node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AHSP | CYB5R3 | ENSP00000307199 | ENSP00000354468 | alpha hemoglobin stabilizing protein; Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia | cytochrome b5 reductase 3 | 0.720 |
AHSP | FKBP1A | ENSP00000307199 | ENSP00000371138 | alpha hemoglobin stabilizing protein; Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia | FK506 binding protein 1A, 12kDa; Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruites SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | 0.576 |
AHSP | HBA1 | ENSP00000307199 | ENSP00000322421 | alpha hemoglobin stabilizing protein; Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia | hemoglobin, alpha 1; Involved in oxygen transport from the lung to the various peripheral tissues (By similarity) | 0.973 |
AHSP | HBA2 | ENSP00000307199 | ENSP00000251595 | alpha hemoglobin stabilizing protein; Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia | hemoglobin, alpha 2 | 0.996 |
AHSP | HBB | ENSP00000307199 | ENSP00000333994 | alpha hemoglobin stabilizing protein; Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia | hemoglobin, beta | 0.951 |
AHSP | HBD | ENSP00000307199 | ENSP00000369654 | alpha hemoglobin stabilizing protein; Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia | hemoglobin, delta; Involved in oxygen transport from the lung to the various peripheral tissues | 0.858 |
AHSP | HBE1 | ENSP00000307199 | ENSP00000292896 | alpha hemoglobin stabilizing protein; Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia | hemoglobin, epsilon 1; The epsilon chain is a beta-type chain of early mammalian embryonic hemoglobin | 0.907 |
AHSP | HBG1 | ENSP00000307199 | ENSP00000327431 | alpha hemoglobin stabilizing protein; Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia | hemoglobin, gamma A; Gamma chains make up the fetal hemoglobin F, in combination with alpha chains | 0.454 |
AHSP | HBG2 | ENSP00000307199 | ENSP00000338082 | alpha hemoglobin stabilizing protein; Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia | hemoglobin, gamma G; Gamma chains make up the fetal hemoglobin F, in combination with alpha chains | 0.510 |
AHSP | HBQ1 | ENSP00000307199 | ENSP00000199708 | alpha hemoglobin stabilizing protein; Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia | hemoglobin, theta 1 | 0.771 |
AHSP | HBZ | ENSP00000307199 | ENSP00000252951 | alpha hemoglobin stabilizing protein; Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia | hemoglobin, zeta; The zeta chain is an alpha-type chain of mammalian embryonic hemoglobin, synthesized primarily in the yolk sac | 0.748 |
AHSP | UBE3A | ENSP00000307199 | ENSP00000381045 | alpha hemoglobin stabilizing protein; Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia | ubiquitin protein ligase E3A | 0.499 |
AHSP | ZC3H12A | ENSP00000307199 | ENSP00000362174 | alpha hemoglobin stabilizing protein; Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia | zinc finger CCCH-type containing 12A; Has RNase activity and selectively degrades specific target mRNA species. Modulates the immune response and inflammation by regulating the decay of specific mRNA molecules. Recognizes the 3’-untranslated region (UTR) of the mRNA for IL6, CALCR and IL12B. Required for normal decay of IL6 mRNA (By similarity). Triggers apoptosis and promotes angiogenesis in response to the binding of CCL2 to CCR2. Regulates expression of CDH12 and CHD19 | 0.771 |
CYB5R3 | AHSP | ENSP00000354468 | ENSP00000307199 | cytochrome b5 reductase 3 | alpha hemoglobin stabilizing protein; Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia | 0.720 |
CYB5R3 | HBA1 | ENSP00000354468 | ENSP00000322421 | cytochrome b5 reductase 3 | hemoglobin, alpha 1; Involved in oxygen transport from the lung to the various peripheral tissues (By similarity) | 0.887 |
CYB5R3 | HBA2 | ENSP00000354468 | ENSP00000251595 | cytochrome b5 reductase 3 | hemoglobin, alpha 2 | 0.899 |
CYB5R3 | HBB | ENSP00000354468 | ENSP00000333994 | cytochrome b5 reductase 3 | hemoglobin, beta | 0.841 |
CYB5R3 | HBD | ENSP00000354468 | ENSP00000369654 | cytochrome b5 reductase 3 | hemoglobin, delta; Involved in oxygen transport from the lung to the various peripheral tissues | 0.846 |
CYB5R3 | HBE1 | ENSP00000354468 | ENSP00000292896 | cytochrome b5 reductase 3 | hemoglobin, epsilon 1; The epsilon chain is a beta-type chain of early mammalian embryonic hemoglobin | 0.762 |
CYB5R3 | HBG1 | ENSP00000354468 | ENSP00000327431 | cytochrome b5 reductase 3 | hemoglobin, gamma A; Gamma chains make up the fetal hemoglobin F, in combination with alpha chains | 0.456 |