ATP5PF encodes coupling factor 6 (F6) of mitochondrial F1F0 ATP synthase (complex V), a small, nuclear-encoded, mitochondrially imported subunit of the peripheral stalk. Together with subunits b, d and OSCP, the stalk acts as a stator that holds the catalytic alpha3beta3 head and subunit a static against the rotating central stalk and c-ring. It is required for functional coupling of the catalytic F(1) and proton-translocating F(o) sectors during oxidative ATP synthesis.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005515 protein binding | IPI PMID:27499296 Mitochondrial Protein Interaction Mapping Identifies Regulat... | REMOVE | Summary: Protein binding (IPI) with ATP5F1A, from a mitochondrial protein-interaction mapping study. ATP5F1A is a fellow complex V subunit, so this co-purification reflects complex membership, which GO:0045259 already captures. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma... | REMOVE | Summary: Protein binding (IPI) with ATP5PD, from a crosslinking mass-spectrometry study. ATP5PD is a fellow complex V subunit, so this co-purification reflects complex membership, which GO:0045259 already captures. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma... | REMOVE | Summary: Protein binding (IPI) with ATP5F1A, from a crosslinking mass-spectrometry study. ATP5F1A is a fellow complex V subunit, so this co-purification reflects complex membership, which GO:0045259 already captures. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Protein binding (IPI) with MOSPD3, from the HuRI binary Y2H map. MOSPD3 has no established functional link to F6. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Protein binding (IPI) with KCNK5, from the HuRI binary Y2H map. KCNK5 has no established functional link to F6. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Protein binding (IPI) with SFT2D2, from the HuRI binary Y2H map. SFT2D2 has no established functional link to F6. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Protein binding (IPI) with ABHD16A, from the HuRI binary Y2H map. ABHD16A has no established functional link to F6. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Protein binding (IPI) with PTPN9, from the HuRI binary Y2H map. PTPN9 has no established functional link to F6. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Protein binding (IPI) with PLP2, from the HuRI binary Y2H map. PLP2 has no established functional link to F6. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Protein binding (IPI) with MALL, from the HuRI binary Y2H map. MALL has no established functional link to F6. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Protein binding (IPI) with PHOSPHO2, from the HuRI binary Y2H map. PHOSPHO2 has no established functional link to F6. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Protein binding (IPI) with BCL2L2, from the HuRI binary Y2H map. BCL2L2 has no established functional link to F6. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Protein binding (IPI) with MIEF2, from the HuRI binary Y2H map. MIEF2 has no established functional link to F6. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Protein binding (IPI) with REEP6, from the HuRI binary Y2H map. REEP6 has no established functional link to F6. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Protein binding (IPI) with SIGLEC12, from the HuRI binary Y2H map. SIGLEC12 has no established functional link to F6. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Protein binding (IPI) with INPP5K, from the HuRI binary Y2H map. INPP5K has no established functional link to F6. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Protein binding (IPI) with MIEF1, from the HuRI binary Y2H map. MIEF1 has no established functional link to F6. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Protein binding (IPI) with NDRG4, from the HuRI binary Y2H map. NDRG4 has no established functional link to F6. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Protein binding (IPI) with ATP5PD, from the BioPlex dual proteome-scale network. ATP5PD is a fellow complex V subunit, so this co-purification reflects complex membership, which GO:0045259 already captures. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Protein binding (IPI) with ATP5F1A, from the BioPlex dual proteome-scale network. ATP5F1A is a fellow complex V subunit, so this co-purification reflects complex membership, which GO:0045259 already captures. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Protein binding (IPI) with ATP5PD, from a multimodal cell map. ATP5PD is a fellow complex V subunit, so this co-purification reflects complex membership, which GO:0045259 already captures. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Protein binding (IPI) with ATP5F1A, from a multimodal cell map. ATP5F1A is a fellow complex V subunit, so this co-purification reflects complex membership, which GO:0045259 already captures. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005739 mitochondrion | HDA PMID:20833797 Phosphoproteome analysis of functional mitochondria isolated... | ACCEPT | Summary: Mitochondrion (HDA). F6 is a mitochondrial complex V subunit attached to the inner-membrane F(o) domain. Accepted. Reason: [file:human/ATP5PF/ATP5PF-uniprot.txt "CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase"] [file:human/ATP5PF/ATP5PF-uniprot.txt "CC peripheric stalk, which acts as a stator to hold the catalytic"] Supporting Evidence: file:human/ATP5PF/ATP5PF-uniprot.txt CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase file:human/ATP5PF/ATP5PF-uniprot.txt CC peripheric stalk, which acts as a stator to hold the catalytic |
| GO:0005739 mitochondrion | HTP PMID:34800366 Quantitative high-confidence human mitochondrial proteome an... | ACCEPT | Summary: Mitochondrion (HTP). F6 is a mitochondrial complex V subunit attached to the inner-membrane F(o) domain. Accepted. Reason: [file:human/ATP5PF/ATP5PF-uniprot.txt "CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase"] [file:human/ATP5PF/ATP5PF-uniprot.txt "CC peripheric stalk, which acts as a stator to hold the catalytic"] Supporting Evidence: file:human/ATP5PF/ATP5PF-uniprot.txt CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase file:human/ATP5PF/ATP5PF-uniprot.txt CC peripheric stalk, which acts as a stator to hold the catalytic |
| GO:0005739 mitochondrion | IC PMID:12110673 A functionally active human F1F0 ATPase can be purified by i... | ACCEPT | Summary: Mitochondrion (IC). F6 is a mitochondrial complex V subunit attached to the inner-membrane F(o) domain. Accepted. Reason: [file:human/ATP5PF/ATP5PF-uniprot.txt "CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase"] [file:human/ATP5PF/ATP5PF-uniprot.txt "CC peripheric stalk, which acts as a stator to hold the catalytic"] Supporting Evidence: file:human/ATP5PF/ATP5PF-uniprot.txt CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase file:human/ATP5PF/ATP5PF-uniprot.txt CC peripheric stalk, which acts as a stator to hold the catalytic |
| GO:0005739 mitochondrion | IDA GO_REF:0000052 | ACCEPT | Summary: Mitochondrion (IDA). F6 is a mitochondrial complex V subunit attached to the inner-membrane F(o) domain. Accepted. Reason: [file:human/ATP5PF/ATP5PF-uniprot.txt "CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase"] [file:human/ATP5PF/ATP5PF-uniprot.txt "CC peripheric stalk, which acts as a stator to hold the catalytic"] Supporting Evidence: file:human/ATP5PF/ATP5PF-uniprot.txt CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase file:human/ATP5PF/ATP5PF-uniprot.txt CC peripheric stalk, which acts as a stator to hold the catalytic |
| GO:0005739 mitochondrion | IEA GO_REF:0000044 | ACCEPT | Summary: Mitochondrion (IEA). F6 is a mitochondrial complex V subunit attached to the inner-membrane F(o) domain. Accepted. Reason: [file:human/ATP5PF/ATP5PF-uniprot.txt "CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase"] [file:human/ATP5PF/ATP5PF-uniprot.txt "CC peripheric stalk, which acts as a stator to hold the catalytic"] Supporting Evidence: file:human/ATP5PF/ATP5PF-uniprot.txt CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase file:human/ATP5PF/ATP5PF-uniprot.txt CC peripheric stalk, which acts as a stator to hold the catalytic |
