VAPA (VAP-A, VAP-33) is a tail-anchored protein of the endoplasmic reticulum membrane. Its N-terminal major sperm protein (MSP) domain faces the cytosol and binds FFAT and phospho-FFAT motifs in partner proteins, a central coiled coil mediates homo- and hetero-oligomerization with VAPB, and a C-terminal transmembrane segment anchors it in the ER. By capturing FFAT-bearing lipid-transfer proteins (OSBP, CERT, ORPs, STARD3, VPS13A) and other partners (protrudin, WDR44, Kv2 channels), VAPA recruits them to the ER and builds membrane contact sites with the Golgi/trans-Golgi network, endosomes, mitochondria and plasma membrane, so that the partner proteins can move sterols, ceramide and phospholipids between membranes. VAPA itself has no lipid-transfer or catalytic activity. It is also co-opted by hepatitis C virus as an ER platform for viral RNA replication.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000139 Golgi membrane | IDA PMID:24209621 A four-step cycle driven by PI(4)P hydrolysis directs sterol... | KEEP AS NON CORE | Summary: The ERโGolgi contact role is established, while Golgi-side residence needs topological care. Reason: OSBP binds VAPA at the ER and Golgi phosphoinositides through its PH domain. A contact-site localization is mechanistically sound; a broad Golgi-membrane observation is retained as non-core without claiming that the canonical VAPA membrane anchor is inserted into Golgi rather than ER. Supporting Evidence: PMID:24209621 a FFAT motif that interacts with the ER protein VAP-A, and a lipid transfer domain. |
| GO:0005515 protein binding | IPI PMID:10544080 Hepatitis C virus RNA polymerase and NS5A complex with a SNA... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P27958-PRO_0000037576) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:10544080 Hepatitis C virus RNA polymerase and NS5A complex with a SNA... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P27958-PRO_0000037577) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:16227268 Human VAP-B is involved in hepatitis C virus replication thr... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:O95292) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:16227268 Human VAP-B is involved in hepatitis C virus replication thr... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P27958-PRO_0000037576) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:16227268 Human VAP-B is involved in hepatitis C virus replication thr... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P27958-PRO_0000037577) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:16227268 Human VAP-B is involved in hepatitis C virus replication thr... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q03463-PRO_0000278740) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:16227268 Human VAP-B is involved in hepatitis C virus replication thr... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q03463-PRO_0000278741) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:16895911 Efficient trafficking of ceramide from the endoplasmic retic... | MODIFY | Summary: The interaction is an FFAT-motif-dependent recruitment of a partner by the VAPA MSP domain; FFAT motif binding captures it. Reason: Bare protein binding carries no functional information. For this partner (UniProtKB:Q9Y5P4) the interaction with VAPA is mediated by an FFAT or phospho-FFAT motif in the partner bound by the VAPA MSP domain, which is VAPA's core molecular activity. The informative replacement is GO:0033149 FFAT motif binding, already carried by VAPA (IDA, IMP). Proposed replacements: FFAT motif binding Supporting Evidence: PMID:16895911 Both VAPs were actually co-immunoprecipitated with CERT, and the CERT/VAP interaction was abolished by mutations in the FFAT motif. |
| GO:0005515 protein binding | IPI PMID:16996479 Subproteomic study of hepatitis C virus replicon reveals Ras... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P27958-PRO_0000037576) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:18160438 Human butyrate-induced transcript 1 interacts with hepatitis... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q9P035) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:19289470 Promotion of neurite extension by protrudin requires its int... | MODIFY | Summary: The interaction is an FFAT-motif-dependent recruitment of a partner by the VAPA MSP domain; FFAT motif binding captures it. Reason: Bare protein binding carries no functional information. For this partner (UniProtKB:Q5T4F4) the interaction with VAPA is mediated by an FFAT or phospho-FFAT motif in the partner bound by the VAPA MSP domain, which is VAPA's core molecular activity. The informative replacement is GO:0033149 FFAT motif binding, already carried by VAPA (IDA, IMP). Proposed replacements: FFAT motif binding Supporting Evidence: PMID:19289470 Both the interaction between protrudin and VAP-A as well as the induction of process formation by protrudin were markedly inhibited by mutation of the FFAT motif. |
| GO:0005515 protein binding | IPI PMID:19515777 Human VAP-C negatively regulates hepatitis C virus propagati... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:O95292-1) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:19515777 Human VAP-C negatively regulates hepatitis C virus propagati... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q03463-PRO_0000278740) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:19515777 Human VAP-C negatively regulates hepatitis C virus propagati... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q03463-PRO_0000278741) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:19615732 Defining the human deubiquitinating enzyme interaction lands... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q9Y2K6) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P00533) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:21900206 A directed protein interaction network for investigating int... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q96TC7) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:21957124 Viperin inhibits hepatitis C virus replication by interferin... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q8WXG1) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:21957124 Viperin inhibits hepatitis C virus replication by interferin... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q9WMX2-PRO_0000037551) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:21957124 Viperin inhibits hepatitis C virus replication by interferin... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q9WMX2-PRO_0000037552) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:21976701 Protrudin serves as an adaptor molecule that connects KIF5 a... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P33175) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:21976701 Protrudin serves as an adaptor molecule that connects KIF5 a... | MODIFY | Summary: The interaction is an FFAT-motif-dependent recruitment of a partner by the VAPA MSP domain; FFAT motif binding captures it. Reason: Bare protein binding carries no functional information. For this partner (UniProtKB:Q5T4F4) the interaction with VAPA is mediated by an FFAT or phospho-FFAT motif in the partner bound by the VAPA MSP domain, which is VAPA's core molecular activity. The informative replacement is GO:0033149 FFAT motif binding, already carried by VAPA (IDA, IMP). Proposed replacements: FFAT motif binding Supporting Evidence: PMID:19289470 Both the interaction between protrudin and VAP-A as well as the induction of process formation by protrudin were markedly inhibited by mutation of the FFAT motif. |
| GO:0005515 protein binding | IPI PMID:22045669 The antiviral protein viperin inhibits hepatitis C virus rep... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q8WXG1) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:23736259 The ALS8 protein VAPB interacts with the ER-Golgi recycling ... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:O95070) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:23840749 MOR is not enough: identification of novel mu-opioid recepto... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P35372) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:23935497 Rab18 binds to hepatitis C virus NS5A and promotes interacti... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q99IB8-PRO_0000045602) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:24105263 STARD3 or STARD3NL and VAP form a novel molecular tether bet... | MODIFY | Summary: The interaction is an FFAT-motif-dependent recruitment of a partner by the VAPA MSP domain; FFAT motif binding captures it. Reason: Bare protein binding carries no functional information. For this partner (UniProtKB:Q14849-1) the interaction with VAPA is mediated by an FFAT or phospho-FFAT motif in the partner bound by the VAPA MSP domain, which is VAPA's core molecular activity. The informative replacement is GO:0033149 FFAT motif binding, already carried by VAPA (IDA, IMP). Proposed replacements: FFAT motif binding Supporting Evidence: PMID:24105263 STARD3 and STARD3NL use a conserved two phenylalanines in an acidic tract (FFAT)-motif to interact with ER-anchored VAP proteins. |
