Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 (EC 1.14.11.-) (Histone arginine demethylase JMJD6) (JmjC domain-containing protein 6) (Jumonji domain-containing protein 6) (Lysyl-hydroxylase JMJD6) (Peptide-lysine 5-dioxygenase JMJD6) (Phosphatidylserine receptor) (Protein PTDSR)
1_MNHKS 6_ KKRIR 11_ EAKRS 16_ ARPEL 21_ KDSLD 26_ WTRHN 31_ YYESF 36_ SLSPA 41_ AVADN 46_ VERAD 51_ ALQLS 56_ VEEFV 61_ ERYER 66_ PYKPV 71_ VLLNA 76_ QEGWS 81_ AQEKW 86_ TLERL 91_ KRKYR 96_ NQKFK 101_ CGEDN 106_ DGYSV 111_ KMKMK 116_ YYIEY 121_ MESTR 126_ DDSPL 131_ YIFDS 136_ SYGEH 141_ PKRRK 146_ LLEDY 151_ KVPKF 156_ FTDDL 161_ FQYAG 166_ EKRRP 171_ PYRWF 176_ VMGPP 181_ RSGTG 186_ IHIDP 191_ LGTSA 196_ WNALV 201_ QGHKR 206_ WCLFP 211_ TSTPR 216_ ELIKV 221_ TRDEG 226_ GNQQD 231_ EAITW 236_ FNVIY 241_ PRTQL 246_ PTWPP 251_ EFKPL 256_ EILQK 261_ PGETV 266_ FVPGG 271_ WWHVV 276_ LNLDT 281_ TIAIT 286_ QNFAS 291_ STNFP 296_ VVWHK 301_ TVRGR 306_ PKLSR 311_ KWYRI 316_ LKQEH 321_ PELAV 326_ LADSV 331_ DLQES 336_ TGIAS 341_ DSSSD 346_ SSSSS 351_ SSSSS 356_ DSDSE 361_ CESGS 366_ EGDGT 371_ VHRRK 376_ KRRTC 381_ SMVGN 386_ GDTTS 391_ QDDCV 396_SKERS
1: 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)