node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ATL18 | ERD14 | Q9SZL4 | P42763 | RING-H2 finger protein ATL18; Belongs to the RING-type zinc finger family. ATL subfamily. | Dehydrin ERD14; Intrinsically disordered protein acting as a chaperone. Prevents heat-induced aggregation and/or inactivation of various substrates. Binds to acidic phospholipid vesicles without affecting membrane fluidity. | 0.757 |
ATL18 | HIRD11 | Q9SZL4 | Q9SLJ2 | RING-H2 finger protein ATL18; Belongs to the RING-type zinc finger family. ATL subfamily. | Dehydrin HIRD11; Intrinsically disordered and metal-binding protein. Binds to the divalent cations cobalt, nickel, copper and zinc, but not to magnesium, calcium, manganese or cadmium. Binding to metal ions decreases disordered state, decreases susceptibility to trypsin and promotes self-association. Can reduce the formation of reactive oxygen species (ROS) in a copper-ascorbate in vitro system. Belongs to the KS-type dehydrin family. | 0.434 |
ATL18 | T22F8.30 | Q9SZL4 | Q9T022 | RING-H2 finger protein ATL18; Belongs to the RING-type zinc finger family. ATL subfamily. | Dehydrin family protein. | 0.899 |
ATL18 | XERO2 | Q9SZL4 | P42758 | RING-H2 finger protein ATL18; Belongs to the RING-type zinc finger family. ATL subfamily. | Dehydrin Xero 2; Belongs to the plant dehydrin family. | 0.759 |
ERD14 | ATL18 | P42763 | Q9SZL4 | Dehydrin ERD14; Intrinsically disordered protein acting as a chaperone. Prevents heat-induced aggregation and/or inactivation of various substrates. Binds to acidic phospholipid vesicles without affecting membrane fluidity. | RING-H2 finger protein ATL18; Belongs to the RING-type zinc finger family. ATL subfamily. | 0.757 |
ERD14 | HIRD11 | P42763 | Q9SLJ2 | Dehydrin ERD14; Intrinsically disordered protein acting as a chaperone. Prevents heat-induced aggregation and/or inactivation of various substrates. Binds to acidic phospholipid vesicles without affecting membrane fluidity. | Dehydrin HIRD11; Intrinsically disordered and metal-binding protein. Binds to the divalent cations cobalt, nickel, copper and zinc, but not to magnesium, calcium, manganese or cadmium. Binding to metal ions decreases disordered state, decreases susceptibility to trypsin and promotes self-association. Can reduce the formation of reactive oxygen species (ROS) in a copper-ascorbate in vitro system. Belongs to the KS-type dehydrin family. | 0.916 |
ERD14 | LEA2 | P42763 | Q9SRX6 | Dehydrin ERD14; Intrinsically disordered protein acting as a chaperone. Prevents heat-induced aggregation and/or inactivation of various substrates. Binds to acidic phospholipid vesicles without affecting membrane fluidity. | Late embryogenis abundant protein 2; Belongs to the LEA type 3 family. | 0.777 |
ERD14 | MENB | P42763 | Q8GYN9 | Dehydrin ERD14; Intrinsically disordered protein acting as a chaperone. Prevents heat-induced aggregation and/or inactivation of various substrates. Binds to acidic phospholipid vesicles without affecting membrane fluidity. | 1,4-dihydroxy-2-naphthoyl-CoA synthase, peroxisomal; Involved in the biosynthesis of phylloquinone (vitamin K1). Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl- CoA (DHNA-CoA) (By similarity). | 0.897 |
ERD14 | SRK2B | P42763 | Q9C958 | Dehydrin ERD14; Intrinsically disordered protein acting as a chaperone. Prevents heat-induced aggregation and/or inactivation of various substrates. Binds to acidic phospholipid vesicles without affecting membrane fluidity. | Serine/threonine-protein kinase SRK2B; Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. | 0.791 |
ERD14 | T22F8.30 | P42763 | Q9T022 | Dehydrin ERD14; Intrinsically disordered protein acting as a chaperone. Prevents heat-induced aggregation and/or inactivation of various substrates. Binds to acidic phospholipid vesicles without affecting membrane fluidity. | Dehydrin family protein. | 0.882 |
ERD14 | T23E18.11 | P42763 | A0A1P8ASI0 | Dehydrin ERD14; Intrinsically disordered protein acting as a chaperone. Prevents heat-induced aggregation and/or inactivation of various substrates. Binds to acidic phospholipid vesicles without affecting membrane fluidity. | 2-thiocytidine tRNA biosynthesis protein, TtcA. | 0.784 |