| GO:0005515 protein binding | IPI PMID:24209621 A four-step cycle driven by PI(4)P hydrolysis directs sterol... | MODIFY | Summary: The interaction is an FFAT-motif-dependent recruitment of a partner by the VAPA MSP domain; FFAT motif binding captures it. Reason: Bare protein binding carries no functional information. For this partner (UniProtKB:P22059) the interaction with VAPA is mediated by an FFAT or phospho-FFAT motif in the partner bound by the VAPA MSP domain, which is VAPA's core molecular activity. The informative replacement is GO:0033149 FFAT motif binding, already carried by VAPA (IDA, IMP). Proposed replacements: FFAT motif binding Supporting Evidence: PMID:24209621 FFAT motif that interacts with the ER protein VAP-A PMID:20178991 we determined the complex structure between the VAP-A MSP domain (VAP-A(MSP)) and the OSBP fragment containing a VAP-A binding motif FFAT (OSBP(F)) by NMR. |
| GO:0005515 protein binding | IPI PMID:25616068 A combined proteomics/genomics approach links hepatitis C vi... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q99IB8-PRO_0000045600) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:25616068 A combined proteomics/genomics approach links hepatitis C vi... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q99IB8-PRO_0000045602) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:25681634 Sterol liganding of OSBP-related proteins (ORPs) regulates t... | MODIFY | Summary: The interaction is an FFAT-motif-dependent recruitment of a partner by the VAPA MSP domain; FFAT motif binding captures it. Reason: Bare protein binding carries no functional information. For this partner (UniProtKB:P22059) the interaction with VAPA is mediated by an FFAT or phospho-FFAT motif in the partner bound by the VAPA MSP domain, which is VAPA's core molecular activity. The informative replacement is GO:0033149 FFAT motif binding, already carried by VAPA (IDA, IMP). Proposed replacements: FFAT motif binding Supporting Evidence: PMID:25681634 a motif targeting the endoplasmic reticulum (ER) via VAMP-associated proteins (VAPs) PMID:20178991 we determined the complex structure between the VAP-A MSP domain (VAP-A(MSP)) and the OSBP fragment containing a VAP-A binding motif FFAT (OSBP(F)) by NMR. |
| GO:0005515 protein binding | IPI PMID:25681634 Sterol liganding of OSBP-related proteins (ORPs) regulates t... | MODIFY | Summary: The interaction is an FFAT-motif-dependent recruitment of a partner by the VAPA MSP domain; FFAT motif binding captures it. Reason: Bare protein binding carries no functional information. For this partner (UniProtKB:Q9H1P3) the interaction with VAPA is mediated by an FFAT or phospho-FFAT motif in the partner bound by the VAPA MSP domain, which is VAPA's core molecular activity. The informative replacement is GO:0033149 FFAT motif binding, already carried by VAPA (IDA, IMP). Proposed replacements: FFAT motif binding Supporting Evidence: PMID:25681634 a motif targeting the endoplasmic reticulum (ER) via VAMP-associated proteins (VAPs) |
| GO:0005515 protein binding | IPI PMID:25910212 Widespread macromolecular interaction perturbations in human... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P05090) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:O95070) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:O95292) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P22059) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q96TC7) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:26618866 โF508 CFTR interactome remodelling promotes rescue of cystic... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P13569) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:28298427 Systematic protein-protein interaction mapping for clinicall... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P35372) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:28377464 STARD3 mediates endoplasmic reticulum-to-endosome cholestero... | MODIFY | Summary: The interaction is an FFAT-motif-dependent recruitment of a partner by the VAPA MSP domain; FFAT motif binding captures it. Reason: Bare protein binding carries no functional information. For this partner (UniProtKB:Q14849) the interaction with VAPA is mediated by an FFAT or phospho-FFAT motif in the partner bound by the VAPA MSP domain, which is VAPA's core molecular activity. The informative replacement is GO:0033149 FFAT motif binding, already carried by VAPA (IDA, IMP). Proposed replacements: FFAT motif binding Supporting Evidence: PMID:24105263 STARD3 and STARD3NL use a conserved two phenylalanines in an acidic tract (FFAT)-motif to interact with ER-anchored VAP proteins. |
| GO:0005515 protein binding | IPI PMID:29858488 Identification of MOSPD2, a novel scaffold for endoplasmic r... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q9BXW6) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:29997244 LuTHy: a double-readout bioluminescence-based two-hybrid tec... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P22059) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:30659099 The activity of Sac1 across ER-TGN contact sites requires th... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q9HB20) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:30659099 The activity of Sac1 across ER-TGN contact sites requires th... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q9NTJ5) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:30741634 Human VPS13A is associated with multiple organelles and infl... | MODIFY | Summary: The interaction is an FFAT-motif-dependent recruitment of a partner by the VAPA MSP domain; FFAT motif binding captures it. Reason: Bare protein binding carries no functional information. For this partner (UniProtKB:Q96RL7) the interaction with VAPA is mediated by an FFAT or phospho-FFAT motif in the partner bound by the VAPA MSP domain, which is VAPA's core molecular activity. The informative replacement is GO:0033149 FFAT motif binding, already carried by VAPA (IDA, IMP). Proposed replacements: FFAT motif binding Supporting Evidence: PMID:30741634 VAP-A via its FFAT domain |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P00533) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:O00559) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:O15173) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:O15209) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:O60669) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:O95214) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P05090) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P11912) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P49447) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P78383) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q06432) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q13520) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q15125) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q53FP2) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q53TN4) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q7Z5P4) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q86VR2) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q8N5M9) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q8N661) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q8NBD8) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q8NBQ5) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q96K78) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q96LZ7) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q9BY50) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q9NS71) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q9NY72) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q9Y2K6) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q9Y320) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:32344433 GRAF2, WDR44, and MICAL1 mediate Rab8/10/11-dependent export... | MODIFY | Summary: The interaction is an FFAT-motif-dependent recruitment of a partner by the VAPA MSP domain; FFAT motif binding captures it. Reason: Bare protein binding carries no functional information. For this partner (UniProtKB:Q5JSH3) the interaction with VAPA is mediated by an FFAT or phospho-FFAT motif in the partner bound by the VAPA MSP domain, which is VAPA's core molecular activity. The informative replacement is GO:0033149 FFAT motif binding, already carried by VAPA (IDA, IMP). Proposed replacements: FFAT motif binding Supporting Evidence: PMID:32344433 WDR44 has an FFAT sequence (Fig. 2 B), and WDR44 ฮFFAT was not coimmunoprecipitated by VAPA |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P22059) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:33124732 FFAT motif phosphorylation controls formation and lipid tran... | MODIFY | Summary: The interaction is an FFAT-motif-dependent recruitment of a partner by the VAPA MSP domain; FFAT motif binding captures it. Reason: Bare protein binding carries no functional information. For this partner (UniProtKB:Q14721, UniProtKB:Q14849, UniProtKB:Q7L4E1, UniProtKB:Q8TDY2, UniProtKB:Q92953, UniProtKB:Q96TC7) the interaction with VAPA is mediated by an FFAT or phospho-FFAT motif in the partner bound by the VAPA MSP domain, which is VAPA's core molecular activity. The informative replacement is GO:0033149 FFAT motif binding, already carried by VAPA (IDA, IMP). Proposed replacements: FFAT motif binding Supporting Evidence: PMID:33124732 In contrast, VAP proteins were efficiently pulled down by all the peptides whose FFAT motif was phosphorylated (STARD3, FIP200, MIGA2, PTPIP51, Kv2.1, and Kv2.2). |
