Search Results
Overview
| Uniprot ID | P02760 |
|---|---|
| Protein Name | Protein AMBP |
| Gene Name | AMBP |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 100 | ETSGAYEKTDTDGKF |
| 106 | EKTDTDGKFLYHKSK |
| 111 | DGKFLYHKSKWNITM |
| 149 | HGPTITAKLYGRAPQ |
| 88 | MTSTRWRKGVCEETS |
Function
Antioxidant and tissue repair protein with reductase, heme-binding and radical-scavenging activities. Removes and protects against harmful oxidants and repairs macromolecules in intravascular and extravascular spaces and in intracellular compartments (PubMed:11877257, PubMed:15683711, PubMed:22096585, PubMed:23157686, PubMed:23642167, PubMed:25698971, PubMed:32092412, PubMed:32823731). Intravascularly, plays a regulatory role in red cell homeostasis by preventing heme- and reactive oxygen species-induced cell damage. Binds and degrades free heme to protect fetal and adult red blood cells from hemolysis (PubMed:11877257, PubMed:32092412). Reduces extracellular methemoglobin, a Fe3+ (ferric) form of hemoglobin that cannot bind oxygen, back to the Fe2+ (ferrous) form deoxyhemoglobin, which has oxygen-carrying potential (PubMed:15683711). Upon acute inflammation, inhibits oxidation of low-density lipoprotein particles by MPO and limits vascular damage (PubMed:25698971). Extravascularly, protects from oxidation products formed on extracellular matrix structures and cell membranes. Catalyzes the reduction of carbonyl groups on oxidized collagen fibers and preserves cellular and extracellular matrix ultrastructures (PubMed:22096585, PubMed:23642167). Importantly, counteracts the oxidative damage at blood-placenta interface, preventing leakage of free fetal hemoglobin into the maternal circulation (PubMed:21356557). Intracellularly, has a role in maintaining mitochondrial redox homeostasis. Bound to complex I of the respiratory chain of mitochondria, may scavenge free radicals and preserve mitochondrial ATP synthesis. Protects renal tubule epithelial cells from heme-induced oxidative damage to mitochondria (PubMed:23157686, PubMed:32823731). Reduces cytochrome c from Fe3+ (ferric) to the Fe2+ (ferrous) state through formation of superoxide anion radicals in the presence of ascorbate or NADH/NADPH electron donor cofactors, ascorbate being the preferred cofactor (PubMed:15683711). Has a chaperone role in facilitating the correct folding of bikunin in the endoplasmic reticulum compartment (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0072562 | blood microparticle |
| Molecular Function | GO:0019855 | calcium channel inhibitor activity |
| Molecular Function | GO:0046904 | calcium oxalate binding |
| Molecular Function | GO:0030246 | carbohydrate binding |
| Molecular Function | GO:0020037 | heme binding |
| Molecular Function | GO:0019862 | IgA binding |
| Molecular Function | GO:0016491 | oxidoreductase activity |
| Molecular Function | GO:0042803 | protein homodimerization activity |
| Molecular Function | GO:0004867 | serine-type endopeptidase inhibitor activity |
| Biological Process | GO:0007155 | cell adhesion |
| Biological Process | GO:0007565 | female pregnancy |
| Biological Process | GO:0042167 | heme catabolic process |
| Biological Process | GO:0050777 | negative regulation of immune response |
| Biological Process | GO:0046329 | negative regulation of JNK cascade |
| Biological Process | GO:0030163 | protein catabolic process |
| Cellular Component | GO:0009986 | cell surface |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0031012 | extracellular matrix |
| Cellular Component | GO:0005576 | extracellular region |
| Cellular Component | GO:0005615 | extracellular space |
| Cellular Component | GO:0005743 | mitochondrial inner membrane |
| Cellular Component | GO:0031965 | nuclear membrane |
| Cellular Component | GO:0005886 | plasma membrane |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.