Bifunctional peptidase and arginyl-hydroxylase JMJD5 (EC 1.14.11.73) (EC 3.4.-.-) (JmjC domain-containing protein 5) (Jumonji C domain-containing protein 5) (L-arginine (3R)-hydroxylase KDM8)
1_MAGDT 6_ HCPAE 11_ PLARE 16_ GTLWE 21_ ALRAL 26_ LPHSK 31_ EDLKL 36_ DLGEK 41_ VERSV 46_ VTLLQ 51_ RATEL 56_ FYEGR 61_ RDECL 66_ QSSEV 71_ ILDYS 76_ WEKLN 81_ TGTWQ 86_ DVDKD 91_ WRRVY 96_ AIGCL 101_ LKALC 106_ LCQAP 111_ EDANT 116_ VAAAL 121_ RVCDM 126_ GLLMG 131_ AAILG 136_ DILLK 141_ VAAIL 146_ QTHLP 151_ GKRPA 156_ RGSLP 161_ EQPCT 166_ KKARA 171_ DHGLI 176_ PDVKL 181_ EKTVP 186_ RLHRP 191_ SLQHF 196_ REQFL 201_ VPGRP 206_ VILKG 211_ VADHW 216_ PCMQK 221_ WSLEY 226_ IQEIA 231_ GCRTV 236_ PVEVG 241_ SRYTD 246_ EEWSQ 251_ TLMTV 256_ NEFIS 261_ KYIVN 266_ EPRDV 271_ GYLAQ 276_ HQLFD 281_ QIPEL 286_ KQDIS 291_ IPDYC 296_ SLGDG 301_ EEEEI 306_ TINAW 311_ FGPQG 316_ TISPL 321_ HQDPQ 326_ QNFLV 331_ QVMGR 336_ KYIRL 341_ YSPQE 346_ SGALY 351_ PHDTH 356_ LLHNT 361_ SQVDV 366_ ENPDL 371_ EKFPK 376_ FAKAP 381_ FLSCI 386_ LSPGE 391_ ILFIP 396_ VKYWH 401_ YVRAL 406_ DLSFS 411_VSFWW
1: Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monooxygenase (PubMed:28847961, PubMed:28982940, PubMed:29459673, PubMed:29563586). Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation (PubMed:28847961, PubMed:28982940, PubMed:29459673). Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its aminopeptidase activity (PubMed:28847961, PubMed:29459673). Upon DNA damage, cleaves the N-terminal tail of histone H3 at monomethylated lysine residues, preferably at monomethylated 'Lys-9' (H3K9me1). The histone variant H3F3A is the major target for cleavage (PubMed:28982940). Additionally, acts as a Fe(2+) and 2-oxoglutarate-dependent monooxygenase, catalyzing (R)-stereospecific hydroxylation at C-3 of 'Arg-137' of RPS6 and 'Arg-141' of RCCD1, but the biological significance of this activity remains to be established (PubMed:29563586). Regulates mitosis through different mechanisms: Plays a role in transcriptional repression of satellite repeats, possibly by regulating H3K36 methylation levels in centromeric regions together with RCCD1. Possibly together with RCCD1, is involved in proper mitotic spindle organization and chromosome segregation (PubMed:24981860). Negatively regulates cell cycle repressor CDKN1A/p21, which controls G1/S phase transition (PubMed:24740926). Required for G2/M phase cell cycle progression. Regulates expression of CCNA1/cyclin-A1, leading to cancer cell proliferation (PubMed:20457893). Also, plays a role in regulating alpha-tubulin acetylation and cytoskeletal microtubule stability involved in epithelial to mesenchymal transition (PubMed:28455245). Regulates the circadian gene expression in the liver (By similarity). Represses the transcriptional activator activity of the CLOCK-BMAL1 heterodimer in a catalytically-independent manner (PubMed:30500822). Negatively regulates the protein stability and function of CRY1; required for AMPK-FBXL3-induced CRY1 degradation (PubMed:30500822)