSA-5694522 SAR1:GTP recruits the cytoplasmic SEC23:SEC24 complex. PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-2213243 | ACCEPT | Summary: ER membrane location of SEC23A in a Reactome COPII reaction. Reason: Reactome places the SEC23:SEC24 inner coat on the cytoplasmic face of the ER membrane during COPII coat assembly, cargo capture and budding; consistent with immunoelectron microscopy of hSec23A at the transitional ER (PMID:8898360). Supporting Evidence: Reactome:R-HSA-5694522 SAR1:GTP recruits the cytoplasmic SEC23:SEC24 complex. PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-5694415 | ACCEPT | Summary: ER membrane location of SEC23A in a Reactome COPII reaction. Reason: Reactome places the SEC23:SEC24 inner coat on the cytoplasmic face of the ER membrane during COPII coat assembly, cargo capture and budding; consistent with immunoelectron microscopy of hSec23A at the transitional ER (PMID:8898360). Supporting Evidence: Reactome:R-HSA-5694522 SAR1:GTP recruits the cytoplasmic SEC23:SEC24 complex. PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-5694417 | ACCEPT | Summary: ER membrane location of SEC23A in a Reactome COPII reaction. Reason: Reactome places the SEC23:SEC24 inner coat on the cytoplasmic face of the ER membrane during COPII coat assembly, cargo capture and budding; consistent with immunoelectron microscopy of hSec23A at the transitional ER (PMID:8898360). Supporting Evidence: Reactome:R-HSA-5694522 SAR1:GTP recruits the cytoplasmic SEC23:SEC24 complex. PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-5694435 | ACCEPT | Summary: ER membrane location of SEC23A in a Reactome COPII reaction. Reason: Reactome places the SEC23:SEC24 inner coat on the cytoplasmic face of the ER membrane during COPII coat assembly, cargo capture and budding; consistent with immunoelectron microscopy of hSec23A at the transitional ER (PMID:8898360). Supporting Evidence: Reactome:R-HSA-5694522 SAR1:GTP recruits the cytoplasmic SEC23:SEC24 complex. PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-5694436 | ACCEPT | Summary: ER membrane location of SEC23A in a Reactome COPII reaction. Reason: Reactome places the SEC23:SEC24 inner coat on the cytoplasmic face of the ER membrane during COPII coat assembly, cargo capture and budding; consistent with immunoelectron microscopy of hSec23A at the transitional ER (PMID:8898360). Supporting Evidence: Reactome:R-HSA-5694522 SAR1:GTP recruits the cytoplasmic SEC23:SEC24 complex. PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-5694522 | ACCEPT | Summary: ER membrane location of SEC23A in a Reactome COPII reaction. Reason: Reactome places the SEC23:SEC24 inner coat on the cytoplasmic face of the ER membrane during COPII coat assembly, cargo capture and budding; consistent with immunoelectron microscopy of hSec23A at the transitional ER (PMID:8898360). Supporting Evidence: Reactome:R-HSA-5694522 SAR1:GTP recruits the cytoplasmic SEC23:SEC24 complex. PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-5694527 | ACCEPT | Summary: ER membrane location of SEC23A in a Reactome COPII reaction. Reason: Reactome places the SEC23:SEC24 inner coat on the cytoplasmic face of the ER membrane during COPII coat assembly, cargo capture and budding; consistent with immunoelectron microscopy of hSec23A at the transitional ER (PMID:8898360). Supporting Evidence: Reactome:R-HSA-5694522 SAR1:GTP recruits the cytoplasmic SEC23:SEC24 complex. PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-983424 | ACCEPT | Summary: ER membrane location of SEC23A in a Reactome COPII reaction. Reason: Reactome places the SEC23:SEC24 inner coat on the cytoplasmic face of the ER membrane during COPII coat assembly, cargo capture and budding; consistent with immunoelectron microscopy of hSec23A at the transitional ER (PMID:8898360). Supporting Evidence: Reactome:R-HSA-5694522 SAR1:GTP recruits the cytoplasmic SEC23:SEC24 complex. PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-983425 | ACCEPT | Summary: ER membrane location of SEC23A in a Reactome COPII reaction. Reason: Reactome places the SEC23:SEC24 inner coat on the cytoplasmic face of the ER membrane during COPII coat assembly, cargo capture and budding; consistent with immunoelectron microscopy of hSec23A at the transitional