APOA2
Gene Ontology Biological Process
- cellular lipid metabolic process [TAS]
- cholesterol efflux [IDA]
- cholesterol homeostasis [IDA]
- diacylglycerol catabolic process [IDA]
- high-density lipoprotein particle assembly [IDA]
- high-density lipoprotein particle clearance [IDA]
- high-density lipoprotein particle remodeling [IDA]
- lipoprotein metabolic process [TAS]
- low-density lipoprotein particle remodeling [IDA]
- negative regulation of cholesterol import [IDA]
- negative regulation of cholesterol transport [IMP]
- negative regulation of cholesterol transporter activity [IDA]
- negative regulation of cytokine secretion involved in immune response [IDA]
- negative regulation of lipase activity [IDA]
- negative regulation of lipid catabolic process [IDA]
- negative regulation of very-low-density lipoprotein particle remodeling [IDA]
- peptidyl-methionine modification [IDA]
- phosphatidylcholine biosynthetic process [IDA]
- phospholipid catabolic process [IDA]
- phospholipid efflux [IDA]
- phototransduction, visible light [TAS]
- positive regulation of catalytic activity [IDA]
- positive regulation of cholesterol esterification [IDA]
- positive regulation of interleukin-8 biosynthetic process [IDA]
- positive regulation of lipid catabolic process [IDA]
- protein folding [IDA]
- protein oxidation [IDA]
- regulation of protein stability [IDA]
- response to glucose [IDA]
- retinoid metabolic process [TAS]
- reverse cholesterol transport [IDA]
- small molecule metabolic process [TAS]
- triglyceride metabolic process [TAS]
- triglyceride-rich lipoprotein particle remodeling [IDA]
Gene Ontology Molecular Function- apolipoprotein receptor binding [IPI]
- cholesterol binding [IDA]
- cholesterol transporter activity [IDA]
- high-density lipoprotein particle receptor binding [IPI]
- lipase inhibitor activity [IDA]
- lipid binding [IDA]
- lipid transporter activity [IDA]
- phosphatidylcholine binding [IDA]
- phosphatidylcholine-sterol O-acyltransferase activator activity [IDA]
- phospholipid binding [IDA]
- protein binding [IPI]
- protein heterodimerization activity [IPI]
- protein homodimerization activity [IDA]
- apolipoprotein receptor binding [IPI]
- cholesterol binding [IDA]
- cholesterol transporter activity [IDA]
- high-density lipoprotein particle receptor binding [IPI]
- lipase inhibitor activity [IDA]
- lipid binding [IDA]
- lipid transporter activity [IDA]
- phosphatidylcholine binding [IDA]
- phosphatidylcholine-sterol O-acyltransferase activator activity [IDA]
- phospholipid binding [IDA]
- protein binding [IPI]
- protein heterodimerization activity [IPI]
- protein homodimerization activity [IDA]
Gene Ontology Cellular Component
- blood microparticle [IDA]
- chylomicron [IDA]
- cytosol [TAS]
- early endosome [TAS]
- endoplasmic reticulum lumen [TAS]
- extracellular region [NAS, TAS]
- extracellular vesicular exosome [IDA]
- high-density lipoprotein particle [IDA]
- spherical high-density lipoprotein particle [IDA]
- very-low-density lipoprotein particle [IDA]
APOA1
Gene Ontology Biological Process
- ERK1 and ERK2 cascade [IDA]
- G-protein coupled receptor signaling pathway [IDA]
- blood coagulation [TAS]
- cellular lipid metabolic process [TAS]
- cholesterol efflux [IDA]
- cholesterol homeostasis [IDA, IMP]
- cholesterol import [IMP]
- cholesterol metabolic process [IMP]
- cholesterol transport [IDA]
- high-density lipoprotein particle assembly [IDA]
- high-density lipoprotein particle clearance [IC]
- high-density lipoprotein particle remodeling [IC]
- integrin-mediated signaling pathway [IDA]
- lipoprotein metabolic process [TAS]
- negative chemotaxis [IDA]
- negative regulation of cell adhesion molecule production [IDA]
- negative regulation of cytokine secretion involved in immune response [IDA]
- negative regulation of heterotypic cell-cell adhesion [IDA]
- negative regulation of inflammatory response [IDA]
- negative regulation of interleukin-1 beta secretion [IDA]
- negative regulation of response to cytokine stimulus [IDA]
- negative regulation of tumor necrosis factor-mediated signaling pathway [IDA]