| GO:0005515 protein binding | IPI PMID:33124732 FFAT motif phosphorylation controls formation and lipid tran... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q9P0L0) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:O95292) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P22059) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q5T4F4) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q96LZ7) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q96TC7) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q9BXW6) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q9H1P3) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q9Y2K6) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:35156780 CFTR interactome mapping using the mammalian membrane two-hy... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P13569) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:O15173) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:O95292) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P22059) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q5T4F4) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q96LZ7) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q96TC7) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q9P035) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P00533) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:36012204 Differential CFTR-Interactome Proximity Labeling Procedures ... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P13569) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:O95292) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:P22059) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q96LZ7) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q96TC7) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Generic protein binding is uninformative; removal does not dispute the reported interaction. Reason: Per the GO:0005515 policy, a bare protein-binding row records an interaction (UniProtKB:Q9H1P3) without saying what VAPA does. The source does not establish an FFAT-dependent recruitment for this partner that would justify GO:0033149, and homo- or hetero-oligomerization with VAP family members is already captured by GO:0042803 and GO:0046982. Viral partners, interactome-screen hits and other non-FFAT partners are not converted into a more specific function from interaction evidence alone. |
| GO:0005783 endoplasmic reticulum | HDA PMID:16791210 Dynamic proteomics in individual human cells uncovers widesp... | ACCEPT | Summary: ER membrane anchoring and contact-site residence are integral to VAPA function. Reason: The C-terminal membrane anchor places the MSP domain in the cytosol, where FFAT-bearing partners form membrane contacts. Structural, biochemical and cellular studies establish this topology. An ER-endosome contact annotation describes the tethering assembly rather than VAPA moving wholly onto the endosome. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. |
| GO:0005783 endoplasmic reticulum | IDA GO_REF:0000052 | ACCEPT | Summary: ER membrane anchoring and contact-site residence are integral to VAPA function. Reason: The C-terminal membrane anchor places the MSP domain in the cytosol, where FFAT-bearing partners form membrane contacts. Structural, biochemical and cellular studies establish this topology. An ER-endosome contact annotation describes the tethering assembly rather than VAPA moving wholly onto the endosome. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. |
| GO:0005783 endoplasmic reticulum | IDA PMID:18713837 FFAT rescues VAPA-mediated inhibition of ER-to-Golgi transpo... | ACCEPT | Summary: ER membrane anchoring and contact-site residence are integral to VAPA function. Reason: The C-terminal membrane anchor places the MSP domain in the cytosol, where FFAT-bearing partners form membrane contacts. Structural, biochemical and cellular studies establish this topology. An ER-endosome contact annotation describes the tethering assembly rather than VAPA moving wholly onto the endosome. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. |
| GO:0005783 endoplasmic reticulum | IDA PMID:19289470 Promotion of neurite extension by protrudin requires its int... | ACCEPT | Summary: ER membrane anchoring and contact-site residence are integral to VAPA function. Reason: The C-terminal membrane anchor places the MSP domain in the cytosol, where FFAT-bearing partners form membrane contacts. Structural, biochemical and cellular studies establish this topology. An ER-endosome contact annotation describes the tethering assembly rather than VAPA moving wholly onto the endosome. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. |
| GO:0005783 endoplasmic reticulum | IEA GO_REF:0000107 | ACCEPT | Summary: ER membrane anchoring and contact-site residence are integral to VAPA function. Reason: The C-terminal membrane anchor places the MSP domain in the cytosol, where FFAT-bearing partners form membrane contacts. Structural, biochemical and cellular studies establish this topology. An ER-endosome contact annotation describes the tethering assembly rather than VAPA moving wholly onto the endosome. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. |
| GO:0005789 endoplasmic reticulum membrane | IBA GO_REF:0000033 | ACCEPT | Summary: ER membrane anchoring and contact-site residence are integral to VAPA function. Reason: The C-terminal membrane anchor places the MSP domain in the cytosol, where FFAT-bearing partners form membrane contacts. Structural, biochemical and cellular studies establish this topology. An ER-endosome contact annotation describes the tethering assembly rather than VAPA moving wholly onto the endosome. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. |
| GO:0005789 endoplasmic reticulum membrane | IDA PMID:12023275 Vesicle-associated membrane protein-associated protein-A (VA... | ACCEPT | Summary: ER membrane anchoring and contact-site residence are integral to VAPA function. Reason: The C-terminal membrane anchor places the MSP domain in the cytosol, where FFAT-bearing partners form membrane contacts. Structural, biochemical and cellular studies establish this topology. An ER-endosome contact annotation describes the tethering assembly rather than VAPA moving wholly onto the endosome. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. |
| GO:0005789 endoplasmic reticulum membrane | IDA PMID:19564404 Cholesterol sensor ORP1L contacts the ER protein VAP to cont... | ACCEPT | Summary: ER membrane anchoring and contact-site residence are integral to VAPA function. Reason: The C-terminal membrane anchor places the MSP domain in the cytosol, where FFAT-bearing partners form membrane contacts. Structural, biochemical and cellular studies establish this topology. An ER-endosome contact annotation describes the tethering assembly rather than VAPA moving wholly onto the endosome. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. |
| GO:0005789 endoplasmic reticulum membrane | IDA PMID:30741634 Human VPS13A is associated with multiple organelles and infl... | ACCEPT | Summary: ER membrane anchoring and contact-site residence are integral to VAPA function. Reason: The C-terminal membrane anchor places the MSP domain in the cytosol, where FFAT-bearing partners form membrane contacts. Structural, biochemical and cellular studies establish this topology. An ER-endosome contact annotation describes the tethering assembly rather than VAPA moving wholly onto the endosome. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. |
| GO:0005789 endoplasmic reticulum membrane | IDA PMID:32234213 Calcium-stimulated disassembly of focal adhesions mediated b... | ACCEPT | Summary: ER membrane anchoring and contact-site residence are integral to VAPA function. Reason: The C-terminal membrane anchor places the MSP domain in the cytosol, where FFAT-bearing partners form membrane contacts. Structural, biochemical and cellular studies establish this topology. An ER-endosome contact annotation describes the tethering assembly rather than VAPA moving wholly onto the endosome. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. |
| GO:0005789 endoplasmic reticulum membrane | IDA PMID:32344433 GRAF2, WDR44, and MICAL1 mediate Rab8/10/11-dependent export... | ACCEPT | Summary: ER membrane anchoring and contact-site residence are integral to VAPA function. Reason: The C-terminal membrane anchor places the MSP domain in the cytosol, where FFAT-bearing partners form membrane contacts. Structural, biochemical and cellular studies establish this topology. An ER-endosome contact annotation describes the tethering assembly rather than VAPA moving wholly onto the endosome. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. |
| GO:0005789 endoplasmic reticulum membrane | IDA PMID:33124732 FFAT motif phosphorylation controls formation and lipid tran... | ACCEPT | Summary: ER membrane anchoring and contact-site residence are integral to VAPA function. Reason: The C-terminal membrane anchor places the MSP domain in the cytosol, where FFAT-bearing partners form membrane contacts. Structural, biochemical and cellular studies establish this topology. An ER-endosome contact annotation describes the tethering assembly rather than VAPA moving wholly onto the endosome. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. |