ER (PMID:8898360). Supporting Evidence: Reactome:R-HSA-5694522 SAR1:GTP recruits the cytoplasmic SEC23:SEC24 complex. PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-983426 | ACCEPT | Summary: ER membrane location of SEC23A in a Reactome COPII reaction. Reason: Reactome places the SEC23:SEC24 inner coat on the cytoplasmic face of the ER membrane during COPII coat assembly, cargo capture and budding; consistent with immunoelectron microscopy of hSec23A at the transitional ER (PMID:8898360). Supporting Evidence: Reactome:R-HSA-5694522 SAR1:GTP recruits the cytoplasmic SEC23:SEC24 complex. PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: Cytosol localisation from the Human Protein Atlas immunofluorescence screen. Reason: Consistent with the soluble cytosolic Sec23/24 pool (PMID:8898360). Supporting Evidence: PMID:8898360 Cytosolic hSec23Ap migrated with an apparent molecular weight of 350 kDa on a gel filtration column, suggesting that it is part of a protein complex. |
| GO:0005829 cytosol | IDA PMID:8898360 Cloning and functional characterization of mammalian homolog... | ACCEPT | Summary: Cytosolic pool of hSec23A shown by gel filtration of cytosol. Reason: SEC23A cycles between a soluble cytosolic Sec23/24 complex and the ER membrane; the cytosolic pool is experimentally shown. Supporting Evidence: PMID:8898360 Cytosolic hSec23Ap migrated with an apparent molecular weight of 350 kDa on a gel filtration column, suggesting that it is part of a protein complex. |
| GO:0005829 cytosol | IEA GO_REF:0000044 | ACCEPT | Summary: Cytosol from UniProt subcellular-location mapping. Reason: Consistent with the experimentally shown cytosolic pool (PMID:8898360). Supporting Evidence: PMID:8898360 Cytosolic hSec23Ap migrated with an apparent molecular weight of 350 kDa on a gel filtration column, suggesting that it is part of a protein complex. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-203973 | ACCEPT | Summary: Cytosolic location of SEC23A in a Reactome COPII reaction. Reason: Reactome represents the soluble cytosolic pool of SEC23:SEC24 that is recruited by SAR1-GTP, and released back to the cytosol after uncoating. Cytosolic hSec23A was shown directly by gel filtration (PMID:8898360). Supporting Evidence: PMID:8898360 Cytosolic hSec23Ap migrated with an apparent molecular weight of 350 kDa on a gel filtration column, suggesting that it is part of a protein complex. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-203979 | ACCEPT | Summary: Cytosolic location of SEC23A in a Reactome COPII reaction. Reason: Reactome represents the soluble cytosolic pool of SEC23:SEC24 that is recruited by SAR1-GTP, and released back to the cytosol after uncoating. Cytosolic hSec23A was shown directly by gel filtration (PMID:8898360). Supporting Evidence: PMID:8898360 Cytosolic hSec23Ap migrated with an apparent molecular weight of 350 kDa on a gel filtration column, suggesting that it is part of a protein complex. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-204008 | ACCEPT | Summary: Cytosolic location of SEC23A in a Reactome COPII reaction. Reason: Reactome represents the soluble cytosolic pool of SEC23:SEC24 that is recruited by SAR1-GTP, and released back to the cytosol after uncoating. Cytosolic hSec23A was shown directly by gel filtration (PMID:8898360). Supporting Evidence: PMID:8898360 Cytosolic hSec23Ap migrated with an apparent molecular weight of 350 kDa on a gel filtration column, suggesting that it is part of a protein complex. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5694409 | ACCEPT | Summary: Cytosolic location of SEC23A in a Reactome COPII reaction. Reason: Reactome represents the soluble cytosolic pool of SEC23:SEC24 that is recruited by SAR1-GTP, and released back to the cytosol after uncoating. Cytosolic hSec23A was shown directly by gel filtration (PMID:8898360). Supporting Evidence: PMID:8898360 Cytosolic hSec23Ap migrated with an apparent molecular weight of 350 kDa on a gel filtration column, suggesting that it is part of a protein complex. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5694413 | ACCEPT | Summary: Cytosolic location of SEC23A in a Reactome COPII reaction. Reason: Reactome represents the soluble cytosolic pool of SEC23:SEC24 that is recruited by SAR1-GTP, and released back to the cytosol after uncoating. Cytosolic hSec23A was shown directly by gel filtration (PMID:8898360). Supporting Evidence: PMID:8898360 Cytosolic hSec23Ap migrated with an apparent molecular weight of 350 kDa on a gel filtration column, suggesting that it is part of a protein complex. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5694415 | ACCEPT | Summary: Cytosolic location of SEC23A in a Reactome COPII reaction. Reason: Reactome represents the soluble cytosolic pool of SEC23:SEC24 that is recruited by SAR1-GTP, and released back to the cytosol after uncoating. Cytosolic hSec23A was shown directly by gel filtration (PMID:8898360). Supporting Evidence: PMID:8898360 Cytosolic hSec23Ap migrated with an apparent molecular weight of 350 kDa on a gel filtration column, suggesting that it is part of a protein complex. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5694417 | ACCEPT | Summary: Cytosolic location of SEC23A in a Reactome COPII reaction. Reason: Reactome represents the soluble cytosolic pool of SEC23:SEC24 that is recruited by SAR1-GTP, and released back to the cytosol after uncoating. Cytosolic hSec23A was shown directly by gel filtration (PMID:8898360). Supporting Evidence: PMID:8898360 Cytosolic hSec23Ap migrated with an apparent molecular weight of 350 kDa on a gel filtration column, suggesting that it is part of a protein complex. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5694418 | ACCEPT | Summary: Cytosolic location of SEC23A in a Reactome COPII reaction. Reason: Reactome represents the soluble cytosolic pool of SEC23:SEC24 that is recruited by SAR1-GTP, and released back to the cytosol after uncoating. Cytosolic hSec23A was shown directly by gel filtration (PMID:8898360). Supporting Evidence: PMID:8898360 Cytosolic hSec23Ap migrated with an apparent molecular weight of 350 kDa on a gel filtration column, suggesting that it is part of a protein complex. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5694435 | ACCEPT | Summary: Cytosolic location of SEC23A in a Reactome COPII reaction. Reason: Reactome represents the soluble cytosolic pool of SEC23:SEC24 that is recruited by SAR1-GTP, and released back to the cytosol after uncoating. Cytosolic hSec23A was shown directly by gel filtration (PMID:8898360). Supporting Evidence: PMID:8898360 Cytosolic hSec23Ap migrated with an apparent molecular weight of 350 kDa on a gel filtration column, suggesting that it is part of a protein complex. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5694439 | ACCEPT | Summary: Cytosolic location of SEC23A in a Reactome COPII reaction. Reason: Reactome represents the soluble cytosolic pool of SEC23:SEC24 that is recruited by SAR1-GTP, and released back to the cytosol after uncoating. Cytosolic hSec23A was shown directly by gel filtration (PMID:8898360). Supporting Evidence: PMID:8898360 Cytosolic hSec23Ap migrated with an apparent molecular weight of 350 kDa on a gel filtration column, suggesting that it is part of a protein complex. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5694441 | ACCEPT | Summary: Cytosolic location of SEC23A in a Reactome COPII reaction. Reason: Reactome represents the soluble cytosolic pool of SEC23:SEC24 that is recruited by SAR1-GTP, and released back to the cytosol after uncoating. Cytosolic hSec23A was shown directly by gel filtration (PMID:8898360). Supporting Evidence: PMID:8898360 Cytosolic hSec23Ap migrated with an apparent molecular weight of 350 kDa on a gel filtration column, suggesting that it is part of a protein complex. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5694446 | ACCEPT | Summary: Cytosolic location of SEC23A in a Reactome COPII reaction. Reason: Reactome represents the soluble cytosolic pool of SEC23:SEC24 that is recruited by SAR1-GTP, and released back to the cytosol after uncoating. Cytosolic hSec23A was shown directly by gel filtration (PMID:8898360). Supporting Evidence: PMID:8898360 Cytosolic hSec23Ap migrated with an apparent molecular weight of 350 kDa on a gel filtration column, suggesting that it is part of a protein complex. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5694522 | ACCEPT | Summary: Cytosolic location of SEC23A in a Reactome COPII reaction. Reason: Reactome represents the soluble cytosolic pool of SEC23:SEC24 that is recruited by SAR1-GTP, and released back to the cytosol after uncoating. Cytosolic hSec23A was shown directly by gel filtration (PMID:8898360). Supporting Evidence: PMID:8898360 Cytosolic hSec23Ap migrated with an apparent molecular weight of 350 kDa on a gel filtration column, suggesting that it is part of a protein complex. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5694527 | ACCEPT | Summary: Cytosolic location of SEC23A in a Reactome COPII reaction. Reason: Reactome represents the soluble cytosolic pool of SEC23:SEC24 that is recruited by SAR1-GTP, and released back to the cytosol after uncoating. Cytosolic hSec23A was shown directly by gel filtration (PMID:8898360). Supporting Evidence: PMID:8898360 Cytosolic hSec23Ap migrated with an apparent molecular weight of 350 kDa on a gel filtration column, suggesting that it is part of a protein complex. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-983422 | ACCEPT | Summary: Cytosolic location of SEC23A in a Reactome COPII reaction. Reason: Reactome represents the soluble cytosolic pool of SEC23:SEC24 that is recruited by SAR1-GTP, and released back to the cytosol after uncoating. Cytosolic hSec23A was shown directly by gel filtration (PMID:8898360). Supporting Evidence: PMID:8898360 Cytosolic hSec23Ap migrated with an apparent molecular weight of 350 kDa on a gel filtration column, suggesting that it is part of a protein complex. |
| GO:0006886 intracellular protein transport | IEA GO_REF:0000002 | ACCEPT | Summary: Intracellular protein transport from InterPro Sec23/24 domain mapping. Reason: Correct: SEC23A, as part of the COPII inner coat, mediates the export of protein cargo from the ER. A broad electronic term; the specific roles are captured by COPII-coated vesicle cargo loading and ER to Golgi vesicle-mediated transport. Supporting Evidence: PMID:8898360 hSec23Ap is a functional homologue of the yeast Sec23p as the hSec23A isoform complemented the temperature sensitivity of the Saccharomyces cerevisiae sec23-1 mutation at a restrictive temperature of 34 degrees C. PMID:16980979 Cell-free vesicle budding assays show that the F382L substitution results in loss of SEC23A function. |
| GO:0006888 endoplasmic reticulum to Golgi vesicle-mediated transport | IEA GO_REF:0000002 | ACCEPT | Summary: ER to Golgi vesicle-mediated transport from InterPro Sec23/24 domain mapping. Reason: Core process. hSec23A complements yeast sec23-1, and the CLSD F382L mutation abolishes SEC23A function in cell-free budding and causes ER dilatation with retained cargo in patient fibroblasts. Supporting Evidence: PMID:8898360 hSec23Ap is a functional homologue of the yeast Sec23p as the hSec23A isoform complemented the temperature sensitivity of the Saccharomyces cerevisiae sec23-1 mutation at a restrictive temperature of 34 degrees C. PMID:16980979 Cell-free vesicle budding assays show that the F382L substitution results in loss of SEC23A function. |
| GO:0008270 zinc ion binding | IDA PMID:18843296 Structural basis of cargo membrane protein discrimination by... | KEEP AS NON CORE | Summary: Zinc bound in the Sec23/Sec24-type zinc finger seen in crystal structures of human Sec23a complexes. Reason: Structural zinc coordinated by four cysteines (C61, C66, C85, C88 in UniProt structure-derived features) in the zinc-finger domain; real but a structural cofactor rather than the functional activity of the protein. Supporting Evidence: file:human/SEC23A/SEC23A-uniprot.txt /ligand="Zn(2+)" |
| GO:0008270 zinc ion binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: Zinc ion binding from InterPro Sec23/Sec24 zinc-finger domain mapping. Reason: Consistent with the structure-derived zinc-binding residues; structural, non-core. Supporting Evidence: file:human/SEC23A/SEC23A-uniprot.txt /ligand="Zn(2+)" |