| GO:0005739 mitochondrion | TAS PMID:1825642 Human mitochondrial ATP synthase: cloning cDNA for the nucle... | ACCEPT | Summary: Mitochondrion (TAS). F6 is a mitochondrial complex V subunit attached to the inner-membrane F(o) domain. Accepted. Reason: [file:human/ATP5PF/ATP5PF-uniprot.txt "CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase"] [file:human/ATP5PF/ATP5PF-uniprot.txt "CC peripheric stalk, which acts as a stator to hold the catalytic"] Supporting Evidence: file:human/ATP5PF/ATP5PF-uniprot.txt CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase file:human/ATP5PF/ATP5PF-uniprot.txt CC peripheric stalk, which acts as a stator to hold the catalytic |
| GO:0005743 mitochondrial inner membrane | IEA GO_REF:0000044 | ACCEPT | Summary: Mitochondrial inner membrane (IEA). F6 is a mitochondrial complex V subunit attached to the inner-membrane F(o) domain. Accepted. Reason: [file:human/ATP5PF/ATP5PF-uniprot.txt "CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase"] [file:human/ATP5PF/ATP5PF-uniprot.txt "CC peripheric stalk, which acts as a stator to hold the catalytic"] Supporting Evidence: file:human/ATP5PF/ATP5PF-uniprot.txt CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase file:human/ATP5PF/ATP5PF-uniprot.txt CC peripheric stalk, which acts as a stator to hold the catalytic |
| GO:0005743 mitochondrial inner membrane | NAS PMID:26297831 Assembly of human mitochondrial ATP synthase through two sep... | ACCEPT | Summary: Mitochondrial inner membrane (NAS). F6 is a mitochondrial complex V subunit attached to the inner-membrane F(o) domain. Accepted. Reason: [file:human/ATP5PF/ATP5PF-uniprot.txt "CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase"] [file:human/ATP5PF/ATP5PF-uniprot.txt "CC peripheric stalk, which acts as a stator to hold the catalytic"] Supporting Evidence: file:human/ATP5PF/ATP5PF-uniprot.txt CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase file:human/ATP5PF/ATP5PF-uniprot.txt CC peripheric stalk, which acts as a stator to hold the catalytic |
| GO:0005743 mitochondrial inner membrane | TAS Reactome:R-HSA-164832 | ACCEPT | Summary: Mitochondrial inner membrane (TAS). F6 is a mitochondrial complex V subunit attached to the inner-membrane F(o) domain. The Reactome event is 'ATPase synthesizes ATP'. Accepted. Reason: [file:human/ATP5PF/ATP5PF-uniprot.txt "CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase"] [file:human/ATP5PF/ATP5PF-uniprot.txt "CC peripheric stalk, which acts as a stator to hold the catalytic"] Supporting Evidence: file:human/ATP5PF/ATP5PF-uniprot.txt CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase file:human/ATP5PF/ATP5PF-uniprot.txt CC peripheric stalk, which acts as a stator to hold the catalytic |
| GO:0005743 mitochondrial inner membrane | TAS Reactome:R-HSA-164834 | ACCEPT | Summary: Mitochondrial inner membrane (TAS). F6 is a mitochondrial complex V subunit attached to the inner-membrane F(o) domain. The Reactome event is 'Enzyme-bound ATP is released'. Accepted. Reason: [file:human/ATP5PF/ATP5PF-uniprot.txt "CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase"] [file:human/ATP5PF/ATP5PF-uniprot.txt "CC peripheric stalk, which acts as a stator to hold the catalytic"] Supporting Evidence: file:human/ATP5PF/ATP5PF-uniprot.txt CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase file:human/ATP5PF/ATP5PF-uniprot.txt CC peripheric stalk, which acts as a stator to hold the catalytic |
| GO:0005743 mitochondrial inner membrane | TAS Reactome:R-HSA-164840 | ACCEPT | Summary: Mitochondrial inner membrane (TAS). F6 is a mitochondrial complex V subunit attached to the inner-membrane F(o) domain. The Reactome event is 'ADP and Pi bind to ATPase'. Accepted. Reason: [file:human/ATP5PF/ATP5PF-uniprot.txt "CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase"] [file:human/ATP5PF/ATP5PF-uniprot.txt "CC peripheric stalk, which acts as a stator to hold the catalytic"] Supporting Evidence: file:human/ATP5PF/ATP5PF-uniprot.txt CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase file:human/ATP5PF/ATP5PF-uniprot.txt CC peripheric stalk, which acts as a stator to hold the catalytic |
