GYPA encodes glycophorin A, the major sialoglycoprotein of the human erythrocyte membrane. It is a single-pass type I membrane protein whose heavily O- and N-glycosylated extracellular N-terminal segment is exposed on the red-cell surface and carries the MN blood group antigens. Through its transmembrane helix (GXXXG motif) it forms homodimers and binds the band 3 anion exchanger (SLC4A1); a GYPA monomer sits at each end of the SLC4A1 dimer. GYPA is an integral component of the erythrocyte ankyrin-1 complex, contributing to red-cell membrane stability and shape and supporting SLC4A1 activity. Its surface glycans are exploited as entry receptors by pathogens including Plasmodium falciparum (via EBA-175) and Hepatitis A virus.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005515 protein binding | IPI PMID:19438409 Interaction of anion exchanger 1 and glycophorin A in human ... | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:23219802 Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aqu... | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:24297912 RH5-Basigin interaction plays a major role in the host tropi... | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:24297912 RH5-Basigin interaction plays a major role in the host tropi... | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:24297912 RH5-Basigin interaction plays a major role in the host tropi... | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:25910212 Widespread macromolecular interaction perturbations in human... | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:25910212 Widespread macromolecular interaction perturbations in human... | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:25910212 Widespread macromolecular interaction perturbations in human... | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Generic protein binding, including large interactome-screen hits and the functionally important SLC4A1/band 3 interaction. Reason: Bare protein binding is uninformative and is removed under the protein-binding policy. The biologically meaningful interactions (the band 3/SLC4A1 association and ankyrin-1 complex membership) are captured by the specific ankyrin-1 complex annotation and by identical protein binding (homodimer); removal does not dispute that the interactions occur. Supporting Evidence: PMID:35835865 a GPA monomer is bound at each end of the band 3 dimer |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Glycophorin A is a cell-surface transmembrane protein of the erythrocyte plasma membrane, extracellular glycosylated domain exposed. Reason: GYPA is the major intrinsic membrane protein of the red cell; its N-terminal glycosylated segment lies outside the membrane and it localizes to the cell surface. Supporting Evidence: PMID:19438409 GPA was localized at the cell file:human/GYPA/GYPA-uniprot.txt The N-terminal glycosylated segment, which |
| GO:0005886 plasma membrane | IDA GO_REF:0000052 | ACCEPT | Summary: Glycophorin A is a cell-surface transmembrane protein of the erythrocyte plasma membrane, extracellular glycosylated domain exposed. Reason: GYPA is the major intrinsic membrane protein of the red cell; its N-terminal glycosylated segment lies outside the membrane and it localizes to the cell surface. Supporting Evidence: PMID:19438409 GPA was localized at the cell file:human/GYPA/GYPA-uniprot.txt The N-terminal glycosylated segment, which |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: Glycophorin A is a cell-surface transmembrane protein of the erythrocyte plasma membrane, extracellular glycosylated domain exposed. Reason: GYPA is the major intrinsic membrane protein of the red cell; its N-terminal glycosylated segment lies outside the membrane and it localizes to the cell surface. Supporting Evidence: PMID:19438409 GPA was localized at the cell file:human/GYPA/GYPA-uniprot.txt The N-terminal glycosylated segment, which |
| GO:0005886 plasma membrane | TAS PMID:8245024 Alteration of splice site selection by an exon mutation in t... | ACCEPT | Summary: Glycophorin A is a cell-surface transmembrane protein of the erythrocyte plasma membrane, extracellular glycosylated domain exposed. Reason: GYPA is the major intrinsic membrane protein of the red cell; its N-terminal glycosylated segment lies outside the membrane and it localizes to the cell surface. Supporting Evidence: PMID:19438409 GPA was localized at the cell file:human/GYPA/GYPA-uniprot.txt The N-terminal glycosylated segment, which |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8867098 | ACCEPT | Summary: Glycophorin A is a cell-surface transmembrane protein of the erythrocyte plasma membrane, extracellular glycosylated domain exposed. Reason: GYPA is the major intrinsic membrane protein of the red cell; its N-terminal glycosylated segment lies outside the membrane and it localizes to the cell surface. Supporting Evidence: PMID:19438409 GPA was localized at the cell file:human/GYPA/GYPA-uniprot.txt The N-terminal glycosylated segment, which |
