Jmjd6
entrez
107817
canonical
uniprot
Q9ERI5
canonical
ensembl
ENSMUSG00000056962
resolver
ensp
ENSMUSP00000047570
resolver
ensp
ENSMUSP00000221866
resolver
genesymbol
Jmjd6
resolver
genesymbol_syn
Kiaa0585
resolver
genesymbol_syn
Ptdsr
resolver
uniprot
A2AA26
resolver
uniprot
A8Y5I2
resolver
uniprot
B2WTI2
resolver
uniprot
Q80TX1
resolver
uniprot_entry
B2WTI2_MOUSE
resolver
uniprot_entry
JMJD6_MOUSE
resolver
uniprot_sec
A2AA26
resolver
uniprot_sec
A8Y5I2
resolver
uniprot_sec
Q80TX1
resolver
amino_acid_sequence
MNHKSKKRIREAKRSARPELKDSLDWTRHNYYESYPLNPAAVPDNVERADALQLSVKEFVERYERPYKPVVLLNAQEGWSAQEKWTLERLKRKYRNQKFKCGEDNDGYSVKMKMKYYIEYMESTRDDSPLYIFDSSYGEHPKRRKLLEDYKVPKFFTDDLFQYAGEKRRPPYRWFVMGPPRSGTGIHIDPLGTSAWNALVQGHKRWCLFPTNTPRELIKVTREEGGNQQDEAITWFNVIYPRTQLPTWPPEFKPLEILQKPGETVFVPGGWWHVVLNLDTTIAITQNFASSTNFPVVWHKTVRGRPKLSRKWYRILKQEHPELAVLADAVDLQESTGIASDSSSDSSSSSSSSSSDSDSECESGSEGDGTTHRRKKRRTCSMVGNGDTTSQDDCVSKERSSSR
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 (PubMed:25369936, PubMed:33443146). 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 (PubMed:15345036). Acts as a key regulator of hematopoietic differentiation: required for angiogenic sprouting by regulating the pre-mRNA splicing activity of U2AF2/U2AF65 (PubMed:21300889). Seems to be necessary for the regulation of macrophage cytokine responses (By similarity). {ECO:0000250|UniProtKB:Q6NYC1, ECO:0000269|PubMed:15345036, ECO:0000269|PubMed:21300889, ECO:0000269|PubMed:25369936, ECO:0000269|PubMed:33443146}.
uniprot
proteins
mass_dalton
46567
uniprot
proteins
mutagenesis
MUTAGEN 277; /note="N->A: Loss of lysyl-hydroxylase activity."; /evidence="ECO:0000269|PubMed:33443146
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
10811223
uniprot
proteins
pubmed
12693553
uniprot
proteins
pubmed
14645847
uniprot
proteins
pubmed
14715629
uniprot
proteins
pubmed
14729065
uniprot
proteins
pubmed
15345036
uniprot
proteins
pubmed
15453906
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21300889
uniprot
proteins
pubmed
25369936
uniprot
proteins
pubmed
33443146
uniprot
proteins
sequence_length
403
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:14729065}. 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