| GO:0005743 mitochondrial inner membrane | TAS Reactome:R-HSA-8949580 | ACCEPT | Summary: Mitochondrial inner membrane (TAS). F6 is a mitochondrial complex V subunit attached to the inner-membrane F(o) domain. The Reactome event is 'F1Fo ATP synthase dimerizes'. Accepted. Reason: [file:human/ATP5PF/ATP5PF-uniprot.txt "CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase"] [file:human/ATP5PF/ATP5PF-uniprot.txt "CC peripheric stalk, which acts as a stator to hold the catalytic"] Supporting Evidence: file:human/ATP5PF/ATP5PF-uniprot.txt CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase file:human/ATP5PF/ATP5PF-uniprot.txt CC peripheric stalk, which acts as a stator to hold the catalytic |
| GO:0005743 mitochondrial inner membrane | TAS Reactome:R-HSA-9837978 | ACCEPT | Summary: Mitochondrial inner membrane (TAS). F6 is a mitochondrial complex V subunit attached to the inner-membrane F(o) domain. The Reactome event is 'LONP1 binds mitochondrial inner membrane proteins'. Accepted. Reason: [file:human/ATP5PF/ATP5PF-uniprot.txt "CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase"] [file:human/ATP5PF/ATP5PF-uniprot.txt "CC peripheric stalk, which acts as a stator to hold the catalytic"] Supporting Evidence: file:human/ATP5PF/ATP5PF-uniprot.txt CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase file:human/ATP5PF/ATP5PF-uniprot.txt CC peripheric stalk, which acts as a stator to hold the catalytic |
| GO:0005743 mitochondrial inner membrane | TAS Reactome:R-HSA-9838004 | ACCEPT | Summary: Mitochondrial inner membrane (TAS). F6 is a mitochondrial complex V subunit attached to the inner-membrane F(o) domain. The Reactome event is 'LONP1 degrades mitochondrial inner membrane proteins'. Accepted. Reason: [file:human/ATP5PF/ATP5PF-uniprot.txt "CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase"] [file:human/ATP5PF/ATP5PF-uniprot.txt "CC peripheric stalk, which acts as a stator to hold the catalytic"] Supporting Evidence: file:human/ATP5PF/ATP5PF-uniprot.txt CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase file:human/ATP5PF/ATP5PF-uniprot.txt CC peripheric stalk, which acts as a stator to hold the catalytic |
| GO:0015078 proton transmembrane transporter activity | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: Proton transmembrane transporter activity (IEA, InterPro F6 family). UniProt places F6 in the peripheral stalk (stator) and describes the membrane proton channel as the F(o) domain built from subunits c, a, 8, e, f, g, k and j, a list that does not include F6. An 'enables' transporter activity overstates its role; its contribution is captured by contributes_to rotary ATP synthase activity. Over-annotation. Reason: [file:human/ATP5PF/ATP5PF-uniprot.txt "CC peripheric stalk, which acts as a stator to hold the catalytic"] [file:human/ATP5PF/ATP5PF-uniprot.txt "CC a membrane F(0) domain - the membrane proton channel (subunits c, a, 8,"] Supporting Evidence: file:human/ATP5PF/ATP5PF-uniprot.txt CC peripheric stalk, which acts as a stator to hold the catalytic file:human/ATP5PF/ATP5PF-uniprot.txt CC a membrane F(0) domain - the membrane proton channel (subunits c, a, 8, |
| GO:0015986 proton motive force-driven ATP synthesis | IEA GO_REF:0000002 | ACCEPT | Summary: Proton motive force-driven ATP synthesis (IEA). F6 is a stator subunit needed to couple F(1) catalysis to F(o) proton flow; it takes part in oxidative ATP synthesis. Core process. Reason: [PMID:1825642 "Coupling factor 6 (F6) is a component of mitochondrial ATP synthase which is required for the interactions of the catalytic and proton-translocating segments."] [file:human/ATP5PF/ATP5PF-uniprot.txt "CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase"] Supporting Evidence: PMID:1825642 Coupling factor 6 (F6) is a component of mitochondrial ATP synthase which is required for the interactions of the catalytic and proton-translocating segments. file:human/ATP5PF/ATP5PF-uniprot.txt CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase |
