VAPA

Existing Annotations Review

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 ER–Golgi 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...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:10544080 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:10544080 Hepatitis C virus RNA polymerase and NS5A complex with a SNA...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:10544080 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:16227268 Human VAP-B is involved in hepatitis C virus replication thr...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:16227268 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:16227268 Human VAP-B is involved in hepatitis C virus replication thr...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:16227268 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:16227268 Human VAP-B is involved in hepatitis C virus replication thr...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:16227268 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:16227268 Human VAP-B is involved in hepatitis C virus replication thr...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:16227268 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:16227268 Human VAP-B is involved in hepatitis C virus replication thr...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:16227268 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:16895911 Efficient trafficking of ceramide from the endoplasmic retic...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:16895911 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:16996479 Subproteomic study of hepatitis C virus replicon reveals Ras...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:16996479 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:18160438 Human butyrate-induced transcript 1 interacts with hepatitis...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:18160438 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:19289470 Promotion of neurite extension by protrudin requires its int...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:19289470 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:19515777 Human VAP-C negatively regulates hepatitis C virus propagati...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:19515777 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:19515777 Human VAP-C negatively regulates hepatitis C virus propagati...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:19515777 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:19515777 Human VAP-C negatively regulates hepatitis C virus propagati...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:19515777 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:19615732 Defining the human deubiquitinating enzyme interaction lands...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:19615732 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:20029029 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:21900206 A directed protein interaction network for investigating int...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:21900206 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:21957124 Viperin inhibits hepatitis C virus replication by interferin...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:21957124 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:21957124 Viperin inhibits hepatitis C virus replication by interferin...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:21957124 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:21957124 Viperin inhibits hepatitis C virus replication by interferin...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:21957124 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:21976701 Protrudin serves as an adaptor molecule that connects KIF5 a...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:21976701 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:21976701 Protrudin serves as an adaptor molecule that connects KIF5 a...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:21976701 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:22045669 The antiviral protein viperin inhibits hepatitis C virus rep...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:22045669 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:23736259 The ALS8 protein VAPB interacts with the ER-Golgi recycling ...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:23736259 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:23840749 MOR is not enough: identification of novel mu-opioid recepto...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:23840749 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:23935497 Rab18 binds to hepatitis C virus NS5A and promotes interacti...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:23935497 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:24105263 STARD3 or STARD3NL and VAP form a novel molecular tether bet...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:24105263 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:24209621 A four-step cycle driven by PI(4)P hydrolysis directs sterol...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:24209621 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:25616068 A combined proteomics/genomics approach links hepatitis C vi...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:25616068 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:25616068 A combined proteomics/genomics approach links hepatitis C vi...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:25616068 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:25681634 Sterol liganding of OSBP-related proteins (ORPs) regulates t...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:25681634 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:25681634 Sterol liganding of OSBP-related proteins (ORPs) regulates t...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:25681634 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:25910212 Widespread macromolecular interaction perturbations in human...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:25910212 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:26496610 A human interactome in three quantitative dimensions organiz...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:26496610 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:26496610 A human interactome in three quantitative dimensions organiz...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:26496610 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:26496610 A human interactome in three quantitative dimensions organiz...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:26496610 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:26496610 A human interactome in three quantitative dimensions organiz...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:26496610 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:26618866 ∆F508 CFTR interactome remodelling promotes rescue of cystic...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:26618866 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:28298427 Systematic protein-protein interaction mapping for clinicall...