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Details on Person UniProt:Q6NYC1-3 JMJD6
| Class:Id | ReferenceIsoform:233315 |
|---|---|
| _chainChangeLog | chain:1-403 added on Fri February 6 2015 |
| _displayName | UniProt:Q6NYC1-3 JMJD6 |
| _timestamp | 2025-02-21 20:10:35 |
| chain | chain:1-403 |
| checksum | 9C9AADA98B24B035 |
| comment | FUNCTION Dioxygenase that can both act as a arginine demethylase and a lysyl-hydroxylase (PubMed:17947579, PubMed:20684070, PubMed:21060799, PubMed:22189873, PubMed:24498420). 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 (PubMed:19574390). Hydroxylates its own N-terminus, which is required for homooligomerization (PubMed:22189873). 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 (By similarity). In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by its ability to bind single strand RNA (PubMed:20679243, PubMed:29176719). Also acts as an arginine demethylase which preferentially demethylates asymmetric dimethylation (PubMed:17947579, PubMed:24360279, PubMed:24498420). 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 (PubMed:17947579, PubMed:24360279). However, histone arginine demethylation may not constitute the primary activity in vivo (PubMed:17947579, PubMed:21060799, PubMed:22189873). 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 (PubMed:24360279). Demethylates other arginine methylated-proteins such as ESR1 (PubMed:24498420). Has no histone lysine demethylase activity (PubMed:21060799). 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 (By similarity). Seems to be necessary for the regulation of macrophage cytokine responses (PubMed:15622002).CATALYTIC ACTIVITY L-lysyl-[protein] + 2-oxoglutarate + O2 = (5S)-5-hydroxy-L-lysyl-[protein] + succinate + CO2CATALYTIC ACTIVITY N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 2-oxoglutarate + 2 O2 = L-arginyl-[protein] + 2 formaldehyde + 2 succinate + 2 CO2CATALYTIC ACTIVITY N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2-oxoglutarate + O2 = N(omega)-methyl-L-arginyl-[protein] + formaldehyde + succinate + CO2CATALYTIC ACTIVITY a 5'-end methyltriphosphate-guanosine-ribonucleotide-snRNA + 2-oxoglutarate + O2 = a 5'-end triphospho-guanosine-ribonucleotide-snRNA + formaldehyde + succinate + CO2 + H(+)COFACTOR Binds 1 Fe(2+) ion per subunit.BIOPHYSICOCHEMICAL PROPERTIES Homooligomerizes; requires lysyl-hydroxylase activity (PubMed:22189873, PubMed:24360279). Interacts with LUC7L2, LUC7L3 and U2AF2/U2AF65 (PubMed:19574390). Interacts with CDK9 and CCNT1; the interaction is direct with CDK9 and associates the P-TEFb complex when active (PubMed:24360279). Interacts (via JmjC and N-terminal domains) with BRD4 (via NET domain); the interaction is stronger in presence of ssRNA and recruits JMJD6 on distal enhancers (PubMed:21555454, PubMed:24360279, PubMed:29176719). Interacts with ARGLU1; interaction may be involved in ARGLU1-mediated modulation of alternative splicing (PubMed:30698747).INTERACTION Mainly found throughout the nucleoplasm outside of regions containing heterochromatic DNA, with some localization in nucleolus. During mitosis, excluded from the nucleus and reappears in the telophase of the cell cycle.ALTERNATIVE PRODUCTS 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.INDUCTION Up-regulated upon cytokine treatment, but not upon TNF treatment.DOMAIN The nuclear localization signal motifs are necessary and sufficient to target it into the nucleus.PTM Hydroxylates its own N-terminus; hydroxylation is required for homooligomerization.SIMILARITY Belongs to the JMJD6 family.CAUTION Was initially thought to constitute the phosphatidylserine receptor, a receptor that mediates recognition of phosphatidylserine, a specific marker only present at the surface of apoptotic cells. Phosphatidylserine receptor probably participates in apoptotic cell phagocytosis. This protein was identified using phage display expressing mAb 217, an antibody that specifically recognizes phosphatidylserine receptor. However, its nuclear localization and the fact that mAb 217 antibody still recognizes the phosphatidylserine receptor in mice lacking JMJD6, strongly suggest that it does not constitute the receptor for phosphatidylserine and is not involved in apoptotic cell removal.SEQUENCE CAUTION Extended N-terminus.SEQUENCE CAUTION Extended N-terminus. |
| created | [InstanceEdit:217385] Schmidt, EE, 2008-03-27 06:23:53 |
| description | recommendedName: fullName evidence="24"Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 ecNumber evidence="8 9 11 14"1.14.11.- alternativeName: Histone arginine demethylase JMJD6 alternativeName: JmjC domain-containing protein 6 alternativeName: Jumonji domain-containing protein 6 alternativeName: Lysyl-hydroxylase JMJD6 alternativeName: Peptide-lysine 5-dioxygenase JMJD6 alternativeName: Phosphatidylserine receptor shortName: Protein PTDSR |
| geneName | JMJD6 KIAA0585 PSR PTDSR |
| identifier | Q6NYC1 |
| isoformParent | |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Alternative splicing Chromatin regulator Cytoplasm Developmental protein Differentiation Dioxygenase Iron Metal-binding mRNA processing mRNA splicing Nucleus Oxidoreductase Phosphoprotein Proteomics identification Reference proteome RNA-binding Transcription Transcription regulation |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9841277] Weiser, Joel [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 |
| name | JMJD6 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:9000107] ENSEMBL:ENSG00000070495 JMJD6 [Homo sapiens] |
| secondaryIdentifier | JMJD6_HUMAN B3KMN8 B4DGX1 Q86VY0 Q8IUM5 Q9Y4E2 |
| sequenceLength | 403 |
| species | [Species:48887] Homo sapiens |
| variantIdentifier | Q6NYC1-3 |
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No pathways have been reviewed or authored by UniProt:Q6NYC1-3 JMJD6 (233315)