| GO:0015986 proton motive force-driven ATP synthesis | NAS PMID:26297831 Assembly of human mitochondrial ATP synthase through two sep... | ACCEPT | Summary: Proton motive force-driven ATP synthesis (NAS). F6 is a stator subunit needed to couple F(1) catalysis to F(o) proton flow; it takes part in oxidative ATP synthesis. Core process. Reason: [PMID:1825642 "Coupling factor 6 (F6) is a component of mitochondrial ATP synthase which is required for the interactions of the catalytic and proton-translocating segments."] [file:human/ATP5PF/ATP5PF-uniprot.txt "CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase"] Supporting Evidence: PMID:1825642 Coupling factor 6 (F6) is a component of mitochondrial ATP synthase which is required for the interactions of the catalytic and proton-translocating segments. file:human/ATP5PF/ATP5PF-uniprot.txt CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase |
| GO:0021762 substantia nigra development | HEP PMID:22926577 Quantitative proteomic analysis of human substantia nigra in... | MARK AS OVER ANNOTATED | Summary: Substantia nigra development (HEP). The source is a quantitative proteomic comparison of human substantia nigra in Alzheimer's disease, Huntington's disease and multiple sclerosis, in which expression changes were mapped to a developmental term. A ubiquitous complex V subunit detected in such a dataset has no demonstrated role in substantia nigra development. Over-annotation, consistent with how other reviews treat rows from this study. Reason: [file:human/ATP5PF/ATP5PF-uniprot.txt "CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase"] Supporting Evidence: file:human/ATP5PF/ATP5PF-uniprot.txt CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase |
| GO:0042776 proton motive force-driven mitochondrial ATP synthesis | IDA PMID:12110673 A functionally active human F1F0 ATPase can be purified by i... | ACCEPT | Summary: Proton motive force-driven mitochondrial ATP synthesis (IDA). F6 is a stator subunit needed to couple F(1) catalysis to F(o) proton flow; it takes part in oxidative ATP synthesis. Core process. Reason: [PMID:1825642 "Coupling factor 6 (F6) is a component of mitochondrial ATP synthase which is required for the interactions of the catalytic and proton-translocating segments."] [file:human/ATP5PF/ATP5PF-uniprot.txt "CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase"] Supporting Evidence: PMID:1825642 Coupling factor 6 (F6) is a component of mitochondrial ATP synthase which is required for the interactions of the catalytic and proton-translocating segments. file:human/ATP5PF/ATP5PF-uniprot.txt CC -!- FUNCTION: Subunit F6, of the mitochondrial membrane ATP synthase |
| GO:0045259 proton-transporting ATP synthase complex | IBA GO_REF:0000033 | ACCEPT | Summary: Proton-transporting ATP synthase complex (IBA). Coupling factor 6 is a subunit of the peripheral stalk (stator) of complex V. It is required for coupling the catalytic F(1) and proton-translocating F(o) sectors, and it co-purifies with human F1F0. Core. Reason: [PMID:1825642 "Coupling factor 6 (F6) is a component of mitochondrial ATP synthase which is required for the interactions of the catalytic and proton-translocating segments."] [file:human/ATP5PF/ATP5PF-uniprot.txt "CC peripheric stalk, which acts as a stator to hold the catalytic"] [PMID:12110673 "The immunoprecipitated F(1)F(0) contained a full complement of subunits that were identified with specific antibodies against five of the subunits (alpha, beta, OSCP, d, and IF(1)) and by MALDI-TOF and/or LC/MS/MS for all subunits except subunit c, which could not be resolved by these methods because of the limits of detection."] Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000966081 SUPPORTS TRANSFER F6 family node; bovine F6 (P02721) and human ATP5PF (P18859) are experimentally grounded members. Supporting Evidence: PMID:1825642 Coupling factor 6 (F6) is a component of mitochondrial ATP synthase which is required for the interactions of the catalytic and proton-translocating segments. file:human/ATP5PF/ATP5PF-uniprot.txt CC peripheric stalk, which acts as a stator to hold the catalytic PMID:12110673 The immunoprecipitated F(1)F(0) contained a full complement of subunits that were identified with specific antibodies against five of the subunits (alpha, beta, OSCP, d, and IF(1)) and by MALDI-TOF and/or LC/MS/MS for all subunits except subunit c, which could not be resolved by these methods because of the limits of detection. |
