ID F8W8R6_HUMAN Unreviewed; 1408 AA. AC F8W8R6; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 3. DT 24-JUL-2024, entry version 97. DE RecName: Full=[histone H3]-trimethyl-L-lysine(27) demethylase {ECO:0000256|ARBA:ARBA00034525}; DE EC=1.14.11.68 {ECO:0000256|ARBA:ARBA00034525}; GN Name=KDM6A {ECO:0000313|Ensembl:ENSP00000372355.6}; 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|Ensembl:ENSP00000372355.6, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [2] {ECO:0007829|PubMed:19413330} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [3] {ECO:0007829|PubMed:19690332} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [4] {ECO:0007829|PubMed:23186163} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=23186163; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [5] {ECO:0000313|Ensembl:ENSP00000372355.6} RP IDENTIFICATION. RG Ensembl; RL Submitted (APR-2024) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(27)- CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L- CC lysyl(27)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60224, CC Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15544, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961; CC EC=1.14.11.68; Evidence={ECO:0000256|ARBA:ARBA00034421}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000256|ARBA:ARBA00001954}; CC -!- COFACTOR: CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; CC Evidence={ECO:0000256|ARBA:ARBA00001961}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the UTX family. {ECO:0000256|ARBA:ARBA00034483}. 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; AC136488; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL133545; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL138744; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF510678; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001278345.1; NM_001291416.1. DR SMR; F8W8R6; -. DR MassIVE; F8W8R6; -. DR PeptideAtlas; F8W8R6; -. DR ProteomicsDB; 30193; -. DR Antibodypedia; 639; 212 antibodies from 27 providers. DR Ensembl; ENST00000382899.9; ENSP00000372355.6; ENSG00000147050.18. DR GeneID; 7403; -. DR UCSC; uc064yru.1; human. DR CTD; 7403; -. DR DisGeNET; 7403; -. DR HGNC; HGNC:12637; KDM6A. DR VEuPathDB; HostDB:ENSG00000147050; -. DR GeneTree; ENSGT00940000155202; -. DR OrthoDB; 20251at2759; -. DR ChiTaRS; KDM6A; human. DR Proteomes; UP000005640; Chromosome X. DR Bgee; ENSG00000147050; Expressed in secondary oocyte and 200 other cell types or tissues. DR ExpressionAtlas; F8W8R6; baseline and differential. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0032452; F:histone demethylase activity; IEA:UniProt. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 1.20.58.1370; -; 2. DR Gene3D; 2.10.110.20; -; 1. DR Gene3D; 2.60.120.650; Cupin; 1. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2. DR InterPro; IPR051630; Corepressor-Demethylase. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR046941; KDM6_GATAL_sf. DR InterPro; IPR048562; KDM6A_B-like_C-hel. DR InterPro; IPR048560; KDM6A_B-like_GATAL. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_repeat. DR PANTHER; PTHR14017; LYSINE-SPECIFIC DEMETHYLASE; 1. DR PANTHER; PTHR14017:SF9; LYSINE-SPECIFIC DEMETHYLASE 6A; 1. DR Pfam; PF02373; JmjC; 1. DR Pfam; PF21322; KDM6_C-hel; 1. DR Pfam; PF21326; KDM6_GATAL; 1. DR Pfam; PF13432; TPR_16; 1. DR Pfam; PF13181; TPR_8; 1. DR SMART; SM00558; JmjC; 1. DR SMART; SM00028; TPR; 6. DR SUPFAM; SSF51197; Clavaminate synthase-like; 1. DR SUPFAM; SSF81901; HCP-like; 1. DR SUPFAM; SSF48452; TPR-like; 1. DR PROSITE; PS51184; JMJC; 1. DR PROSITE; PS50005; TPR; 2. PE 1: Evidence at protein level; KW Iron {ECO:0000256|ARBA:ARBA00023004}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Proteomics identification {ECO:0007829|PeptideAtlas:F8W8R6, KW ECO:0007829|ProteomicsDB:F8W8R6}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}. FT REPEAT 130..163 FT /note="TPR" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339" FT REPEAT 318..351 FT /note="TPR" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339" FT DOMAIN 1102..1265 FT /note="JmjC" FT /evidence="ECO:0000259|PROSITE:PS51184" FT REGION 430..471 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 631..753 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 765..785 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 817..871 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 921..947 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1050..1086 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 817..869 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 924..944 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1053..1083 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1408 AA; 154928 MW; 12E2DA673F80E91F CRC64; MKSCGVSLAT AAAAAAAFGD EEKKMAAGKA SGESEEASPS LTAEEREALG GLDSRLFGFV RFHEDGARTK ALLGKAVRCY ESLILKAEGK VESDFFCQLG HFNLLLEDYP KALSAYQRYY SLQSDYWKNA AFLYGLGLVY FHYNAFQWAI KAFQEVLYVD PSFCRAKEIH LRLGLMFKVN TDYESSLKHF QLALVDCNPC TLSNAEIQFH IAHLYETQRK YHSAKEAYEQ LLQTENLSAQ VKATVLQQLG WMHHTVDLLG DKATKESYAI QYLQKSLEAD PNSGQSWYFL GRCYSSIGKV QDAFISYRQS IDKSEASADT WCSIGVLYQQ QNQPMDALQA YICAVQLDHG HAAAWMDLGT LYESCNQPQD AIKCYLNATR SKSCSNTSAL AARIKYLQAC KPHHPNTEPV LGLSQTPISQ QSLPLHMIPS SQVDDLSSPA KRKRTSSPTK NTSDNWSGGH AVSHPPVQQQ AHSWCLTPQK LQHLEQLRAN RNNLNPAQKL MLEQLESQFV LMQQHQMRPT GVAQVRSTGI PNGPTADSSL PTNSVSGQQP QLALTRVPSV SQPGVRPACP GQPLANGPFS AGHVPCSTSR TLGSTDTILI GNNHITGSGS NGNVPYLQRN ALTLPHNRTN LTSSAEEPWK NQLSNSTQGL HKGQSSHSAG PNGERPLSST GPSQHLQAAG SGIQNQNGHP TLPSNSVTQG AALNHLSSHT ATSGGQQGIT LTKESKPSGN ILTVPETSRH TGETPNSTAS VEGLPNHVHQ MTADAVCSPS HGDSKSPGLL SSDNPQLSAL LMGKANNNVG TGTCDKVNNI HPAVHTKTDN SVASSPSSAI STATPSPKST EQTTTNSVTS LNSPHSGLHT INGEGMEESQ SPMKTDLLLV NHKPSPQIIP SMSVSIYPSS AEVLKACRNL GKNGLSNSSI LLDKCPPPRP PSSPYPPLPK DKLNPPTPSI YLENKRDAFF PPLHQFCTNP NNPVTVIRGL AGALKLDLGL FSTKTLVEAN NEHMVEVRTQ LLQPADENWD PTGTKKIWHC ESNRSHTTIA KYAQYQASSF QESLREENEK RSHHKDHSDS ESTSSDNSGR RRKGPFKTIK FGTNIDLSDD KKWKLQLHEL TKLPAFVRVV SAGNLLSHVG HTILGMNTVQ LYMKVPGSRT PGHQENNNFC SVNINIGPGD CEWFVVPEGY WGVLNDFCEK NNLNFLMGSW WPNLEDLYEA NVPVYRFIQR PGDLVWINAG TVHWVQAIGW CNNIAWNVGP LTACQYKLAV ERYEWNKLQS VKSIVPMVHL SWNMARNIKV SDPKLFEMIK YCLLRTLKQC QTLREALIAA GKEIIWHGRT KEEPAHYCSI CEVEVFDLLF VTNESNSRKT YIVHCQDCAR KTSGNLENFV VLEQYKMEDL MQVYDQFTLA PPLPSASS //