| GO:0005789 endoplasmic reticulum membrane | IDA PMID:41856286 Glycolipid transfer protein modulates vesicular trafficking ... | ACCEPT | Summary: ER membrane anchoring and contact-site residence are integral to VAPA function. Reason: The C-terminal membrane anchor places the MSP domain in the cytosol, where FFAT-bearing partners form membrane contacts. Structural, biochemical and cellular studies establish this topology. An ER-endosome contact annotation describes the tethering assembly rather than VAPA moving wholly onto the endosome. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000120 | ACCEPT | Summary: ER membrane anchoring and contact-site residence are integral to VAPA function. Reason: The C-terminal membrane anchor places the MSP domain in the cytosol, where FFAT-bearing partners form membrane contacts. Structural, biochemical and cellular studies establish this topology. An ER-endosome contact annotation describes the tethering assembly rather than VAPA moving wholly onto the endosome. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-429730 | ACCEPT | Summary: ER membrane anchoring and contact-site residence are integral to VAPA function. Reason: The C-terminal membrane anchor places the MSP domain in the cytosol, where FFAT-bearing partners form membrane contacts. Structural, biochemical and cellular studies establish this topology. An ER-endosome contact annotation describes the tethering assembly rather than VAPA moving wholly onto the endosome. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-9956909 | ACCEPT | Summary: ER membrane anchoring and contact-site residence are integral to VAPA function. Reason: The C-terminal membrane anchor places the MSP domain in the cytosol, where FFAT-bearing partners form membrane contacts. Structural, biochemical and cellular studies establish this topology. An ER-endosome contact annotation describes the tethering assembly rather than VAPA moving wholly onto the endosome. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9609921 | KEEP AS NON CORE | Summary: Retain the ancillary localization without replacing the principal ER-membrane topology. Reason: The curated source reports this location or pathway-associated pool. VAPA has a cytosol-facing ER domain and peripheral/perinuclear membrane pools; such observations do not make the intact canonical protein a freely soluble cytosolic factor or establish an independent core function. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Retain the reported peripheral membrane/junctional/vesicular pool. Reason: The primary localization study detects VAP-33 with occludin at tight junctions and in intracellular vesicles. These pools are compatible with the ER-tether biology but are not the principal site of core function. Supporting Evidence: PMID:10523508 Antibodies to the human VAP-33 co-localized with occludin at the tight junction in many tissues and tissue culture cell lines. |
| GO:0005886 plasma membrane | IDA PMID:10523508 VAP-33 localizes to both an intracellular vesicle population... | KEEP AS NON CORE | Summary: Retain the reported peripheral membrane/junctional/vesicular pool. Reason: The primary localization study detects VAP-33 with occludin at tight junctions and in intracellular vesicles. These pools are compatible with the ER-tether biology but are not the principal site of core function. Supporting Evidence: PMID:10523508 Antibodies to the human VAP-33 co-localized with occludin at the tight junction in many tissues and tissue culture cell lines. |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Retain the reported peripheral membrane/junctional/vesicular pool. Reason: The primary localization study detects VAP-33 with occludin at tight junctions and in intracellular vesicles. These pools are compatible with the ER-tether biology but are not the principal site of core function. Supporting Evidence: PMID:10523508 Antibodies to the human VAP-33 co-localized with occludin at the tight junction in many tissues and tissue culture cell lines. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6798739 | KEEP AS NON CORE | Summary: Retain the reported peripheral membrane/junctional/vesicular pool. Reason: The primary localization study detects VAP-33 with occludin at tight junctions and in intracellular vesicles. These pools are compatible with the ER-tether biology but are not the principal site of core function. Supporting Evidence: PMID:10523508 Antibodies to the human VAP-33 co-localized with occludin at the tight junction in many tissues and tissue culture cell lines. |
| GO:0005923 bicellular tight junction | IDA PMID:10523508 VAP-33 localizes to both an intracellular vesicle population... | KEEP AS NON CORE | Summary: Retain the reported peripheral membrane/junctional/vesicular pool. Reason: The primary localization study detects VAP-33 with occludin at tight junctions and in intracellular vesicles. These pools are compatible with the ER-tether biology but are not the principal site of core function. Supporting Evidence: PMID:10523508 Antibodies to the human VAP-33 co-localized with occludin at the tight junction in many tissues and tissue culture cell lines. |
| GO:0005923 bicellular tight junction | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Retain the reported peripheral membrane/junctional/vesicular pool. Reason: The primary localization study detects VAP-33 with occludin at tight junctions and in intracellular vesicles. These pools are compatible with the ER-tether biology but are not the principal site of core function. Supporting Evidence: PMID:10523508 Antibodies to the human VAP-33 co-localized with occludin at the tight junction in many tissues and tissue culture cell lines. |
| GO:0006649 phospholipid transfer to membrane | IDA PMID:39106189 The ORP9-ORP11 dimer promotes sphingomyelin synthesis. | ACCEPT | Summary: VAPA contributes to lipid transfer and homeostasis through membrane-contact organization. Reason: VAPA anchors FFAT-containing lipid-transfer proteins such as OSBP/STARD3 and thereby participates mechanistically in lipid movement. The transported lipid is handled by the partner, not an intrinsic VAPA carrier pocket. Protein-membrane adaptor activity and this biological-process participation are compatible; the annotation does not require VAPA to catalyze lipid synthesis. Supporting Evidence: PMID:24209621 a FFAT motif that interacts with the ER protein VAP-A, and a lipid transfer domain. |
| GO:0006672 ceramide metabolic process | EXP PMID:34688657 Intellectual-disability-associated mutations in the ceramide... | KEEP AS NON CORE | Summary: Ceramide metabolism is a downstream consequence of VAPA-dependent CERT recruitment; non-core. Reason: VAPA contributes only the ER-side FFAT receptor that positions lipid-transfer proteins such as CERT, OSBP, ORP1L and STARD3; the metabolic enzymes and lipid carriers perform the chemistry and the transfer. The contact-site lipid-transport terms describe VAPA's contribution most directly; this broader metabolic or homeostatic outcome is retained as non-core rather than core. Supporting Evidence: PMID:12023275 A fluorescent ceramide analogue also accumulated in these ER inclusions, and export to the Golgi was partially inhibited |
| GO:0006686 sphingomyelin biosynthetic process | IMP PMID:12023275 Vesicle-associated membrane protein-associated protein-A (VA... | KEEP AS NON CORE | Summary: Sphingomyelin synthesis depends on VAPA-anchored ceramide and sterol transfer; VAPA catalyses no step, so this is non-core. Reason: VAPA contributes only the ER-side FFAT receptor that positions lipid-transfer proteins such as CERT, OSBP, ORP1L and STARD3; the metabolic enzymes and lipid carriers perform the chemistry and the transfer. The contact-site lipid-transport terms describe VAPA's contribution most directly; this broader metabolic or homeostatic outcome is retained as non-core rather than core. Supporting Evidence: PMID:12023275 A fluorescent ceramide analogue also accumulated in these ER inclusions, and export to the Golgi was partially inhibited |
| GO:0006888 endoplasmic reticulum to Golgi vesicle-mediated transport | IDA PMID:41856286 Glycolipid transfer protein modulates vesicular trafficking ... | KEEP AS NON CORE | Summary: VAPA influences ER-to-Golgi traffic through FFAT partners; this is a non-core, context-specific role. Reason: Overexpression of VAPA inhibits ER-to-Golgi transport (PMID:18713837), and the FFAT-dependent GLTP-VAPA interaction modulates vesicular export from the ER (PMID:41856286). These support an influence on ER-to-Golgi traffic mediated by recruited partners, but VAPA is not a coat, cargo receptor or fusion component, so the role is kept as non-core. Supporting Evidence: PMID:41856286 The specific mechanism through which the FFAT-mediated GLTP/VAPA interaction drives the ER-to-Golgi vesicle transport is so far unclear. |