| GO:0016020 membrane | IEA GO_REF:0000002 | TOO GENERAL | Summary: Membrane is the generic parent of the asserted plasma membrane localization. Reason: GYPA is specifically a plasma (erythrocyte) membrane protein, a term already asserted; the bare membrane term is entailed by it and adds no information. Supporting Evidence: file:human/GYPA/GYPA-uniprot.txt Glycophorin A is the major intrinsic membrane |
| GO:0016020 membrane | TAS PMID:3456608 Isolation and characterization of human glycophorin A cDNA c... | TOO GENERAL | Summary: Membrane is the generic parent of the asserted plasma membrane localization. Reason: GYPA is specifically a plasma (erythrocyte) membrane protein, a term already asserted; the bare membrane term is entailed by it and adds no information. Supporting Evidence: file:human/GYPA/GYPA-uniprot.txt Glycophorin A is the major intrinsic membrane |
| GO:0042802 identical protein binding | IPI PMID:14681217 Involvement of transmembrane domain interactions in signal t... | ACCEPT | Summary: Glycophorin A forms homodimers via its transmembrane GXXXG motif. Reason: GYPA homodimerization is well established (the glycophorin A TM helix is the textbook model of a dimerizing transmembrane helix) and is confirmed structurally in the ankyrin-1 complex work. Supporting Evidence: PMID:35835865 the single transmembrane proteins glycophorin A (GPA) and glycophorin B (GPB) PMID:23155421 GpA is the glycophorin A transmembrane domain previously studied and known to have strong homotypic interactions |
| GO:0042802 identical protein binding | IPI PMID:15067009 Dimerization of the transmembrane domain of Integrin alphaII... | ACCEPT | Summary: Glycophorin A forms homodimers via its transmembrane GXXXG motif. Reason: GYPA homodimerization is well established (the glycophorin A TM helix is the textbook model of a dimerizing transmembrane helix) and is confirmed structurally in the ankyrin-1 complex work. Supporting Evidence: PMID:35835865 the single transmembrane proteins glycophorin A (GPA) and glycophorin B (GPB) PMID:23155421 GpA is the glycophorin A transmembrane domain previously studied and known to have strong homotypic interactions |
| GO:0042802 identical protein binding | IPI PMID:23155421 Isolated Toll-like receptor transmembrane domains are capabl... | ACCEPT | Summary: Glycophorin A forms homodimers via its transmembrane GXXXG motif. Reason: GYPA homodimerization is well established (the glycophorin A TM helix is the textbook model of a dimerizing transmembrane helix) and is confirmed structurally in the ankyrin-1 complex work. Supporting Evidence: PMID:35835865 the single transmembrane proteins glycophorin A (GPA) and glycophorin B (GPB) PMID:23155421 GpA is the glycophorin A transmembrane domain previously studied and known to have strong homotypic interactions |
| GO:0170014 ankyrin-1 complex | IDA PMID:35835865 Architecture of the human erythrocyte ankyrin-1 complex. | ACCEPT | Summary: Glycophorin A is a subunit of the erythrocyte ankyrin-1 complex. Reason: Cryo-EM of the native complex purified from human erythrocytes resolves GYPA as a component together with ANK1, SLC4A1, RHAG, RHCE, EPB42, GYPB and AQP1. Supporting Evidence: PMID:35835865 the single transmembrane proteins glycophorin A (GPA) and glycophorin B (GPB) |
| GO:0170014 ankyrin-1 complex | IEA GO_REF:0000117 | ACCEPT | Summary: Glycophorin A is a subunit of the erythrocyte ankyrin-1 complex. Reason: Cryo-EM of the native complex purified from human erythrocytes resolves GYPA as a component together with ANK1, SLC4A1, RHAG, RHCE, EPB42, GYPB and AQP1. Supporting Evidence: PMID:35835865 the single transmembrane proteins glycophorin A (GPA) and glycophorin B (GPB) |
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Download this section (compressed HTML)Q: Does glycophorin A act as an obligatory folding/trafficking chaperone for band 3 in developing erythrocytes, given that steady-state GPA knockdown does not reduce surface AE1?
Q: How do the MN blood group glycan variants alter susceptibility to P. falciparum EBA-175-mediated invasion?
Experiment: Reconstitute GYPA and SLC4A1 in defined lipid nanodiscs and measure anion-exchange kinetics with and without GYPA to quantify its contribution to transporter activity.
Type: biochemistry
Experiment: Erythroid differentiation of GYPA-knockout iPSCs with surface proteomics to test the chaperone/escort role for band 3 and other ankyrin-1 complex members.
Type: cell biology
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