ERD14 | T28I24.15 | P42763 | Q9ZQ26 | Dehydrin ERD14; Intrinsically disordered protein acting as a chaperone. Prevents heat-induced aggregation and/or inactivation of various substrates. Binds to acidic phospholipid vesicles without affecting membrane fluidity. | DNA repair ATPase-like protein. | 0.718 |
ERD14 | T9L24.31 | P42763 | Q9FX44 | Dehydrin ERD14; Intrinsically disordered protein acting as a chaperone. Prevents heat-induced aggregation and/or inactivation of various substrates. Binds to acidic phospholipid vesicles without affecting membrane fluidity. | Uncharacterized protein T9L24.31. | 0.771 |
ERD14 | XERO2 | P42763 | P42758 | Dehydrin ERD14; Intrinsically disordered protein acting as a chaperone. Prevents heat-induced aggregation and/or inactivation of various substrates. Binds to acidic phospholipid vesicles without affecting membrane fluidity. | Dehydrin Xero 2; Belongs to the plant dehydrin family. | 0.926 |
HIRD11 | ATL18 | Q9SLJ2 | Q9SZL4 | Dehydrin HIRD11; Intrinsically disordered and metal-binding protein. Binds to the divalent cations cobalt, nickel, copper and zinc, but not to magnesium, calcium, manganese or cadmium. Binding to metal ions decreases disordered state, decreases susceptibility to trypsin and promotes self-association. Can reduce the formation of reactive oxygen species (ROS) in a copper-ascorbate in vitro system. Belongs to the KS-type dehydrin family. | RING-H2 finger protein ATL18; Belongs to the RING-type zinc finger family. ATL subfamily. | 0.434 |
HIRD11 | ERD14 | Q9SLJ2 | P42763 | Dehydrin HIRD11; Intrinsically disordered and metal-binding protein. Binds to the divalent cations cobalt, nickel, copper and zinc, but not to magnesium, calcium, manganese or cadmium. Binding to metal ions decreases disordered state, decreases susceptibility to trypsin and promotes self-association. Can reduce the formation of reactive oxygen species (ROS) in a copper-ascorbate in vitro system. Belongs to the KS-type dehydrin family. | Dehydrin ERD14; Intrinsically disordered protein acting as a chaperone. Prevents heat-induced aggregation and/or inactivation of various substrates. Binds to acidic phospholipid vesicles without affecting membrane fluidity. | 0.916 |
HIRD11 | LEA2 | Q9SLJ2 | Q9SRX6 | Dehydrin HIRD11; Intrinsically disordered and metal-binding protein. Binds to the divalent cations cobalt, nickel, copper and zinc, but not to magnesium, calcium, manganese or cadmium. Binding to metal ions decreases disordered state, decreases susceptibility to trypsin and promotes self-association. Can reduce the formation of reactive oxygen species (ROS) in a copper-ascorbate in vitro system. Belongs to the KS-type dehydrin family. | Late embryogenis abundant protein 2; Belongs to the LEA type 3 family. | 0.597 |
HIRD11 | MENB | Q9SLJ2 | Q8GYN9 | Dehydrin HIRD11; Intrinsically disordered and metal-binding protein. Binds to the divalent cations cobalt, nickel, copper and zinc, but not to magnesium, calcium, manganese or cadmium. Binding to metal ions decreases disordered state, decreases susceptibility to trypsin and promotes self-association. Can reduce the formation of reactive oxygen species (ROS) in a copper-ascorbate in vitro system. Belongs to the KS-type dehydrin family. | 1,4-dihydroxy-2-naphthoyl-CoA synthase, peroxisomal; Involved in the biosynthesis of phylloquinone (vitamin K1). Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl- CoA (DHNA-CoA) (By similarity). | 0.908 |
HIRD11 | T22F8.30 | Q9SLJ2 | Q9T022 | Dehydrin HIRD11; Intrinsically disordered and metal-binding protein. Binds to the divalent cations cobalt, nickel, copper and zinc, but not to magnesium, calcium, manganese or cadmium. Binding to metal ions decreases disordered state, decreases susceptibility to trypsin and promotes self-association. Can reduce the formation of reactive oxygen species (ROS) in a copper-ascorbate in vitro system. Belongs to the KS-type dehydrin family. | Dehydrin family protein. | 0.915 |
HIRD11 | XERO2 | Q9SLJ2 | P42758 | Dehydrin HIRD11; Intrinsically disordered and metal-binding protein. Binds to the divalent cations cobalt, nickel, copper and zinc, but not to magnesium, calcium, manganese or cadmium. Binding to metal ions decreases disordered state, decreases susceptibility to trypsin and promotes self-association. Can reduce the formation of reactive oxygen species (ROS) in a copper-ascorbate in vitro system. Belongs to the KS-type dehydrin family. | Dehydrin Xero 2; Belongs to the plant dehydrin family. | 0.859 |