| GO:0006888 endoplasmic reticulum to Golgi vesicle-mediated transport | IMP PMID:18713837 FFAT rescues VAPA-mediated inhibition of ER-to-Golgi transpo... | KEEP AS NON CORE | Summary: VAPA influences ER-to-Golgi traffic through FFAT partners; this is a non-core, context-specific role. Reason: Overexpression of VAPA inhibits ER-to-Golgi transport (PMID:18713837), and the FFAT-dependent GLTP-VAPA interaction modulates vesicular export from the ER (PMID:41856286). These support an influence on ER-to-Golgi traffic mediated by recruited partners, but VAPA is not a coat, cargo receptor or fusion component, so the role is kept as non-core. Supporting Evidence: PMID:41856286 The specific mechanism through which the FFAT-mediated GLTP/VAPA interaction drives the ER-to-Golgi vesicle transport is so far unclear. |
| GO:0007029 endoplasmic reticulum organization | IMP NOT PMID:18713837 FFAT rescues VAPA-mediated inhibition of ER-to-Golgi transpo... | ACCEPT | Summary: NOT annotation accepted: VAPA overexpression blocks cargo export but, unlike VAPB-P56S, does not reorganize the ER into aggregates. Reason: This is a negated annotation. The study contrasts the transport block caused by wild-type VAPA overexpression with the large ER aggregates caused by the ALS-linked VAPB-P56S mutant. The negative result for VAPA in ER organization is consistent with VAPA acting as a membrane receptor rather than an ER-shaping protein, and the curator read the full text. The negation is accepted. Supporting Evidence: PMID:18713837 The P56S mutation of the B isoform (VAPB) has been linked to late-onset amyotrophic lateral sclerosis (ALS8) and its expression causes formation of large ER aggregates. |
| GO:0008017 microtubule binding | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Microtubule association is a supported ancillary property. Reason: The VAPA overexpression study links inhibited lateral membrane diffusion to stable microtubule association and reports disruption by FFAT peptide. This supports association without making VAPA a motor or a primary microtubule structural subunit. Supporting Evidence: PMID:18713837 Application of a FFAT peptide restored in vitro ER vesicle budding and disrupted VAP-microtubule association. |
| GO:0008017 microtubule binding | IMP PMID:18713837 FFAT rescues VAPA-mediated inhibition of ER-to-Golgi transpo... | KEEP AS NON CORE | Summary: Microtubule association is a supported ancillary property. Reason: The VAPA overexpression study links inhibited lateral membrane diffusion to stable microtubule association and reports disruption by FFAT peptide. This supports association without making VAPA a motor or a primary microtubule structural subunit. Supporting Evidence: PMID:18713837 Application of a FFAT peptide restored in vitro ER vesicle budding and disrupted VAP-microtubule association. |
| GO:0015630 microtubule cytoskeleton | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Microtubule association is a supported ancillary property. Reason: The VAPA overexpression study links inhibited lateral membrane diffusion to stable microtubule association and reports disruption by FFAT peptide. This supports association without making VAPA a motor or a primary microtubule structural subunit. Supporting Evidence: PMID:18713837 Application of a FFAT peptide restored in vitro ER vesicle budding and disrupted VAP-microtubule association. |
| GO:0015914 phospholipid transport | IDA PMID:24209621 A four-step cycle driven by PI(4)P hydrolysis directs sterol... | ACCEPT | Summary: VAPA contributes to lipid transfer and homeostasis through membrane-contact organization. Reason: VAPA anchors FFAT-containing lipid-transfer proteins such as OSBP/STARD3 and thereby participates mechanistically in lipid movement. The transported lipid is handled by the partner, not an intrinsic VAPA carrier pocket. Protein-membrane adaptor activity and this biological-process participation are compatible; the annotation does not require VAPA to catalyze lipid synthesis. Supporting Evidence: PMID:24209621 a FFAT motif that interacts with the ER protein VAP-A, and a lipid transfer domain. |
| GO:0015918 sterol transport | IDA PMID:24209621 A four-step cycle driven by PI(4)P hydrolysis directs sterol... | ACCEPT | Summary: VAPA contributes to lipid transfer and homeostasis through membrane-contact organization. Reason: VAPA anchors FFAT-containing lipid-transfer proteins such as OSBP/STARD3 and thereby participates mechanistically in lipid movement. The transported lipid is handled by the partner, not an intrinsic VAPA carrier pocket. Protein-membrane adaptor activity and this biological-process participation are compatible; the annotation does not require VAPA to catalyze lipid synthesis. Supporting Evidence: PMID:24209621 a FFAT motif that interacts with the ER protein VAP-A, and a lipid transfer domain. |
| GO:0019076 viral release from host cell | IDA PMID:19515777 Human VAP-C negatively regulates hepatitis C virus propagati... | UNDECIDED | Summary: The study measures HCV replication and propagation; a specific role in viral release is not shown. Reason: The cached abstract reports that VAPA overexpression enhanced HCV replication and that VAP-C reduced propagation of the JFH1 strain, but does not describe an assay of virion release. The full text, which is not cached, may contain a release assay; without it this row cannot be accepted or rejected. Supporting Evidence: PMID:19515777 Overexpression of VAP-C impaired the RNA replication of the HCV replicon and the propagation of the HCV JFH1 strain, whereas overexpression of VAP-A and VAP-B enhanced the replication. |
| GO:0019076 viral release from host cell | IEA GO_REF:0000117 | UNDECIDED | Summary: The study measures HCV replication and propagation; a specific role in viral release is not shown. Reason: The cached abstract reports that VAPA overexpression enhanced HCV replication and that VAP-C reduced propagation of the JFH1 strain, but does not describe an assay of virion release. The full text, which is not cached, may contain a release assay; without it this row cannot be accepted or rejected. Supporting Evidence: PMID:19515777 Overexpression of VAP-C impaired the RNA replication of the HCV replicon and the propagation of the HCV JFH1 strain, whereas overexpression of VAP-A and VAP-B enhanced the replication. |
| GO:0019904 protein domain specific binding | IPI PMID:20178991 Electrostatic interaction between oxysterol-binding protein ... | MODIFY | Summary: FFAT motif binding gives a more informative molecular description. Reason: The VAPA-OSBP interaction is formed between the VAPA MSP domain and the FFAT motif of OSBP, as shown by the NMR structure of the complex in this paper. GO:0033149 FFAT motif binding names this domain-motif interaction precisely. Proposed replacements: FFAT motif binding Supporting Evidence: PMID:20178991 we determined the complex structure between the VAP-A MSP domain (VAP-A(MSP)) and the OSBP fragment containing a VAP-A binding motif FFAT (OSBP(F)) by NMR. |
| GO:0030301 cholesterol transport | IDA PMID:33124732 FFAT motif phosphorylation controls formation and lipid tran... | ACCEPT | Summary: VAPA contributes to lipid transfer and homeostasis through membrane-contact organization. Reason: VAPA anchors FFAT-containing lipid-transfer proteins such as OSBP/STARD3 and thereby participates mechanistically in lipid movement. The transported lipid is handled by the partner, not an intrinsic VAPA carrier pocket. Protein-membrane adaptor activity and this biological-process participation are compatible; the annotation does not require VAPA to catalyze lipid synthesis. Supporting Evidence: PMID:24209621 a FFAT motif that interacts with the ER protein VAP-A, and a lipid transfer domain. |
| GO:0030301 cholesterol transport | IEA GO_REF:0000117 | ACCEPT | Summary: VAPA contributes to lipid transfer and homeostasis through membrane-contact organization. Reason: VAPA anchors FFAT-containing lipid-transfer proteins such as OSBP/STARD3 and thereby participates mechanistically in lipid movement. The transported lipid is handled by the partner, not an intrinsic VAPA carrier pocket. Protein-membrane adaptor activity and this biological-process participation are compatible; the annotation does not require VAPA to catalyze lipid synthesis. Supporting Evidence: PMID:24209621 a FFAT motif that interacts with the ER protein VAP-A, and a lipid transfer domain. |
| GO:0031175 neuron projection development | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Neuronal projection development is a supported downstream context of VAPA trafficking. Reason: VAPA binds the protrudin/ZFYVE27 pathway and helps organize membrane delivery in neuronal processes. The developmental phenotype is retained as non-core rather than being treated as a separate biochemical activity. Supporting Evidence: file:human/VAPA/VAPA-uniprot.txt Interacts (via MSP domain) with ZFYVE27 |
| GO:0031175 neuron projection development | IMP PMID:19289470 Promotion of neurite extension by protrudin requires its int... | KEEP AS NON CORE | Summary: Neuronal projection development is a supported downstream context of VAPA trafficking. Reason: VAPA binds the protrudin/ZFYVE27 pathway and helps organize membrane delivery in neuronal processes. The developmental phenotype is retained as non-core rather than being treated as a separate biochemical activity. Supporting Evidence: file:human/VAPA/VAPA-uniprot.txt Interacts (via MSP domain) with ZFYVE27 |
