| Tissue Specificity | Highly expressed in the heart, skeletal muscle and kidney. Expressed at moderate or low level in brain, placenta, lung, liver, pancreas, spleen, thymus, prostate, testis and ovary. Up-regulated in many patients with chronic pancreatitis. Expressed in nursing thymic epithelial cells. |
| Post Translational Modifications | Hydroxylates its own N-terminus.hydroxylation is required for homooligomerization. |
| Function | 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. Plays a role in the regulation of nucleolar liquid-liquid phase separation (LLPS) by post-translationally modifying LIAT1 at its lysine-rich domain which inhibits LIAT1 nucleolar targeting. In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by its ability to bind single strand RNA. Also acts as an arginine demethylase which preferentially demethylates asymmetric dimethylation. Demethylates histone H3 at 'Arg-2' (H3R2me) and histone H4 at 'Arg-3' (H4R3me), including mono-, symmetric di- and asymmetric dimethylated forms, thereby playing a role in histone code. However, histone arginine demethylation may not constitute the primary activity in vivo. In collaboration with BRD4, interacts with the positive transcription elongation factor b (P-TEFb) complex in its active form to regulate polymerase II promoter-proximal pause release for transcriptional activation of a large cohort of genes. On distal enhancers, so called anti-pause enhancers, demethylates both histone H4R3me2 and the methyl cap of 7SKsnRNA leading to the dismissal of the 7SKsnRNA:HEXIM1 inhibitor complex. After removal of repressive marks, the complex BRD4:JMJD6 attract and retain the P-TEFb complex on chromatin, leading to its activation, promoter-proximal polymerase II pause release, and transcriptional activation. Demethylates other arginine methylated-proteins such as ESR1. Has no histone lysine demethylase activity. Required for differentiation of multiple organs during embryogenesis. Acts as a key regulator of hematopoietic differentiation: required for angiogenic sprouting by regulating the pre-mRNA splicing activity of U2AF2/U2AF65. Seems to be necessary for the regulation of macrophage cytokine responses. |
| Protein Name | Bifunctional Arginine Demethylase And Lysyl-Hydroxylase Jmjd6Histone Arginine Demethylase Jmjd6Jmjc Domain-Containing Protein 6Jumonji Domain-Containing Protein 6Lysyl-Hydroxylase Jmjd6Peptide-Lysine 5-Dioxygenase Jmjd6Phosphatidylserine ReceptorProtein Ptdsr |
| Database Links | Reactome: R-HSA-3214842Reactome: R-HSA-9629569 |
| Cellular Localisation | NucleusNucleoplasmNucleolusCytoplasmMainly Found Throughout The Nucleoplasm Outside Of Regions Containing Heterochromatic DnaWith Some Localization In NucleolusDuring MitosisExcluded From The Nucleus And Reappears In The Telophase Of The Cell Cycle |
| Alternative Protein Names | Bifunctional Arginine Demethylase And Lysyl-Hydroxylase Jmjd6 proteinHistone Arginine Demethylase Jmjd6 proteinJmjc Domain-Containing Protein 6 proteinJumonji Domain-Containing Protein 6 proteinLysyl-Hydroxylase Jmjd6 proteinPeptide-Lysine 5-Dioxygenase Jmjd6 proteinPhosphatidylserine Receptor proteinProtein Ptdsr proteinJMJD6 proteinKIAA0585 proteinPSR proteinPTDSR protein |
Information sourced from Uniprot.org
