JMJD6
entrez
23210
canonical
uniprot
Q6NYC1
canonical
ensembl
ENSG00000070495
resolver
ensp
ENSP00000302916
resolver
ensp
ENSP00000380750
resolver
ensp
ENSP00000394085
resolver
ensp
ENSP00000442362
resolver
enst
ENST00000303996
resolver
enst
ENST00000542934
resolver
genesymbol
JMJD6
resolver
genesymbol_syn
KIAA0585
resolver
genesymbol_syn
PSR
resolver
genesymbol_syn
PTDSR
resolver
hgnc
HGNC:19355
resolver
uniprot
B2WTI3
resolver
uniprot
B2WTI4
resolver
uniprot
B3KMN8
resolver
uniprot
B4DGX1
resolver
uniprot
F6YAN4
resolver
uniprot
J3KND7
resolver
uniprot
Q86VY0
resolver
uniprot
Q8IUM5
resolver
uniprot
Q9Y4E2
resolver
uniprot_entry
B2WTI3_HUMAN
resolver
uniprot_entry
B2WTI4_HUMAN
resolver
uniprot_entry
F6YAN4_HUMAN
resolver
uniprot_entry
J3KND7_HUMAN
resolver
uniprot_entry
JMJD6_HUMAN
resolver
uniprot_sec
B3KMN8
resolver
uniprot_sec
B4DGX1
resolver
uniprot_sec
Q86VY0
resolver
uniprot_sec
Q8IUM5
resolver
uniprot_sec
Q9Y4E2
resolver
amino_acid_sequence
MNHKSKKRIREAKRSARPELKDSLDWTRHNYYESFSLSPAAVADNVERADALQLSVEEFVERYERPYKPVVLLNAQEGWSAQEKWTLERLKRKYRNQKFKCGEDNDGYSVKMKMKYYIEYMESTRDDSPLYIFDSSYGEHPKRRKLLEDYKVPKFFTDDLFQYAGEKRRPPYRWFVMGPPRSGTGIHIDPLGTSAWNALVQGHKRWCLFPTSTPRELIKVTRDEGGNQQDEAITWFNVIYPRTQLPTWPPEFKPLEILQKPGETVFVPGGWWHVVLNLDTTIAITQNFASSTNFPVVWHKTVRGRPKLSRKWYRILKQEHPELAVLADSVDLQESTGIASDSSSDSSSSSSSSSSDSDSECESGSEGDGTVHRRKKRRTCSMVGNGDTTSQDDCVSKERSSSR
uniprot
proteins
ec_number
1.14.11.-
uniprot
proteins
function
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). {ECO:0000250|UniProtKB:Q9ERI5, ECO:0000269|PubMed:15622002, ECO:0000269|PubMed:17947579, ECO:0000269|PubMed:19574390, ECO:0000269|PubMed:20679243, ECO:0000269|PubMed:20684070, ECO:0000269|PubMed:21060799, ECO:0000269|PubMed:22189873, ECO:0000269|PubMed:24360279, ECO:0000269|PubMed:24498420, ECO:0000269|PubMed:29176719}.
uniprot
proteins
mass_dalton
46462
uniprot
proteins
mutagenesis
MUTAGEN 85; /note="W->A: Decreases interaction with the NET domain of BRD4."; /evidence="ECO:0000269|PubMed:29176719"; MUTAGEN 90; /note="L->A: Nearly abolishes the interaction with the NET domain of BRD4."; /evidence="ECO:0000269|PubMed:29176719"; MUTAGEN 91; /note="K->A: Nearly abolishes the interaction with the NET domain of BRD4."; /evidence="ECO:0000269|PubMed:29176719"; MUTAGEN 95; /note="R->A: Nearly abolishes the interaction with the NET domain of BRD4."; /evidence="ECO:0000269|PubMed:29176719"; MUTAGEN 131; /note="Y->F: Abolishes 2-oxoglutarate-binding and enzyme activity."; /evidence="ECO:0000269|PubMed:20684070"; MUTAGEN 187; /note="H->A: Loss of histone arginine demethylase and lysyl-hydroxylase activities. Abolishes homooligomerization. Loss of arginine demethylase and a lysyl-hydroxylase activities; when associated with A-189 and A-273."; /evidence="ECO:0000269|PubMed:17947579, ECO:0000269|PubMed:19574390, ECO:0000269|PubMed:22189873, ECO:0000269|PubMed:24360279"; MUTAGEN 189; /note="D->A: Loss of arginine demethylase and a lysyl-hydroxylase activities; when associated with A-187 and A-273."; /evidence="ECO:0000269|PubMed:17947579, ECO:0000269|PubMed:19574390"; MUTAGEN 204; /note="K->A: Impairs enzyme activity without affecting 2-oxoglutarate-binding."; /evidence="ECO:0000269|PubMed:20684070"; MUTAGEN 231; /note="E->A: Impairs both hydroxylation activity and 2-oxoglutarate turnover assays."; /evidence="ECO:0000269|PubMed:20684070"; MUTAGEN 273; /note="H->A: Loss of arginine demethylase and a lysyl-hydroxylase activities; when associated with A-187 and A-189."; /evidence="ECO:0000269|PubMed:17947579"; MUTAGEN 285; /note="T->A: Impairs enzyme activity and 2-oxoglutarate-binding."; /evidence="ECO:0000269|PubMed:20684070"; MUTAGEN 287; /note="N->A: Impairs enzyme activity."; /evidence="ECO:0000269|PubMed:20684070
uniprot
proteins
post_translational_modification
PTM: Hydroxylates its own N-terminus; hydroxylation is required for homooligomerization. {ECO:0000269|PubMed:22189873}.
uniprot
proteins
protein_family
JMJD6 family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14729065
uniprot
proteins
pubmed
15072554
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15622002
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
17947579
uniprot
proteins
pubmed
19574390
uniprot
proteins
pubmed
20679243
uniprot
proteins
pubmed
20684070
uniprot
proteins
pubmed
21060799
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21555454
uniprot
proteins
pubmed
22189873
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24360279
uniprot
proteins
pubmed
24498420
uniprot
proteins
pubmed
29176719
uniprot
proteins
pubmed
30698747
uniprot
proteins
pubmed
9628581
uniprot
proteins
sequence_length
403
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:14729065, ECO:0000269|PubMed:21060799}. Nucleus, nucleolus {ECO:0000269|PubMed:21060799}. Cytoplasm {ECO:0000269|PubMed:21060799, ECO:0000269|PubMed:24498420}. 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:0000269|PubMed:21060799}.
uniprot
proteins