APOD
Gene Ontology Biological Process
- aging [NAS]
- angiogenesis [NAS]
- brain development [ISS]
- glucose metabolic process [IDA]
- lipid metabolic process [IDA]
- lipid transport [NAS]
- negative regulation of T cell migration [IDA]
- negative regulation of cytokine production involved in inflammatory response [IDA]
- negative regulation of focal adhesion assembly [IMP]
- negative regulation of lipoprotein lipid oxidation [IDA]
- negative regulation of monocyte chemotactic protein-1 production [IDA]
- negative regulation of platelet-derived growth factor receptor signaling pathway [IDA]
- negative regulation of protein import into nucleus [IDA]
- negative regulation of smooth muscle cell proliferation [IDA]
- negative regulation of smooth muscle cell-matrix adhesion [IMP]
- peripheral nervous system axon regeneration [ISS]
- response to axon injury [ISS]
- response to drug [ISS]
- response to reactive oxygen species [IDA]
- tissue regeneration [ISS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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]
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.
Publication
Structure of human apolipoprotein D: locations of the intermolecular and intramolecular disulfide links.
We have determined the primary structure of human apolipoprotein D (apoD) by aligning peptides derived from digestions by cyanogen bromide, trypsin, and chymotrypsin. Our results confirm the primary structure derived from cDNA [Drayna et al. (1986) J. Biol. Chem. 261, 16535-16539]. ApoD consists of 169 amino acid residues, including 5 cysteines. Tryptic peptide analysis indicated that Cys41 and Cys16 are ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| APOA2 APOD | 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 | 853069 | |
| APOA2 APOD | 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 | 3724041 | |
| APOD 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 | 3724061 |
Curated By
- BioGRID