| GO:0031965 nuclear membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Retain the ancillary localization without replacing the principal ER-membrane topology. Reason: The curated source reports this location or pathway-associated pool. VAPA has a cytosol-facing ER domain and peripheral/perinuclear membrane pools; such observations do not make the intact canonical protein a freely soluble cytosolic factor or establish an independent core function. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. |
| GO:0031965 nuclear membrane | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Retain the ancillary localization without replacing the principal ER-membrane topology. Reason: The curated source reports this location or pathway-associated pool. VAPA has a cytosol-facing ER domain and peripheral/perinuclear membrane pools; such observations do not make the intact canonical protein a freely soluble cytosolic factor or establish an independent core function. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. |
| GO:0031982 vesicle | IDA PMID:10523508 VAP-33 localizes to both an intracellular vesicle population... | KEEP AS NON CORE | Summary: Retain the reported peripheral membrane/junctional/vesicular pool. Reason: The primary localization study detects VAP-33 with occludin at tight junctions and in intracellular vesicles. These pools are compatible with the ER-tether biology but are not the principal site of core function. Supporting Evidence: PMID:10523508 Antibodies to the human VAP-33 co-localized with occludin at the tight junction in many tissues and tissue culture cell lines. |
| GO:0032374 regulation of cholesterol transport | IDA PMID:41741634 STARD3 regulates lysosome positioning and contacts via a GSK... | KEEP AS NON CORE | Summary: Regulation of cholesterol transport via phosphorylation-gated STARD3-VAP contacts; non-core. Reason: VAPA contributes only the ER-side FFAT receptor that positions lipid-transfer proteins such as CERT, OSBP, ORP1L and STARD3; the metabolic enzymes and lipid carriers perform the chemistry and the transfer. The contact-site lipid-transport terms describe VAPA's contribution most directly; this broader metabolic or homeostatic outcome is retained as non-core rather than core. Supporting Evidence: PMID:24209621 a FFAT motif that interacts with the ER protein VAP-A, and a lipid transfer domain. |
| GO:0033149 FFAT motif binding | IDA PMID:33124732 FFAT motif phosphorylation controls formation and lipid tran... | ACCEPT | Summary: FFAT motif recognition is a directly established molecular activity. Reason: MSP-domain structures and peptide pull-down assays establish binding to conventional and phosphorylated FFAT motifs. This specific activity explains recruitment of lipid-transfer and trafficking partners. Supporting Evidence: PMID:33124732 The FFAT of ORP1 efficiently pulled down VAPโA and VAPโB from the whole cell protein extract |
| GO:0033149 FFAT motif binding | IEA GO_REF:0000117 | ACCEPT | Summary: FFAT motif recognition is a directly established molecular activity. Reason: MSP-domain structures and peptide pull-down assays establish binding to conventional and phosphorylated FFAT motifs. This specific activity explains recruitment of lipid-transfer and trafficking partners. Supporting Evidence: PMID:33124732 The FFAT of ORP1 efficiently pulled down VAPโA and VAPโB from the whole cell protein extract |
| GO:0033149 FFAT motif binding | IMP PMID:18713837 FFAT rescues VAPA-mediated inhibition of ER-to-Golgi transpo... | ACCEPT | Summary: FFAT motif recognition is a directly established molecular activity. Reason: MSP-domain structures and peptide pull-down assays establish binding to conventional and phosphorylated FFAT motifs. This specific activity explains recruitment of lipid-transfer and trafficking partners. Supporting Evidence: PMID:33124732 The FFAT of ORP1 efficiently pulled down VAPโA and VAPโB from the whole cell protein extract |
| GO:0034975 protein folding in endoplasmic reticulum | IMP NOT PMID:18713837 FFAT rescues VAPA-mediated inhibition of ER-to-Golgi transpo... | ACCEPT | Summary: NOT annotation accepted: the VAPA-induced transport block reflects impaired cargo segregation, not a role in protein folding. Reason: This is a negated annotation. The cited study attributes the VAPA-overexpression export block to decreased segregation of membrane cargo into ER vesicles and reduced lateral diffusion, which the curator recorded as evidence against a role in ER protein folding. Nothing in the VAPA literature indicates a chaperone or folding activity, so the negation is accepted and deferred to the curator who read the full text. Supporting Evidence: PMID:18713837 This transport block by VAPA was primarily due to decreased segregation of membrane cargo into ER vesicles. |
| GO:0035577 azurophil granule membrane | TAS Reactome:R-HSA-6798739 | KEEP AS NON CORE | Summary: Retain the ancillary localization without replacing the principal ER-membrane topology. Reason: The curated source reports this location or pathway-associated pool. VAPA has a cytosol-facing ER domain and peripheral/perinuclear membrane pools; such observations do not make the intact canonical protein a freely soluble cytosolic factor or establish an independent core function. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. |
| GO:0035621 ER to Golgi ceramide transport | IDA PMID:34688657 Intellectual-disability-associated mutations in the ceramide... | ACCEPT | Summary: VAPA participates in ceramide trafficking and sphingomyelin production through lipid-transfer-protein recruitment. Reason: The VAPAโOSBP perturbation study PMID:12023275 links ER ceramide retention to reduced Golgi export and sphingomyelin synthesis. VAPA is a membrane-contact adaptor rather than the lipid carrier or sphingomyelin synthase. This supports participation in the annotated process without assigning intrinsic lipid-transfer chemistry. The cited CERT-mutant study observes VAP-A-positive puncta; the interpretation is supported jointly with the direct VAPA perturbation evidence. Supporting Evidence: PMID:12023275 A fluorescent ceramide analogue also accumulated in these ER inclusions, and export to the Golgi was partially inhibited |
| GO:0035627 ceramide transport | IMP PMID:12023275 Vesicle-associated membrane protein-associated protein-A (VA... | ACCEPT | Summary: VAPA participates in ceramide trafficking and sphingomyelin production through lipid-transfer-protein recruitment. Reason: The VAPAโOSBP perturbation study PMID:12023275 links ER ceramide retention to reduced Golgi export and sphingomyelin synthesis. VAPA is a membrane-contact adaptor rather than the lipid carrier or sphingomyelin synthase. This supports participation in the annotated process without assigning intrinsic lipid-transfer chemistry. Supporting Evidence: PMID:12023275 A fluorescent ceramide analogue also accumulated in these ER inclusions, and export to the Golgi was partially inhibited |
| GO:0042632 cholesterol homeostasis | IDA PMID:19564404 Cholesterol sensor ORP1L contacts the ER protein VAP to cont... | KEEP AS NON CORE | Summary: Cholesterol homeostasis is a downstream outcome of VAPA-anchored sterol sensors and transporters; non-core. Reason: VAPA contributes only the ER-side FFAT receptor that positions lipid-transfer proteins such as CERT, OSBP, ORP1L and STARD3; the metabolic enzymes and lipid carriers perform the chemistry and the transfer. The contact-site lipid-transport terms describe VAPA's contribution most directly; this broader metabolic or homeostatic outcome is retained as non-core rather than core. Supporting Evidence: PMID:24209621 a FFAT motif that interacts with the ER protein VAP-A, and a lipid transfer domain. |
| GO:0042803 protein homodimerization activity | IDA PMID:33124732 FFAT motif phosphorylation controls formation and lipid tran... | KEEP AS NON CORE | Summary: VAPA oligomerization supports assembly but is not the main functional description. Reason: VAPA forms homo- and VAPB heterodimers. Retain the interaction property while prioritizing FFAT recognition and membrane adaptor activity as the core molecular mechanism. Supporting Evidence: file:human/VAPA/VAPA-uniprot.txt Homodimer; disulfide-linked file:human/VAPA/VAPA-uniprot.txt Heterodimer with VAPB |
| GO:0043123 positive regulation of canonical NF-kappaB signal transduction | HMP PMID:12761501 Large-scale identification and characterization of human gen... | MARK AS OVER ANNOTATED | Summary: An overexpression reporter screen hit does not establish a role for VAPA in NF-kappaB signalling. Reason: The annotation derives from a genome-scale screen in which each cDNA was overexpressed in HEK293 cells and scored for NF-kappaB reporter activation. Overexpressed ER membrane proteins can activate stress-linked NF-kappaB signalling nonspecifically, and no focused study places VAPA in the canonical pathway. The row is kept only as an over-annotated screen observation. Supporting Evidence: PMID:12761501 examined whether it activated the transcription of a luciferase reporter gene driven by a promoter containing the consensus NF-kappaB binding sites |
| GO:0043495 protein-membrane adaptor activity | IBA GO_REF:0000033 | ACCEPT | Summary: VAPA anchors partner proteins and tethers the ER to opposing membranes. Reason: Direct FFAT recognition and reconstituted/cellular contact-site experiments support protein-membrane adaptor and ER-endosome tether activity. VAPA supplies the ER anchor; associated lipid-transfer proteins provide cargo transfer. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. PMID:33124732 The FFAT of ORP1 efficiently pulled down VAPโA and VAPโB from the whole cell protein extract file:human/VAPA/VAPA-deep-research-falcon.md Accordingly, VAPA has no known catalytic reaction, pore, or transported substrate of its own. |
