node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Jmjd4 | Kdm2a | ENSRNOP00000037005 | ENSRNOP00000051732 | Jumonji domain containing 4 (Predicted). | F-box and leucine-rich repeat protein 11 (Predicted). | 0.423 |
Jmjd4 | Kdm4c | ENSRNOP00000037005 | ENSRNOP00000009083 | Jumonji domain containing 4 (Predicted). | Lysine demethylase 4C. | 0.458 |
Jmjd4 | Kdm8 | ENSRNOP00000037005 | ENSRNOP00000020388 | Jumonji domain containing 4 (Predicted). | Bifunctional peptidase and arginyl-hydroxylase JMJD5; Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monoxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its aminopeptidase activity. Upon DNA damage, cleaves the N-term [...] | 0.675 |
Jmjd6 | Kdm4c | ENSRNOP00000062806 | ENSRNOP00000009083 | Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6; Dioxygenase that can both act as a arginine demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5- hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Regulates RNA splicing by mediating 5- hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. Hydroxylates its own N-terminus, which is required for homooligomerization. In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by it [...] | Lysine demethylase 4C. | 0.464 |
Jmjd6 | Kdm4e | ENSRNOP00000062806 | ENSRNOP00000059913 | Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6; Dioxygenase that can both act as a arginine demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5- hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Regulates RNA splicing by mediating 5- hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. Hydroxylates its own N-terminus, which is required for homooligomerization. In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by it [...] | Lysine-specific demethylase 4D; Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys- 20'. Demethylates both di- and trimethylated H3 'Lys-9' residue, while it has no activity on monomethylated residues. Demethylation of Lys residue generates formaldehyde and succinate (By similarity). | 0.464 |
Jmjd6 | Kdm8 | ENSRNOP00000062806 | ENSRNOP00000020388 | Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6; Dioxygenase that can both act as a arginine demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5- hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Regulates RNA splicing by mediating 5- hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. Hydroxylates its own N-terminus, which is required for homooligomerization. In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by it [...] | Bifunctional peptidase and arginyl-hydroxylase JMJD5; Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monoxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its aminopeptidase activity. Upon DNA damage, cleaves the N-term [...] | 0.651 |
Kdm2a | Jmjd4 | ENSRNOP00000051732 | ENSRNOP00000037005 | F-box and leucine-rich repeat protein 11 (Predicted). | Jumonji domain containing 4 (Predicted). | 0.423 |
Kdm2a | Kdm4c | ENSRNOP00000051732 | ENSRNOP00000009083 | F-box and leucine-rich repeat protein 11 (Predicted). | Lysine demethylase 4C. | 0.490 |
Kdm2a | Kdm4e | ENSRNOP00000051732 | ENSRNOP00000059913 | F-box and leucine-rich repeat protein 11 (Predicted). | Lysine-specific demethylase 4D; Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys- 20'. Demethylates both di- and trimethylated H3 'Lys-9' residue, while it has no activity on monomethylated residues. Demethylation of Lys residue generates formaldehyde and succinate (By similarity). | 0.463 |
Kdm2a | Kdm8 | ENSRNOP00000051732 | ENSRNOP00000020388 | F-box and leucine-rich repeat protein 11 (Predicted). | Bifunctional peptidase and arginyl-hydroxylase JMJD5; Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monoxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its aminopeptidase activity. Upon DNA damage, cleaves the N-term [...] | 0.595 |
Kdm4c | Jmjd4 | ENSRNOP00000009083 | ENSRNOP00000037005 | Lysine demethylase 4C. | Jumonji domain containing 4 (Predicted). | 0.458 |
Kdm4c | Jmjd6 | ENSRNOP00000009083 | ENSRNOP00000062806 | Lysine demethylase 4C. | Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6; Dioxygenase that can both act as a arginine demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5- hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Regulates RNA splicing by mediating 5- hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. Hydroxylates its own N-terminus, which is required for homooligomerization. In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by it [...] | 0.464 |
Kdm4c | Kdm2a | ENSRNOP00000009083 | ENSRNOP00000051732 | Lysine demethylase 4C. | F-box and leucine-rich repeat protein 11 (Predicted). | 0.490 |
Kdm4c | Kdm8 | ENSRNOP00000009083 | ENSRNOP00000020388 | Lysine demethylase 4C. | Bifunctional peptidase and arginyl-hydroxylase JMJD5; Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monoxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its aminopeptidase activity. Upon DNA damage, cleaves the N-term [...] | 0.622 |
Kdm4e | Jmjd6 | ENSRNOP00000059913 | ENSRNOP00000062806 | Lysine-specific demethylase 4D; Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys- 20'. Demethylates both di- and trimethylated H3 'Lys-9' residue, while it has no activity on monomethylated residues. Demethylation of Lys residue generates formaldehyde and succinate (By similarity). | Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6; Dioxygenase that can both act as a arginine demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5- hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Regulates RNA splicing by mediating 5- hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. Hydroxylates its own N-terminus, which is required for homooligomerization. In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by it [...] | 0.464 |
Kdm4e | Kdm2a | ENSRNOP00000059913 | ENSRNOP00000051732 | Lysine-specific demethylase 4D; Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys- 20'. Demethylates both di- and trimethylated H3 'Lys-9' residue, while it has no activity on monomethylated residues. Demethylation of Lys residue generates formaldehyde and succinate (By similarity). | F-box and leucine-rich repeat protein 11 (Predicted). | 0.463 |
Kdm4e | Kdm8 | ENSRNOP00000059913 | ENSRNOP00000020388 | Lysine-specific demethylase 4D; Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys- 20'. Demethylates both di- and trimethylated H3 'Lys-9' residue, while it has no activity on monomethylated residues. Demethylation of Lys residue generates formaldehyde and succinate (By similarity). | Bifunctional peptidase and arginyl-hydroxylase JMJD5; Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monoxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its aminopeptidase activity. Upon DNA damage, cleaves the N-term [...] | 0.601 |
Kdm4e | Phf8 | ENSRNOP00000059913 | ENSRNOP00000040672 | Lysine-specific demethylase 4D; Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys- 20'. Demethylates both di- and trimethylated H3 'Lys-9' residue, while it has no activity on monomethylated residues. Demethylation of Lys residue generates formaldehyde and succinate (By similarity). | PHD finger protein 8. | 0.565 |
Kdm8 | Jmjd4 | ENSRNOP00000020388 | ENSRNOP00000037005 | Bifunctional peptidase and arginyl-hydroxylase JMJD5; Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monoxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its aminopeptidase activity. Upon DNA damage, cleaves the N-term [...] | Jumonji domain containing 4 (Predicted). | 0.675 |
Kdm8 | Jmjd6 | ENSRNOP00000020388 | ENSRNOP00000062806 | Bifunctional peptidase and arginyl-hydroxylase JMJD5; Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monoxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its aminopeptidase activity. Upon DNA damage, cleaves the N-term [...] | Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6; Dioxygenase that can both act as a arginine demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5- hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Regulates RNA splicing by mediating 5- hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. Hydroxylates its own N-terminus, which is required for homooligomerization. In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by it [...] | 0.651 |