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:28298427 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:28377464 STARD3 mediates endoplasmic reticulum-to-endosome cholestero...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:28377464 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:29858488 Identification of MOSPD2, a novel scaffold for endoplasmic r...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:29858488 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:29997244 LuTHy: a double-readout bioluminescence-based two-hybrid tec...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:29997244 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:30659099 The activity of Sac1 across ER-TGN contact sites requires th...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:30659099 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:30659099 The activity of Sac1 across ER-TGN contact sites requires th...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:30659099 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:30741634 Human VPS13A is associated with multiple organelles and infl...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:30741634 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:31980649 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32296183 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32344433 GRAF2, WDR44, and MICAL1 mediate Rab8/10/11-dependent export...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32344433 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:32814053 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:33124732 FFAT motif phosphorylation controls formation and lipid tran...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:33124732 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:33124732 FFAT motif phosphorylation controls formation and lipid tran...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:33124732 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:33961781 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:33961781 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:33961781 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:33961781 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:33961781 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:33961781 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:33961781 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:33961781 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:35156780 CFTR interactome mapping using the mammalian membrane two-hy...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:35156780 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:35271311 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:35271311 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:35271311 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:35271311 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:35271311 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:35271311 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:35271311 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:35384245 Physical and functional interactome atlas of human receptor ...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:35384245 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:36012204 Differential CFTR-Interactome Proximity Labeling Procedures ...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:36012204 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:40205054 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:40205054 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:40205054 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:40205054 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction alone.
GO:0005515 protein binding	IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func...	KEEP AS NON CORE	Summary: Retain the curated interaction as a non-core binding observation. Reason: The IPI observation from PMID:40205054 records an interaction with the listed partner. VAPA's core function is FFAT-dependent membrane recruitment and tethering; generic protein binding does not establish that every partner uses that mechanism or that each interaction defines an additional physiological role. The observation is retained without inferring function from interaction 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal 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...	ACCEPT	Summary: VAPA participates in ceramide trafficking and sphingomyelin production through lipid-transfer-protein recruitment. Reason: The VAPA–OSBP 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:0006686 sphingomyelin biosynthetic process	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 VAPA–OSBP 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:0006888 endoplasmic reticulum to Golgi vesicle-mediated transport	IDA PMID:41856286 Glycolipid transfer protein modulates vesicular trafficking ...	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:0006888 endoplasmic reticulum to Golgi vesicle-mediated transport	IMP PMID:18713837 FFAT rescues VAPA-mediated inhibition of ER-to-Golgi transpo...	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:0007029 endoplasmic reticulum organization	IMP NOT PMID:18713837 FFAT rescues VAPA-mediated inhibition of ER-to-Golgi transpo...	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: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 direction and viral-system specificity require the complete cited infection study. Reason: VAPA interacts with viral replication machinery, but both activation and suppression annotations occur with the same PMID. A generic virus interaction cannot resolve directionality, host/virus context or whether the measured step is genome replication versus release. The full experiment is needed; neither opposite term is automatically removed.
GO:0019076 viral release from host cell	IEA GO_REF:0000117	UNDECIDED	Summary: The direction and viral-system specificity require the complete cited infection study. Reason: VAPA interacts with viral replication machinery, but both activation and suppression annotations occur with the same PMID. A generic virus interaction cannot resolve directionality, host/virus context or whether the measured step is genome replication versus release. The full experiment is needed; neither opposite term is automatically removed.
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 mediated by the FFAT recognition surface of the MSP domain; the specific FFAT motif term captures this directly demonstrated mechanism. Proposed replacements: FFAT motif binding Supporting Evidence: PMID:33124732 The FFAT of ORP1 efficiently pulled down VAP‐A and VAP‐B from the whole cell protein extract
