Jmjd6
entrez
360665
canonical
uniprot
Q6AYK2
canonical
ensembl
ENSRNOG00000000250
resolver
ensembl
ENSRNOG00055031572
resolver
ensp
ENSRNOP00000062806
resolver
ensp
ENSRNOP00000077039
resolver
ensp
ENSRNOP00055045210
resolver
enst
ENSRNOT00000064671
resolver
enst
ENSRNOT00000116096
resolver
enst
ENSRNOT00055054701
resolver
genesymbol
Jmjd6
resolver
genesymbol_syn
Ptdsr
resolver
uniprot
A0A8I5Y5A5
resolver
uniprot
A0A8L2QWD0
resolver
uniprot_entry
A0A8I5Y5A5_RAT
resolver
uniprot_entry
A0A8L2QWD0_RAT
resolver
uniprot_entry
JMJD6_RAT
resolver
amino_acid_sequence
MNHKSKKRIREAKRSARPELKDSLDWTRHNYYESYPLSPAAVPDNVERADALQLSVKEFVERYERPYKPVVLLNAQEGWSAQEKWTLERLKRKYRNQKFKCGEDNDGYSVKMKMKYYIEYMESTRDDSPLYIFDSSYGEHPKRRKLLEDYKVPKFFTDDLFQYAGEKRRPPYRWFVMGPPRSGTGIHIDPLGTSAWNALVQGHKRWCLFPTNTPRELIKVTREEGGNQQDEAITWFNVIYPRTQLPTWPPEFKPLEILQKPGETVFVPGGWWHVVLNLDTTIAITQNFASSTNFPVVWHKTVRGRPKLSRKWYRILKQEHPELAVLADAVDLQESTGIASDSSSDSSSSSSSSSSDSDSECESGSEGDGTTHRRKKRRTCSMVGNGDTTSQDDCVSKERSSSR
uniprot
proteins
ec_number
1.14.11.-
uniprot
proteins
function
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 (By similarity). 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. 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 (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:Q6NYC1, ECO:0000250|UniProtKB:Q9ERI5}.
uniprot
proteins
mass_dalton
46540
uniprot
proteins
post_translational_modification
PTM: Hydroxylates its own N-terminus; hydroxylation is required for homooligomerization. {ECO:0000250|UniProtKB:Q6NYC1}.
uniprot
proteins
protein_family
JMJD6 family
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
15489334
uniprot
proteins
sequence_length
403
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q6NYC1}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q6NYC1}. Cytoplasm {ECO:0000250|UniProtKB:Q6NYC1}. Note=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. {ECO:0000250|UniProtKB:Q6NYC1}.
uniprot
proteins