| GO:0012507 ER to Golgi transport vesicle membrane | IEA GO_REF:0000044 | ACCEPT | Summary: ER to Golgi transport vesicle membrane from UniProt subcellular-location mapping. Reason: Consistent with immuno-EM (PMID:8898360). Supporting Evidence: PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0012507 ER to Golgi transport vesicle membrane | IGI PMID:8898360 Cloning and functional characterization of mammalian homolog... | ACCEPT | Summary: Location on ER-derived COPII vesicles supported by immuno-EM and functional complementation of yeast sec23-1 (Paccaud et al. 1996). Reason: hSec23A is found on vesicles associated with the transitional ER and functionally replaces yeast Sec23p, a COPII vesicle coat subunit. Supporting Evidence: PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. PMID:8898360 hSec23Ap is a functional homologue of the yeast Sec23p as the hSec23A isoform complemented the temperature sensitivity of the Saccharomyces cerevisiae sec23-1 mutation at a restrictive temperature of 34 degrees C. |
| GO:0012507 ER to Golgi transport vesicle membrane | TAS Reactome:R-HSA-203973 | ACCEPT | Summary: SEC23A on COPII vesicle membrane in a Reactome reaction. Reason: Reactome places SEC23A on the membrane of budded COPII ER-to-Golgi transport vesicles before uncoating; consistent with immuno-EM of hSec23A on vesicles associated with transitional ER (PMID:8898360). Supporting Evidence: PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0012507 ER to Golgi transport vesicle membrane | TAS Reactome:R-HSA-5694409 | ACCEPT | Summary: SEC23A on COPII vesicle membrane in a Reactome reaction. Reason: Reactome places SEC23A on the membrane of budded COPII ER-to-Golgi transport vesicles before uncoating; consistent with immuno-EM of hSec23A on vesicles associated with transitional ER (PMID:8898360). Supporting Evidence: PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0012507 ER to Golgi transport vesicle membrane | TAS Reactome:R-HSA-5694418 | ACCEPT | Summary: SEC23A on COPII vesicle membrane in a Reactome reaction. Reason: Reactome places SEC23A on the membrane of budded COPII ER-to-Golgi transport vesicles before uncoating; consistent with immuno-EM of hSec23A on vesicles associated with transitional ER (PMID:8898360). Supporting Evidence: PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0012507 ER to Golgi transport vesicle membrane | TAS Reactome:R-HSA-5694439 | ACCEPT | Summary: SEC23A on COPII vesicle membrane in a Reactome reaction. Reason: Reactome places SEC23A on the membrane of budded COPII ER-to-Golgi transport vesicles before uncoating; consistent with immuno-EM of hSec23A on vesicles associated with transitional ER (PMID:8898360). Supporting Evidence: PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0012507 ER to Golgi transport vesicle membrane | TAS Reactome:R-HSA-5694441 | ACCEPT | Summary: SEC23A on COPII vesicle membrane in a Reactome reaction. Reason: Reactome places SEC23A on the membrane of budded COPII ER-to-Golgi transport vesicles before uncoating; consistent with immuno-EM of hSec23A on vesicles associated with transitional ER (PMID:8898360). Supporting Evidence: PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0012507 ER to Golgi transport vesicle membrane | TAS Reactome:R-HSA-5694446 | ACCEPT | Summary: SEC23A on COPII vesicle membrane in a Reactome reaction. Reason: Reactome places SEC23A on the membrane of budded COPII ER-to-Golgi transport vesicles before uncoating; consistent with immuno-EM of hSec23A on vesicles associated with transitional ER (PMID:8898360). Supporting Evidence: PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0012507 ER to Golgi transport vesicle membrane | TAS Reactome:R-HSA-983422 | ACCEPT | Summary: SEC23A on COPII vesicle membrane in a Reactome reaction. Reason: Reactome places SEC23A on the membrane of budded COPII ER-to-Golgi transport vesicles before uncoating; consistent with immuno-EM of hSec23A on vesicles associated with transitional ER (PMID:8898360). Supporting Evidence: PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0012507 ER to Golgi transport vesicle membrane | TAS Reactome:R-HSA-983424 | ACCEPT | Summary: SEC23A on COPII vesicle membrane in a Reactome reaction. Reason: Reactome places SEC23A on the membrane of budded COPII ER-to-Golgi transport vesicles before uncoating; consistent with immuno-EM of hSec23A on vesicles associated with transitional ER (PMID:8898360). Supporting Evidence: PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0030127 COPII vesicle coat | IBA GO_REF:0000033 | ACCEPT | Summary: COPII vesicle coat propagated by PAINT from node PTN000124617; human SEC23A is itself one of the experimental donors. Reason: SEC23 coat membership is ancestral to the SEC23 family; human SEC23A in PTHR11141:SF7 lies inside the inheriting clade and has its own experimental support (PMID:17499046, PMID:8898360). Supporting Evidence: PMID:8898360 hSec23Ap is a functional homologue of the yeast Sec23p as the hSec23A isoform complemented the temperature sensitivity of the Saccharomyces cerevisiae sec23-1 mutation at a restrictive temperature of 34 degrees C. PMID:17499046 The 200 kDa crystal structure of Sec22 bound to Sec23/24 reveals that the transport signal is a folded epitope rather than a conventional short peptide sequence. |