| GO:0045259 proton-transporting ATP synthase complex | IDA PMID:12110673 A functionally active human F1F0 ATPase can be purified by i... | ACCEPT | Summary: Proton-transporting ATP synthase complex (IDA). Coupling factor 6 is a subunit of the peripheral stalk (stator) of complex V. It is required for coupling the catalytic F(1) and proton-translocating F(o) sectors, and it co-purifies with human F1F0. Core. Reason: [PMID:1825642 "Coupling factor 6 (F6) is a component of mitochondrial ATP synthase which is required for the interactions of the catalytic and proton-translocating segments."] [file:human/ATP5PF/ATP5PF-uniprot.txt "CC peripheric stalk, which acts as a stator to hold the catalytic"] [PMID:12110673 "The immunoprecipitated F(1)F(0) contained a full complement of subunits that were identified with specific antibodies against five of the subunits (alpha, beta, OSCP, d, and IF(1)) and by MALDI-TOF and/or LC/MS/MS for all subunits except subunit c, which could not be resolved by these methods because of the limits of detection."] Supporting Evidence: PMID:1825642 Coupling factor 6 (F6) is a component of mitochondrial ATP synthase which is required for the interactions of the catalytic and proton-translocating segments. file:human/ATP5PF/ATP5PF-uniprot.txt CC peripheric stalk, which acts as a stator to hold the catalytic PMID:12110673 The immunoprecipitated F(1)F(0) contained a full complement of subunits that were identified with specific antibodies against five of the subunits (alpha, beta, OSCP, d, and IF(1)) and by MALDI-TOF and/or LC/MS/MS for all subunits except subunit c, which could not be resolved by these methods because of the limits of detection. |
| GO:0045259 proton-transporting ATP synthase complex | IEA GO_REF:0000120 | ACCEPT | Summary: Proton-transporting ATP synthase complex (IEA). Coupling factor 6 is a subunit of the peripheral stalk (stator) of complex V. It is required for coupling the catalytic F(1) and proton-translocating F(o) sectors, and it co-purifies with human F1F0. Core. Reason: [PMID:1825642 "Coupling factor 6 (F6) is a component of mitochondrial ATP synthase which is required for the interactions of the catalytic and proton-translocating segments."] [file:human/ATP5PF/ATP5PF-uniprot.txt "CC peripheric stalk, which acts as a stator to hold the catalytic"] [PMID:12110673 "The immunoprecipitated F(1)F(0) contained a full complement of subunits that were identified with specific antibodies against five of the subunits (alpha, beta, OSCP, d, and IF(1)) and by MALDI-TOF and/or LC/MS/MS for all subunits except subunit c, which could not be resolved by these methods because of the limits of detection."] Supporting Evidence: PMID:1825642 Coupling factor 6 (F6) is a component of mitochondrial ATP synthase which is required for the interactions of the catalytic and proton-translocating segments. file:human/ATP5PF/ATP5PF-uniprot.txt CC peripheric stalk, which acts as a stator to hold the catalytic PMID:12110673 The immunoprecipitated F(1)F(0) contained a full complement of subunits that were identified with specific antibodies against five of the subunits (alpha, beta, OSCP, d, and IF(1)) and by MALDI-TOF and/or LC/MS/MS for all subunits except subunit c, which could not be resolved by these methods because of the limits of detection. |
| GO:0045259 proton-transporting ATP synthase complex | NAS PMID:26297831 Assembly of human mitochondrial ATP synthase through two sep... | ACCEPT | Summary: Proton-transporting ATP synthase complex (NAS). Coupling factor 6 is a subunit of the peripheral stalk (stator) of complex V. It is required for coupling the catalytic F(1) and proton-translocating F(o) sectors, and it co-purifies with human F1F0. Core. Reason: [PMID:1825642 "Coupling factor 6 (F6) is a component of mitochondrial ATP synthase which is required for the interactions of the catalytic and proton-translocating segments."] [file:human/ATP5PF/ATP5PF-uniprot.txt "CC peripheric stalk, which acts as a stator to hold the catalytic"] [PMID:12110673 "The immunoprecipitated F(1)F(0) contained a full complement of subunits that were identified with specific antibodies against five of the subunits (alpha, beta, OSCP, d, and IF(1)) and by MALDI-TOF and/or LC/MS/MS for all subunits except subunit c, which could not be resolved by these methods because of the limits of detection."] Supporting Evidence: PMID:1825642 Coupling factor 6 (F6) is a component of mitochondrial ATP synthase which is required for the interactions of the catalytic and proton-translocating segments. file:human/ATP5PF/ATP5PF-uniprot.txt CC peripheric stalk, which acts as a stator to hold the catalytic PMID:12110673 The immunoprecipitated F(1)F(0) contained a full complement of subunits that were identified with specific antibodies against five of the subunits (alpha, beta, OSCP, d, and IF(1)) and by MALDI-TOF and/or LC/MS/MS for all subunits except subunit c, which could not be resolved by these methods because of the limits of detection. |
| GO:0046933 proton-transporting ATP synthase activity, rotational mechanism | IDA PMID:12110673 A functionally active human F1F0 ATPase can be purified by i... | ACCEPT | Summary: Contributes to proton-transporting ATP synthase activity, rotational mechanism (IDA). F6 is part of the stator that holds alpha3beta3 static against the rotor, and it co-purifies with the active, oligomycin-sensitive human enzyme. The contributes_to qualifier fits a non-catalytic stalk subunit. Core. Reason: [PMID:12110673 "The immunoprecipitated F(1)F(0) contained a full complement of subunits that were identified with specific antibodies against five of the subunits (alpha, beta, OSCP, d, and IF(1)) and by MALDI-TOF and/or LC/MS/MS for all subunits except subunit c, which could not be resolved by these methods because of the limits of detection."] [PMID:12110673 "The captured complex V displayed ATP hydrolysis activity that was fully oligomycin and inhibitor protein IF(1)-sensitive."] [file:human/ATP5PF/ATP5PF-uniprot.txt "CC peripheric stalk, which acts as a stator to hold the catalytic"] Supporting Evidence: PMID:12110673 The immunoprecipitated F(1)F(0) contained a full complement of subunits that were identified with specific antibodies against five of the subunits (alpha, beta, OSCP, d, and IF(1)) and by MALDI-TOF and/or LC/MS/MS for all subunits except subunit c, which could not be resolved by these methods because of the limits of detection. PMID:12110673 The captured complex V displayed ATP hydrolysis activity that was fully oligomycin and inhibitor protein IF(1)-sensitive. file:human/ATP5PF/ATP5PF-uniprot.txt CC peripheric stalk, which acts as a stator to hold the catalytic |
| GO:1902600 proton transmembrane transport | IEA GO_REF:0000108 | KEEP AS NON CORE | Summary: Proton transmembrane transport (IEA, GO_REF:0000108). This row was generated from the GO:0015078 transporter-activity row, which is over-annotated for F6. The process term is retained on its own merits at the complex level: F6 takes part in proton-coupled ATP synthesis as the stator that holds the head static against the rotating c-ring, as in the accepted ATP synthesis rows. It does not conduct protons itself, so it is kept as non-core. Reason: [file:human/ATP5PF/ATP5PF-uniprot.txt "CC peripheric stalk, which acts as a stator to hold the catalytic"] [file:human/ATP5PF/ATP5PF-uniprot.txt "CC a membrane F(0) domain - the membrane proton channel (subunits c, a, 8,"] Supporting Evidence: file:human/ATP5PF/ATP5PF-uniprot.txt CC peripheric stalk, which acts as a stator to hold the catalytic file:human/ATP5PF/ATP5PF-uniprot.txt CC a membrane F(0) domain - the membrane proton channel (subunits c, a, 8, |
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Download this section (compressed HTML)Q: Is F6 required for peripheral-stalk assembly in human cells, as subunit d is (loss of d leaves separate F1-c-ring and b-e-g subcomplexes), or is it added late?
Experiment: Deplete ATP5PF in human cells and measure F1-F(o) coupling (oligomycin-sensitive ATP synthesis vs. hydrolysis) and assembly intermediates by complexome profiling.
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