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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal 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...	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: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 VAP‐A and VAP‐B 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 VAP‐A and VAP‐B 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 VAP‐A and VAP‐B 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...	UNDECIDED	Summary: A direct protein-folding role is not established by the inspected trafficking evidence. Reason: The cited experiment describes ER-to-Golgi traffic and VAP-dependent ER organization. Such perturbations can affect handling of misfolded cargo without showing that VAPA performs or directly participates in protein folding. The complete relevant experimental context is needed before accepting or rejecting this process assignment.
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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal 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 VAPA–OSBP 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 VAPA–OSBP 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...	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: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...	UNDECIDED	Summary: The high-throughput NF-kappaB phenotype requires mechanistic assessment. Reason: A screen phenotype alone does not establish direct participation in canonical NF-kappaB activation. The relevant gene-specific assay and relationship to the ER-adaptor role have not been resolved, so this row remains undecided.
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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal transmembrane domain with their MSP domain projecting into the cytosol. PMID:33124732 The FFAT of ORP1 efficiently pulled down VAP‐A and VAP‐B from the whole cell protein extract
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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal transmembrane domain with their MSP domain projecting into the cytosol. PMID:33124732 The FFAT of ORP1 efficiently pulled down VAP‐A and VAP‐B 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal transmembrane domain with their MSP domain projecting into the cytosol. PMID:33124732 The FFAT of ORP1 efficiently pulled down VAP‐A and VAP‐B 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal transmembrane domain with their MSP domain projecting into the cytosol. PMID:33124732 The FFAT of ORP1 efficiently pulled down VAP‐A and VAP‐B 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal transmembrane domain with their MSP domain projecting into the cytosol. PMID:33124732 The FFAT of ORP1 efficiently pulled down VAP‐A and VAP‐B 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal transmembrane domain with their MSP domain projecting into the cytosol. PMID:33124732 The FFAT of ORP1 efficiently pulled down VAP‐A and VAP‐B 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...	UNDECIDED	Summary: The direction and viral-system specificity require the complete cited infection study. Reason: VAPA interacts with viral replication machinery, but both activation and suppression annotations occur with the same PMID. A generic virus interaction cannot resolve directionality, host/virus context or whether the measured step is genome replication versus release. The full experiment is needed; neither opposite term is automatically removed.
GO:0044828 host-mediated suppression of viral genome replication	IEA GO_REF:0000117	UNDECIDED	Summary: The direction and viral-system specificity require the complete cited infection study. Reason: VAPA interacts with viral replication machinery, but both activation and suppression annotations occur with the same PMID. A generic virus interaction cannot resolve directionality, host/virus context or whether the measured step is genome replication versus release. The full experiment is needed; neither opposite term is automatically removed.
GO:0044829 host-mediated activation of viral genome replication	IDA PMID:19515777 Human VAP-C negatively regulates hepatitis C virus propagati...	UNDECIDED	Summary: The direction and viral-system specificity require the complete cited infection study. Reason: VAPA interacts with viral replication machinery, but both activation and suppression annotations occur with the same PMID. A generic virus interaction cannot resolve directionality, host/virus context or whether the measured step is genome replication versus release. The full experiment is needed; neither opposite term is automatically removed.
GO:0044829 host-mediated activation of viral genome replication	IEA GO_REF:0000117	UNDECIDED	Summary: The direction and viral-system specificity require the complete cited infection study. Reason: VAPA interacts with viral replication machinery, but both activation and suppression annotations occur with the same PMID. A generic virus interaction cannot resolve directionality, host/virus context or whether the measured step is genome replication versus release. The full experiment is needed; neither opposite term is automatically removed.
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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal 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
GO:0061025 membrane fusion	TAS PMID:9657962 Identification of a human homologue of the vesicle-associate...	UNDECIDED	Summary: SNARE association does not by itself establish membrane fusion activity or participation. Reason: VAPA was identified through SNARE-associated interactions, but its established tethering contacts do not fuse membranes. The complete early study must be inspected to decide whether a distinct fusion-process contribution is supported; contact-site tethering alone is insufficient.
GO:0070971 endoplasmic reticulum exit site	IDA NOT PMID:18713837 FFAT rescues VAPA-mediated inhibition of ER-to-Golgi transpo...	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: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	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	IMP PMID:18713837 FFAT rescues VAPA-mediated inhibition of ER-to-Golgi transpo...	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: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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal 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 ER–Golgi 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 ER–Golgi 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal transmembrane domain with their MSP domain projecting into the cytosol. PMID:33124732 The FFAT of ORP1 efficiently pulled down VAP‐A and VAP‐B 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 VAP‐A, VAP‐B, and MOSPD2 are anchored in the ER membrane by a carboxyl‐terminal transmembrane domain with their MSP domain projecting into the cytosol. PMID:33124732 The FFAT of ORP1 efficiently pulled down VAP‐A and VAP‐B from the whole cell protein extract

Gene Description

Existing Annotations Review

Core Functions

Tail-anchored ER adaptor that recognizes FFAT-bearing proteins to organize lipid-transfer and trafficking membrane contacts.

Specific recognition of conventional and phosphorylated FFAT motifs by the MSP domain.

References

Suggested Questions for Experts

Deep Research

Falcon

📚 Additional Documentation

Notes

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