| S.NO | Uniprot ID | Protein Name | Sequence Length | HRM Repeats region | Function |
| 1 | P53701 | Cytochrome c-type heme lyase | 268 | Links covalently the heme group to the apoprotein of cytochrome c | |
| 2 | P30519 | Heme oxygenase 2 | 316 | "Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin Biliverdin is subsequently converted to bilirubin by biliverdin reductase Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter" | |
| 3 | Q9BQI3 | Eukaryotic translation initiation factor 2-alpha kinase 1 | 630 | "Inhibits protein synthesis at the translation initiation level, in response to various stress conditions, including oxidative stress, heme deficiency, osmotic shock and heat shock Exerts its function through the phosphorylation of EIF2S1 at 'Ser-48' and 'Ser-51', thus preventing its recycling Binds hemin forming a 1:1 complex through a cysteine thiolate and histidine nitrogenous coordination This binding occurs with moderate affinity, allowing it to sense the heme concentration within the cell Thanks to this unique heme-sensing capacity, plays a crucial role to shut off protein synthesis during acute heme-deficient conditions In red blood cells (RBCs), controls hemoglobin synthesis ensuring a coordinated regulation of the synthesis of its heme and globin moieties Thus plays an essential protective role for RBC survival in anemias of iron deficiency Similarly, in hepatocytes, involved in heme-mediated translational control of CYP2B and CYP3A and possibly other hepatic P450 cytochromes May also contain ER stress during acute heme-deficient conditions (By similarity)" |