| GO:0030127 COPII vesicle coat | IDA PMID:17499046 The transport signal on Sec22 for packaging into COPII-coate... | ACCEPT | Summary: Human Sec23a/Sec24 inner-coat complex characterised structurally with SEC22B cargo (Mancias & Goldberg 2007). Reason: SEC23A is a core structural subunit of the COPII coat (inner coat with SEC24, recruited by SAR1, binds SEC13-SEC31 outer coat). Supporting Evidence: PMID:17499046 The 200 kDa crystal structure of Sec22 bound to Sec23/24 reveals that the transport signal is a folded epitope rather than a conventional short peptide sequence. PMID:17981132 In vitro assays reveal that the mutant form of SEC23A poorly recruits the Sec13-Sec31 complex, inhibiting vesicle formation. |
| GO:0030127 COPII vesicle coat | IEA GO_REF:0000002 | ACCEPT | Summary: COPII vesicle coat from InterPro Sec23/24 domain mapping. Reason: Consistent with experimental and phylogenetic evidence. Supporting Evidence: PMID:8898360 hSec23Ap is a functional homologue of the yeast Sec23p as the hSec23A isoform complemented the temperature sensitivity of the Saccharomyces cerevisiae sec23-1 mutation at a restrictive temperature of 34 degrees C. |
| GO:0030134 COPII-coated ER to Golgi transport vesicle | IEA GO_REF:0000107 | ACCEPT | Summary: COPII-coated ER to Golgi transport vesicle, transferred from mouse Sec23a. Reason: SEC23A is a coat subunit of these vesicles; supported directly in human by immuno-EM (PMID:8898360). Supporting Evidence: PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0032456 endocytic recycling | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Endocytic recycling, transferred by orthology from mouse Sec23a (GLUT4 trafficking in adipocytes). Reason: UniProt records a requirement for SEC23A in insulin-induced GLUT4 translocation only "By similarity" from mouse. COPII acts at ER exit; a requirement for GLUT4 delivery is most parsimoniously an upstream/indirect consequence of ER export or ERES-derived membrane supply, i.e. necessity rather than participation in endocytic recycling. No human data support it. Supporting Evidence: file:human/SEC23A/SEC23A-uniprot.txt Required for the translocation of insulin-induced glucose transporter |
| GO:0048471 perinuclear region of cytoplasm | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Perinuclear region of cytoplasm, transferred from mouse Sec23a. Reason: ER exit sites and ERGIC cluster in the juxtanuclear region, so COPII components can appear perinuclear; true but a low-resolution description of the ER exit site location. Supporting Evidence: PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0070971 endoplasmic reticulum exit site | IBA GO_REF:0000033 | ACCEPT | Summary: ER exit site propagated by PAINT from node PTN000124617; human SEC23A is one of the experimental donors. Reason: Ancestral location of the SEC23 family; human SEC23A has direct experimental support. Supporting Evidence: PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. file:human/SEC23A/SEC23A-uniprot.txt Note=Enriched at endoplasmic reticulum |
| GO:0070971 endoplasmic reticulum exit site | IDA PMID:28442536 TANGO1 recruits Sec16 to coordinately organize ER exit sites... | ACCEPT | Summary: SEC23A at ER exit sites, colocalising with TANGO1 and SEC16 (Maeda et al. 2017). Reason: Core location; ER exit site organisation by TANGO1/SEC16 recruits SEC23. Supporting Evidence: PMID:28442536 Because TANGO1’s PRD has also been reported to interact with Sec23 (Saito et al., 2009; Ma and Goldberg, 2016), we next tested the interaction with Sec23 (Fig. S3). |