| GO:0043495 protein-membrane adaptor activity | IDA PMID:19564404 Cholesterol sensor ORP1L contacts the ER protein VAP to cont... | ACCEPT | Summary: VAPA anchors partner proteins and tethers the ER to opposing membranes. Reason: Direct FFAT recognition and reconstituted/cellular contact-site experiments support protein-membrane adaptor and ER-endosome tether activity. VAPA supplies the ER anchor; associated lipid-transfer proteins provide cargo transfer. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. PMID:33124732 The FFAT of ORP1 efficiently pulled down VAPโA and VAPโB from the whole cell protein extract |
| GO:0043495 protein-membrane adaptor activity | IDA PMID:32234213 Calcium-stimulated disassembly of focal adhesions mediated b... | ACCEPT | Summary: VAPA anchors partner proteins and tethers the ER to opposing membranes. Reason: Direct FFAT recognition and reconstituted/cellular contact-site experiments support protein-membrane adaptor and ER-endosome tether activity. VAPA supplies the ER anchor; associated lipid-transfer proteins provide cargo transfer. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. PMID:33124732 The FFAT of ORP1 efficiently pulled down VAPโA and VAPโB from the whole cell protein extract |
| GO:0043495 protein-membrane adaptor activity | IDA PMID:34688657 Intellectual-disability-associated mutations in the ceramide... | ACCEPT | Summary: VAPA anchors partner proteins and tethers the ER to opposing membranes. Reason: Direct FFAT recognition and reconstituted/cellular contact-site experiments support protein-membrane adaptor and ER-endosome tether activity. VAPA supplies the ER anchor; associated lipid-transfer proteins provide cargo transfer. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. PMID:33124732 The FFAT of ORP1 efficiently pulled down VAPโA and VAPโB from the whole cell protein extract |
| GO:0043495 protein-membrane adaptor activity | IDA PMID:39106189 The ORP9-ORP11 dimer promotes sphingomyelin synthesis. | ACCEPT | Summary: VAPA anchors partner proteins and tethers the ER to opposing membranes. Reason: Direct FFAT recognition and reconstituted/cellular contact-site experiments support protein-membrane adaptor and ER-endosome tether activity. VAPA supplies the ER anchor; associated lipid-transfer proteins provide cargo transfer. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. PMID:33124732 The FFAT of ORP1 efficiently pulled down VAPโA and VAPโB from the whole cell protein extract |
| GO:0043495 protein-membrane adaptor activity | IDA PMID:41856286 Glycolipid transfer protein modulates vesicular trafficking ... | ACCEPT | Summary: VAPA anchors partner proteins and tethers the ER to opposing membranes. Reason: Direct FFAT recognition and reconstituted/cellular contact-site experiments support protein-membrane adaptor and ER-endosome tether activity. VAPA supplies the ER anchor; associated lipid-transfer proteins provide cargo transfer. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. PMID:33124732 The FFAT of ORP1 efficiently pulled down VAPโA and VAPโB from the whole cell protein extract |
| GO:0044828 host-mediated suppression of viral genome replication | IDA PMID:19515777 Human VAP-C negatively regulates hepatitis C virus propagati... | REMOVE | Summary: The suppressive activity in this study belongs to the VAPB splice variant VAP-C; VAPA itself enhanced replication. Reason: The cited abstract states explicitly that VAP-C, a VAPB splice product, impaired HCV replication, whereas overexpression of VAP-A enhanced it. The same paper supports the opposite direction for VAPA (GO:0044829, kept). Host-mediated suppression of viral genome replication is therefore contradicted for VAPA by the source itself, and the IEA row repeats it. Supporting Evidence: PMID:19515777 Overexpression of VAP-C impaired the RNA replication of the HCV replicon and the propagation of the HCV JFH1 strain, whereas overexpression of VAP-A and VAP-B enhanced the replication. |
| GO:0044828 host-mediated suppression of viral genome replication | IEA GO_REF:0000117 | REMOVE | Summary: The suppressive activity in this study belongs to the VAPB splice variant VAP-C; VAPA itself enhanced replication. Reason: The cited abstract states explicitly that VAP-C, a VAPB splice product, impaired HCV replication, whereas overexpression of VAP-A enhanced it. The same paper supports the opposite direction for VAPA (GO:0044829, kept). Host-mediated suppression of viral genome replication is therefore contradicted for VAPA by the source itself, and the IEA row repeats it. Supporting Evidence: PMID:19515777 Overexpression of VAP-C impaired the RNA replication of the HCV replicon and the propagation of the HCV JFH1 strain, whereas overexpression of VAP-A and VAP-B enhanced the replication. |
| GO:0044829 host-mediated activation of viral genome replication | IDA PMID:19515777 Human VAP-C negatively regulates hepatitis C virus propagati... | KEEP AS NON CORE | Summary: VAPA supports hepatitis C virus RNA replication as a host factor bound by NS5A/NS5B. Reason: VAPA binds HCV NS5B and NS5A and its overexpression enhances HCV replicon replication; the replication complex co-opts the ER-anchored adaptor. This is a real but non-core, virus-specific use of the host protein. Supporting Evidence: PMID:19515777 Overexpression of VAP-C impaired the RNA replication of the HCV replicon and the propagation of the HCV JFH1 strain, whereas overexpression of VAP-A and VAP-B enhanced the replication. |
| GO:0044829 host-mediated activation of viral genome replication | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: VAPA supports hepatitis C virus RNA replication as a host factor bound by NS5A/NS5B. Reason: VAPA binds HCV NS5B and NS5A and its overexpression enhances HCV replicon replication; the replication complex co-opts the ER-anchored adaptor. This is a real but non-core, virus-specific use of the host protein. Supporting Evidence: PMID:19515777 Overexpression of VAP-C impaired the RNA replication of the HCV replicon and the propagation of the HCV JFH1 strain, whereas overexpression of VAP-A and VAP-B enhanced the replication. |
| GO:0045296 cadherin binding | HDA PMID:25468996 E-cadherin interactome complexity and robustness resolved by... | KEEP AS NON CORE | Summary: Retain the proteomic cadherin-binding observation as non-core. Reason: The HDA source provides a curated association with cadherin complexes. This is compatible with junctional/adhesion contexts but does not establish a dedicated cadherin-binding core mechanism. |
| GO:0046982 protein heterodimerization activity | IPI PMID:16227268 Human VAP-B is involved in hepatitis C virus replication thr... | KEEP AS NON CORE | Summary: VAPA oligomerization supports assembly but is not the main functional description. Reason: VAPA forms homo- and VAPB heterodimers. Retain the interaction property while prioritizing FFAT recognition and membrane adaptor activity as the core molecular mechanism. Supporting Evidence: file:human/VAPA/VAPA-uniprot.txt Homodimer; disulfide-linked file:human/VAPA/VAPA-uniprot.txt Heterodimer with VAPB |
| GO:0046982 protein heterodimerization activity | IPI PMID:9920726 Molecular cloning and characterization of mammalian homologu... | KEEP AS NON CORE | Summary: VAPA oligomerization supports assembly but is not the main functional description. Reason: VAPA forms homo- and VAPB heterodimers. Retain the interaction property while prioritizing FFAT recognition and membrane adaptor activity as the core molecular mechanism. Supporting Evidence: file:human/VAPA/VAPA-uniprot.txt Homodimer; disulfide-linked file:human/VAPA/VAPA-uniprot.txt Heterodimer with VAPB |
| GO:0048471 perinuclear region of cytoplasm | IDA PMID:16895911 Efficient trafficking of ceramide from the endoplasmic retic... | KEEP AS NON CORE | Summary: Retain the ancillary localization without replacing the principal ER-membrane topology. Reason: The curated source reports this location or pathway-associated pool. VAPA has a cytosol-facing ER domain and peripheral/perinuclear membrane pools; such observations do not make the intact canonical protein a freely soluble cytosolic factor or establish an independent core function. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. |
| GO:0051893 regulation of focal adhesion assembly | IDA PMID:32234213 Calcium-stimulated disassembly of focal adhesions mediated b... | KEEP AS NON CORE | Summary: Focal-adhesion regulation is a context-specific consequence of VAPA-mediated contacts. Reason: OSBPL3/VAPA-dependent signaling and membrane recruitment connect VAPA to adhesion turnover. This role is supported, but remains a specialized cellular consequence of the membrane-adaptor function. Supporting Evidence: file:human/VAPA/VAPA-uniprot.txt The OSBPL3-VAPA complex CC stimulates RRAS signaling file:human/VAPA/VAPA-deep-research-falcon.md VAPA also stabilized ventral ERโplasma-membrane contacts adjacent to focal adhesions and supported microtubule-dependent adhesion disassembly. |