- negative regulation of very-low-density lipoprotein particle remodeling [IDA]
- peptidyl-methionine modification [IDA]
- phosphatidylcholine biosynthetic process [IDA]
- phospholipid efflux [IDA]
- phospholipid homeostasis [IDA]
- phototransduction, visible light [TAS]
- platelet activation [TAS]
- platelet degranulation [TAS]
- positive regulation of Rho protein signal transduction [IDA]
- positive regulation of cholesterol esterification [IDA]
- positive regulation of hydrolase activity [IDA]
- positive regulation of stress fiber assembly [IDA]
- positive regulation of substrate adhesion-dependent cell spreading [IDA]
- protein oxidation [IDA]
- protein stabilization [IDA]
- regulation of Cdc42 protein signal transduction [IDA]
- retinoid metabolic process [TAS]
- reverse cholesterol transport [IMP]
- small molecule metabolic process [TAS]
- transforming growth factor beta receptor signaling pathway [IDA]
- transmembrane transport [TAS]
- triglyceride homeostasis [IDA]
Gene Ontology Molecular Function- apolipoprotein A-I receptor binding [IPI]
- apolipoprotein receptor binding [IPI]
- beta-amyloid binding [IDA]
- chemorepellent activity [IDA]
- cholesterol binding [IDA]
- cholesterol transporter activity [IDA, IMP]
- enzyme binding [IPI]
- high-density lipoprotein particle receptor binding [IPI]
- identical protein binding [IPI]
- phosphatidylcholine-sterol O-acyltransferase activator activity [IDA]
- phospholipid binding [IDA]
- protein binding [IPI]
- apolipoprotein A-I receptor binding [IPI]
- apolipoprotein receptor binding [IPI]
- beta-amyloid binding [IDA]
- chemorepellent activity [IDA]
- cholesterol binding [IDA]
- cholesterol transporter activity [IDA, IMP]
- enzyme binding [IPI]
- high-density lipoprotein particle receptor binding [IPI]
- identical protein binding [IPI]
- phosphatidylcholine-sterol O-acyltransferase activator activity [IDA]
- phospholipid binding [IDA]
- protein binding [IPI]
Gene Ontology Cellular Component
- blood microparticle [IDA]
- cytoplasmic vesicle [IDA]
- cytosol [TAS]
- early endosome [TAS]
- endocytic vesicle [IDA]
- endocytic vesicle lumen [TAS]
- endoplasmic reticulum lumen [TAS]
- extracellular region [TAS]
- extracellular space [IDA, ISS]
- extracellular vesicular exosome [IDA]
- high-density lipoprotein particle [IDA]
- plasma membrane [TAS]
- secretory granule lumen [TAS]
- spherical high-density lipoprotein particle [IDA]
- very-low-density lipoprotein particle [IDA]
- vesicle [IDA]
Reconstituted Complex
An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.
Publication
Formation of spherical, reconstituted high density lipoproteins containing both apolipoproteins A-I and A-II is mediated by lecithin:cholesterol acyltransferase.
Previous studies have provided detailed information on the formation of spherical high density lipoproteins (HDL) containing apolipoprotein (apo) A-I but no apoA-II (A-I HDL) by an lecithin:cholesterol acyltransferase (LCAT)-mediated process. In this study we have investigated the formation of spherical HDL containing both apoA-I and apoA-II (A-I/A-II HDL). Incubations were carried out containing discoidal A-I reconstituted HDL (rHDL), discoidal A-II ... [more]
Throughput
- Low Throughput
Additional Notes
- found in reconstituted HDL particles; association increases when particles formed in the presence of LCAT
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| APOA2 APOA1 | Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods. | High | 13.4392 | BioGRID | 2950041 | |
| APOA1 APOA2 | Co-purification Co-purification An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps. | Low | - | BioGRID | 853065 | |
| APOA2 APOA1 | Cross-Linking-MS (XL-MS) Cross-Linking-MS (XL-MS) An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071). | High | - | BioGRID | 3724070 | |
| APOA1 APOA2 | Cross-Linking-MS (XL-MS) Cross-Linking-MS (XL-MS) An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071). | High | - | BioGRID | 3724012 | |
| APOA1 APOA2 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | 853039 |
Curated By
- BioGRID