ID A0A0A8K8C0_HUMAN Unreviewed; 641 AA. AC A0A0A8K8C0; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 27-MAR-2024, entry version 30. DE RecName: Full=Bifunctional lysine-specific demethylase and histidyl-hydroxylase {ECO:0000256|RuleBase:RU366061}; DE EC=1.14.11.- {ECO:0000256|RuleBase:RU366061}; GN Name=URLC2 {ECO:0000313|EMBL:BAQ19748.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAQ19748.1}; RN [1] {ECO:0000313|EMBL:BAQ19748.1} RP NUCLEOTIDE SEQUENCE. RA Daigo Y., Nakamura Y.; RT "Isolation and characterization of novel human genes, which are up- RT regulated in lung cancer."; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Oxygenase that can act as both a histone lysine demethylase CC and a ribosomal histidine hydroxylase. {ECO:0000256|RuleBase:RU366061}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2 CC succinate; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA- CC COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, CC ChEBI:CHEBI:61976; EC=1.14.11.27; CC Evidence={ECO:0000256|ARBA:ARBA00034285}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42033; CC Evidence={ECO:0000256|ARBA:ARBA00034285}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + L-histidyl-[protein] + O2 = (3S)-3-hydroxy-L- CC histidyl-[protein] + CO2 + succinate; Xref=Rhea:RHEA:54256, CC Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:13840, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29979, CC ChEBI:CHEBI:30031, ChEBI:CHEBI:138021; EC=1.14.11.79; CC Evidence={ECO:0000256|ARBA:ARBA00036395}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54257; CC Evidence={ECO:0000256|ARBA:ARBA00036395}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + N(6)-methyl-L-lysyl-[protein] + O2 = CO2 + CC formaldehyde + L-lysyl-[protein] + succinate; Xref=Rhea:RHEA:60924, CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, CC ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929; CC Evidence={ECO:0000256|ARBA:ARBA00034225}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60925; CC Evidence={ECO:0000256|ARBA:ARBA00034225}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000256|RuleBase:RU366061}; CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|RuleBase:RU366061}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU366061}. CC -!- SIMILARITY: Belongs to the ROX family. NO66 subfamily. CC {ECO:0000256|ARBA:ARBA00010309}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB101204; BAQ19748.1; -; mRNA. DR AlphaFoldDB; A0A0A8K8C0; -. DR PeptideAtlas; A0A0A8K8C0; -. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0140680; F:histone H3K36me/H3K36me2 demethylase activity; IEA:UniProtKB-EC. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule. DR Gene3D; 3.90.930.40; -; 1. DR Gene3D; 2.60.120.650; Cupin; 1. DR Gene3D; 1.10.10.1500; JmjC domain-containing ribosomal oxygenase (ROX), dimer domain; 1. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR039994; NO66-like. DR InterPro; IPR049043; RIOX1/NO66-like_C_WH. DR PANTHER; PTHR13096; MINA53 MYC INDUCED NUCLEAR ANTIGEN; 1. DR PANTHER; PTHR13096:SF10; RIBOSOMAL OXYGENASE 1-RELATED; 1. DR Pfam; PF08007; JmjC_2; 1. DR Pfam; PF21233; RIOX1_C_WH; 1. DR SMART; SM00558; JmjC; 1. DR SUPFAM; SSF51197; Clavaminate synthase-like; 1. DR PROSITE; PS51184; JMJC; 1. PE 2: Evidence at transcript level; KW Dioxygenase {ECO:0000256|RuleBase:RU366061}; KW Iron {ECO:0000256|RuleBase:RU366061}; KW Metal-binding {ECO:0000256|RuleBase:RU366061}; KW Nucleus {ECO:0000256|RuleBase:RU366061}; KW Oxidoreductase {ECO:0000256|RuleBase:RU366061}; KW Repressor {ECO:0000256|ARBA:ARBA00022491}; KW Transcription {ECO:0000256|RuleBase:RU366061}; KW Transcription regulation {ECO:0000256|RuleBase:RU366061}. FT DOMAIN 294..439 FT /note="JmjC" FT /evidence="ECO:0000259|PROSITE:PS51184" FT REGION 1..35 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 55..81 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 641 AA; 71086 MW; E770642CE70C82FE CRC64; MDGLQASAGP LRRGRPRRRR KPQPHSGSVL ALPLRSRKIR KQLRSVVSRM AALRTQTLPS ENSEESRVES TADDLGDALP GGAAVAAVPD AARREPYGHL GPAELLEASP AARSLQTPSA RLVPASAPPA RLVEVPAAPV RVVETSALLC TAQHLAAVQS SGAPATASGP QVDNTGGEPA WDSPLRRVLA ELNRIPSSRR RAARLFEWLI APMPPDHFYR RLWEREAVLV RRQDHTYYQG LFSTADLDSM LRNEEVQFGQ HLDAARYING RRETLNPPGR ALPAAAWSLY QAGCSLRLLC PQAFSTTVWQ FLAVLQEQFG SMAGSNVYLT PPNSQGFAPH YDDIEAFVLQ LEGRKLWRVY RPRAPTEELA LTSSPNFSQD DLGEPVLQTV LEPGDLLYFP RGFIHQAECQ DGVHSLHLTL STYQRNTWGD FLEAILPLAV QAAMEENVEF RRGLPRDFMD YMGAQHSDSK DPRRTAFMEK VRVLVARLGH FAPVDAVADQ RAKDFIHDSL PPVLTDRERA LSVYGLPIRW EAGEPVNVGA QLTTETEVHM LQDGIARLVG EGGHLFLYYT VENSRVYHLE EPKCLEIYPQ QADAMELLLG SYPEFVRVGD LPCDSVEDQL SLATTLYDKG LLLTKMPLAL N //