| GO:0070971 endoplasmic reticulum exit site | IDA PMID:8898360 Cloning and functional characterization of mammalian homolog... | ACCEPT | Summary: hSec23A at the ribosome-free transitional ER by immuno-EM. Reason: Transitional ER is the ER exit site; core location. Supporting Evidence: PMID:8898360 By immunoelectron microscopy, hSec23Ap was found essentially in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. |
| GO:0090110 COPII-coated vesicle cargo loading | IBA GO_REF:0000033 | ACCEPT | Summary: COPII-coated vesicle cargo loading propagated by PAINT from PTN000124617 (donors yeast Sec23 and human SEC23A). Reason: Ancestral and experimentally supported in human SEC23A. Supporting Evidence: PMID:17499046 The SNARE protein Sec22 contains a signal that binds the COPII subcomplex Sec23/24 and specifies its endoplasmic reticulum (ER) exit as an unassembled SNARE. PMID:8898360 hSec23Ap is a functional homologue of the yeast Sec23p as the hSec23A isoform complemented the temperature sensitivity of the Saccharomyces cerevisiae sec23-1 mutation at a restrictive temperature of 34 degrees C. |
| GO:0090110 COPII-coated vesicle cargo loading | IDA PMID:17499046 The transport signal on Sec22 for packaging into COPII-coate... | ACCEPT | Summary: Sec23/24 recognises a folded transport signal on SEC22B for packaging into COPII vesicles. Reason: Direct structural evidence that the Sec23/24 interface captures cargo. Supporting Evidence: PMID:17499046 The SNARE protein Sec22 contains a signal that binds the COPII subcomplex Sec23/24 and specifies its endoplasmic reticulum (ER) exit as an unassembled SNARE. PMID:17499046 The 200 kDa crystal structure of Sec22 bound to Sec23/24 reveals that the transport signal is a folded epitope rather than a conventional short peptide sequence. |
| GO:0090110 COPII-coated vesicle cargo loading | IDA PMID:18843296 Structural basis of cargo membrane protein discrimination by... | ACCEPT | Summary: Cargo packaging assays with human Sec23/Sec24 isoform complexes. Reason: Human Sec23A/Sec24 complexes package cargo into COPII vesicles in vitro; SEC24 provides most cargo-binding sites, SEC23A is the obligate partner. Supporting Evidence: PMID:18843296 we combined X-ray crystallographic and biochemical analysis with functional assays of cargo packaging into COPII vesicles to establish molecular mechanisms for cargo discrimination by human Sec24 subunits. |
| GO:0090110 COPII-coated vesicle cargo loading | IGI PMID:8898360 Cloning and functional characterization of mammalian homolog... | ACCEPT | Summary: hSec23A complements yeast sec23-1 (Paccaud et al. 1996). Reason: Functional complementation shows hSec23A performs the Sec23p role in COPII vesicle formation and cargo export. Supporting Evidence: PMID:8898360 hSec23Ap is a functional homologue of the yeast Sec23p as the hSec23A isoform complemented the temperature sensitivity of the Saccharomyces cerevisiae sec23-1 mutation at a restrictive temperature of 34 degrees C. |
| GO:0090114 COPII-coated vesicle budding | IEA GO_REF:0000002 | ACCEPT | Summary: COPII-coated vesicle budding from InterPro Sec23 C-terminal domain mapping. Reason: Human SEC23A is required in cell-free budding: the CLSD F382L mutant poorly recruits SEC13-SEC31 and fails to form vesicles. SEC23A contributes structure (inner coat, outer-coat recruitment via PPP-motif binding) to budding. Supporting Evidence: PMID:16980979 Cell-free vesicle budding assays show that the F382L substitution results in loss of SEC23A function. PMID:17981132 In vitro assays reveal that the mutant form of SEC23A poorly recruits the Sec13-Sec31 complex, inhibiting vesicle formation. |
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Download this section (compressed HTML)Q: Has SAR1 GAP stimulation been measured directly for human SEC23A (versus SEC23B) with SAR1A and SAR1B, and do the paralogs differ in GAP potency, given that the human GAP annotation currently rests on PAINT transfer from yeast Sec23?
Q: Which cargo-recognition events attributed to Sec23/24 (SEC22B, MHC-I C-terminal signal) depend on residues of SEC23A rather than SEC24 at the heterodimer interface?
Experiment: Reconstituted SAR1 GTP hydrolysis assays (tryptophan fluorescence or radiolabelled GTP) comparing purified SEC23A-SEC24 and SEC23B-SEC24 with SAR1A and SAR1B, including the CLSD F382L variant and an arginine-finger mutant.
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