| GO:0061025 membrane fusion | TAS PMID:9657962 Identification of a human homologue of the vesicle-associate... | MARK AS OVER ANNOTATED | Summary: Membrane fusion was a speculative role inferred from VAMP binding; VAPA is a tether, not a fusion factor. Reason: The 1998 paper identified human VAP-33 by homology and VAMP binding and suggested possible roles in vesicle fusion. Two decades of later work characterize VAPA as an ER-anchored FFAT receptor that tethers membranes at contact sites without fusing them, and no experiment shows VAPA executing a fusion step. The TAS statement is retained as an over-annotation of historical interest rather than a supported process. Supporting Evidence: PMID:9657962 suggesting possible roles in vesicle fusion in both neuronal and non-neuronal cells |
| GO:0070971 endoplasmic reticulum exit site | IDA NOT PMID:18713837 FFAT rescues VAPA-mediated inhibition of ER-to-Golgi transpo... | ACCEPT | Summary: NOT annotation accepted: VAPA is not concentrated at ER exit sites. Reason: This is a negated localization. VAPA is distributed over the ER membrane and contact sites rather than concentrated at COPII-defined ER exit sites, and the curator recorded an explicit negative observation from this study. The negation is accepted. Supporting Evidence: PMID:18713837 Thus, overexpression of the two VAP isoforms causes retention of ER membrane proteins by impeding lateral diffusion and their incorporation into transport vesicles. |
| GO:0070972 protein localization to endoplasmic reticulum | IMP PMID:19289470 Promotion of neurite extension by protrudin requires its int... | ACCEPT | Summary: VAPA partner recruitment contributes to ER organization and membrane traffic. Reason: VAPA perturbation alters ER cargo segregation and membrane traffic, while FFAT-mediated interactions connect the ER to trafficking intermediates. The annotation captures the adaptor contribution rather than direct vesicle-coat or motor catalysis. Supporting Evidence: PMID:18713837 Overexpression of the wild-type A isoform (VAPA) but not the B isoform (VAPB), inhibited ER-to-Golgi transport of membrane proteins. |
| GO:0090114 COPII-coated vesicle budding | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: Inhibition of COPII budding by VAPA overexpression does not show that VAPA takes part in COPII vesicle budding. Reason: The IMP row rests on overexpression of wild-type VAPA, which sequesters cargo and blocks its incorporation into ER vesicles, an effect relieved by FFAT peptide. This is a dominant interference with budding, not evidence that endogenous VAPA performs any step of COPII coat assembly or vesicle scission. The IEA row restates the same inference. Both are marked as over-annotation rather than removed, because the observation is real. Supporting Evidence: PMID:18713837 Thus, overexpression of the two VAP isoforms causes retention of ER membrane proteins by impeding lateral diffusion and their incorporation into transport vesicles. |
| GO:0090114 COPII-coated vesicle budding | IMP PMID:18713837 FFAT rescues VAPA-mediated inhibition of ER-to-Golgi transpo... | MARK AS OVER ANNOTATED | Summary: Inhibition of COPII budding by VAPA overexpression does not show that VAPA takes part in COPII vesicle budding. Reason: The IMP row rests on overexpression of wild-type VAPA, which sequesters cargo and blocks its incorporation into ER vesicles, an effect relieved by FFAT peptide. This is a dominant interference with budding, not evidence that endogenous VAPA performs any step of COPII coat assembly or vesicle scission. The IEA row restates the same inference. Both are marked as over-annotation rather than removed, because the observation is real. Supporting Evidence: PMID:18713837 Thus, overexpression of the two VAP isoforms causes retention of ER membrane proteins by impeding lateral diffusion and their incorporation into transport vesicles. |
| GO:0098554 cytoplasmic side of endoplasmic reticulum membrane | IDA PMID:34688657 Intellectual-disability-associated mutations in the ceramide... | ACCEPT | Summary: ER membrane anchoring and contact-site residence are integral to VAPA function. Reason: The C-terminal membrane anchor places the MSP domain in the cytosol, where FFAT-bearing partners form membrane contacts. Structural, biochemical and cellular studies establish this topology. An ER-endosome contact annotation describes the tethering assembly rather than VAPA moving wholly onto the endosome. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. |
| GO:0140284 endoplasmic reticulum-endosome membrane contact site | IDA PMID:41741634 STARD3 regulates lysosome positioning and contacts via a GSK... | ACCEPT | Summary: ER membrane anchoring and contact-site residence are integral to VAPA function. Reason: The C-terminal membrane anchor places the MSP domain in the cytosol, where FFAT-bearing partners form membrane contacts. Structural, biochemical and cellular studies establish this topology. An ER-endosome contact annotation describes the tethering assembly rather than VAPA moving wholly onto the endosome. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. |
| GO:0160258 endoplasmic reticulum-trans-Golgi network membrane contact site | IDA PMID:34688657 Intellectual-disability-associated mutations in the ceramide... | ACCEPT | Summary: The ERโGolgi contact role is established, while Golgi-side residence needs topological care. Reason: OSBP binds VAPA at the ER and Golgi phosphoinositides through its PH domain. A contact-site localization is mechanistically sound; a broad Golgi-membrane observation is retained as non-core without claiming that the canonical VAPA membrane anchor is inserted into Golgi rather than ER. Supporting Evidence: PMID:24209621 a FFAT motif that interacts with the ER protein VAP-A, and a lipid transfer domain. |
| GO:0160258 endoplasmic reticulum-trans-Golgi network membrane contact site | IDA PMID:39106189 The ORP9-ORP11 dimer promotes sphingomyelin synthesis. | ACCEPT | Summary: The ERโGolgi contact role is established, while Golgi-side residence needs topological care. Reason: OSBP binds VAPA at the ER and Golgi phosphoinositides through its PH domain. A contact-site localization is mechanistically sound; a broad Golgi-membrane observation is retained as non-core without claiming that the canonical VAPA membrane anchor is inserted into Golgi rather than ER. Supporting Evidence: PMID:24209621 a FFAT motif that interacts with the ER protein VAP-A, and a lipid transfer domain. |
| GO:0170016 endoplasmic reticulum-endosome tether activity | IDA PMID:33124732 FFAT motif phosphorylation controls formation and lipid tran... | ACCEPT | Summary: VAPA anchors partner proteins and tethers the ER to opposing membranes. Reason: Direct FFAT recognition and reconstituted/cellular contact-site experiments support protein-membrane adaptor and ER-endosome tether activity. VAPA supplies the ER anchor; associated lipid-transfer proteins provide cargo transfer. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. PMID:33124732 The FFAT of ORP1 efficiently pulled down VAPโA and VAPโB from the whole cell protein extract |
| GO:0170016 endoplasmic reticulum-endosome tether activity | IDA PMID:41741634 STARD3 regulates lysosome positioning and contacts via a GSK... | ACCEPT | Summary: VAPA anchors partner proteins and tethers the ER to opposing membranes. Reason: Direct FFAT recognition and reconstituted/cellular contact-site experiments support protein-membrane adaptor and ER-endosome tether activity. VAPA supplies the ER anchor; associated lipid-transfer proteins provide cargo transfer. Supporting Evidence: PMID:33124732 VAPโA, VAPโB, and MOSPD2 are anchored in the ER membrane by a carboxylโterminal transmembrane domain with their MSP domain projecting into the cytosol. PMID:33124732 The FFAT of ORP1 efficiently pulled down VAPโA and VAPโB from the whole cell protein extract |
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Download this section (compressed HTML)Q: GO:0160214 endoplasmic reticulum-plasma membrane adaptor activity is defined as bringing the plasma membrane and ER membrane together "via membrane lipid binding". At VAPA-dependent ER-PM contacts the plasma-membrane lipid binding is performed by the FFAT partner (for example the ORP3 PH domain binding PI(4,5)P2), while VAPA contributes the ER-anchored FFAT receptor, a role already captured by GO:0043495 protein-membrane adaptor activity. PomBase nevertheless annotates the fission yeast VAP orthologs scs2 and scs22 to GO:0160214 (IDA/IMP/EXP), and human VAPB carries GO:0160214 both as a UniProt ISS annotation and as the molecular-function node of a production GO-CAM (gomodel:68fac5ed00002250, PITPNM1 at ER-PM contacts). In contrast, the production GO-CAM gomodel:682fbcd000003765, curated from PMID:32234213 (the ORP3 ER-PM contact paper), types VAPA as GO:0043495 protein-membrane adaptor activity occurring in the ER membrane, with the ER-PM contact site placed on the partner nodes. Should GO:0160214 cover ER-anchored FFAT receptors whose plasma-membrane contact is made by a partner protein, or only molecules that themselves bind plasma-membrane lipids (E-Syts, tricalbins, GRAMD2A)? VAPA is not annotated to GO:0160214 in this review pending that clarification.
Suggested experts: Casanova JE
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