ID A0A2K5J0X3_COLAP Unreviewed; 888 AA. AC A0A2K5J0X3; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 27-NOV-2024, entry version 34. DE RecName: Full=JmjC domain-containing protein {ECO:0000259|PROSITE:PS51184}; OS Colobus angolensis palliatus (Peters' Angolan colobus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC Cercopithecidae; Colobinae; Colobus. OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000022583.1, ECO:0000313|Proteomes:UP000233080}; RN [1] {ECO:0000313|Ensembl:ENSCANP00000022583.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2023) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. 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 RefSeq; XP_011796955.1; XM_011941565.1. DR AlphaFoldDB; A0A2K5J0X3; -. DR STRING; 336983.ENSCANP00000022583; -. DR Ensembl; ENSCANT00000045565.1; ENSCANP00000022583.1; ENSCANG00000034724.1. DR GeneID; 105511405; -. DR KEGG; cang:105511405; -. DR CTD; 80853; -. DR OMA; PWEEDIT; -. DR OrthoDB; 2784357at2759; -. DR Proteomes; UP000233080; Unplaced. DR GO; GO:0032452; F:histone demethylase activity; IEA:TreeGrafter. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003712; F:transcription coregulator activity; IEA:TreeGrafter. DR GO; GO:0006482; P:protein demethylation; IEA:TreeGrafter. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:TreeGrafter. DR FunFam; 1.20.58.1360:FF:000003; Lysine-specific demethylase 7A; 1. DR FunFam; 2.60.120.650:FF:000021; Lysine-specific demethylase 7A; 1. DR Gene3D; 1.20.58.1360; -; 1. DR Gene3D; 2.60.120.650; Cupin; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR041070; JHD. DR InterPro; IPR050690; JHDM1_Histone_Demethylase. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR23123:SF15; LYSINE-SPECIFIC DEMETHYLASE 7A; 1. DR PANTHER; PTHR23123; PHD/F-BOX CONTAINING PROTEIN; 1. DR Pfam; PF17811; JHD; 1. DR Pfam; PF02373; JmjC; 1. DR SMART; SM00558; JmjC; 1. DR SUPFAM; SSF51197; Clavaminate synthase-like; 1. DR PROSITE; PS51184; JMJC; 1. PE 4: Predicted; KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853}; KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964}; KW Iron {ECO:0000256|ARBA:ARBA00023004}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022964}; KW Reference proteome {ECO:0000313|Proteomes:UP000233080}; KW Transcription {ECO:0000256|ARBA:ARBA00023163}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}. FT DOMAIN 177..333 FT /note="JmjC" FT /evidence="ECO:0000259|PROSITE:PS51184" FT REGION 544..568 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 599..618 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 624..646 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 764..868 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 550..568 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 627..642 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 781..829 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 888 AA; 101484 MW; E7BE078E2DA8FA8E CRC64; MSPAVGGRKS EPCVGVEEHH AVDIDLYHCP NCAVLHGSSL MKKRRNWHRH DYTEIDDGSK PVQAGTRTFI KELRSRVFPS ADEIIVKMHG SQLTQRYLEK HGFDVPIMVP KLDDLGLRLP PPTFSVMDVE RYVGGDKVID VIDVARQADS KMTLHNYVKY FMNPNRPKVL NVISLEFSDT KMSELVEVPD IAKKLSWVEN YWPDDSVFPK PFVQKYCLMG VQDSYTDFHI DFGGTSVWYH VLWGEKIFYL IKPTDENLAR YESWSSSVTQ SEVFFGDKVD KCYKCVVKQG HTLFVPTGWI HAVLTSQDCM AFGGNFLHNL NIGMQLRCYE MEKRLKTPDL FKFPFFEAIC WFVAKNLLET LKELREDGFQ PQTYLVQGVK ALHTALKLWM KKELVSEHAF EIPDNVRPGH LIKELSKVIR AIEEENGKPV KSQGIPTVCP VSRSSNEATS PYHSRRKMRK LRDHNVQTPS NLDILELHTR EVLKRLEMCP WEEDILSSKL NGKFNKHLQP SSTVPEWRAK DNDLRLLLTN GRIIKDERQP FADQSLYTAD SENEEDKRRT KKAKMKIEER SRIEGVENEE SQKPLNRFFT RVKSELRSRS SGYSDISESE DSGPECTALK NNFTTEESES SGDEKKQEIT SNFKEESNVM RNFLRKSQKP SRSEIPIKRE CPTSTSTEEE AIQGMLSMAG LHYSTCLQRQ IQSTGCSGER NSLQDPSSCH SSNPEVRQLY RYHKPVECGY HVKTEDPDLR TSSWIKQFDT SRFNPQDLSR SQKCIKKEGS SEISQRVQSR NYVDSSGSSL QNGKCMQNSN LTSGTCQLSN GSLSPERPVG ETSFSLPLHP TKRPASNPPP ISNQATKGKR PKKGMATAKQ RLGKILKLNR NGHARFFV //