ID   F5H5V6_HUMAN            Unreviewed;      1322 AA.
AC   F5H5V6;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 3.
DT   27-MAR-2024, entry version 94.
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:ENSP00000443078.3};
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:ENSP00000443078.3, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000443078.3, 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:ENSP00000443078.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) 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}.
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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_001278347.1; NM_001291418.1.
DR   SMR; F5H5V6; -.
DR   IntAct; F5H5V6; 2.
DR   MassIVE; F5H5V6; -.
DR   PeptideAtlas; F5H5V6; -.
DR   ProteomicsDB; 26997; -.
DR   Antibodypedia; 639; 237 antibodies from 27 providers.
DR   Ensembl; ENST00000543216.6; ENSP00000443078.3; ENSG00000147050.18.
DR   GeneID; 7403; -.
DR   UCSC; uc064yrw.1; human.
DR   CTD; 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; F5H5V6; 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; 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; SSF48452; TPR-like; 2.
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|EPD:F5H5V6,
KW   ECO:0007829|MaxQB:F5H5V6};
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          1016..1179
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   REGION          440..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          679..699
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          731..785
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          835..861
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          964..1000
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        731..783
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        838..858
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        967..997
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1322 AA;  145234 MW;  D1AD928C3F65403D 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 AARIKYLQNT SDNWSGGHAV SHPPVQQQAH
     SWCLTPQKLQ MRPTGVAQVR STGIPNGPTA DSSLPTNSVS GQQPQLALTR VPSVSQPGVR
     PACPGQPLAN GPFSAGHVPC STSRTLGSTD TILIGNNHIT GSGSNGNVPY LQRNALTLPH
     NRTNLTSSAE EPWKNQLSNS TQGLHKGQSS HSAGPNGERP LSSTGPSQHL QAAGSGIQNQ
     NGHPTLPSNS VTQGAALNHL SSHTATSGGQ QGITLTKESK PSGNILTVPE TSRHTGETPN
     STASVEGLPN HVHQMTADAV CSPSHGDSKS PGLLSSDNPQ LSALLMGKAN NNVGTGTCDK
     VNNIHPAVHT KTDNSVASSP SSAISTATPS PKSTEQTTTN SVTSLNSPHS GLHTINGEGM
     EESQSPMKTD LLLVNHKPSP QIIPSMSVSI YPSSAEVLKA CRNLGKNGLS NSSILLDKCP
     PPRPPSSPYP PLPKDKLNPP TPSIYLENKR DAFFPPLHQF CTNPNNPVTV IRGLAGALKL
     DLGLFSTKTL VEANNEHMVE VRTQLLQPAD ENWDPTGTKK IWHCESNRSH TTIAKYAQYQ
     ASSFQESLRE ENEKRSHHKD HSDSESTSSD NSGRRRKGPF KTIKFGTNID LSDDKKWKLQ
     LHELTKLPAF VRVVSAGNLL SHVGHTILGM NTVQLYMKVP GSRTPGHQEN NNFCSVNINI
     GPGDCEWFVV PEGYWGVLND FCEKNNLNFL MGSWWPNLED LYEANVPVYR FIQRPGDLVW
     INAGTVHWVQ AIGWCNNIAW NVGPLTACQY KLAVERYEWN KLQSVKSIVP MVHLSWNMAR
     NIKVSDPKLF EMIKYCLLRT LKQCQTLREA LIAAGKEIIW HGRTKEEPAH YCSICEVEVF
     DLLFVTNESN SRKTYIVHCQ DCARKTSGNL ENFVVLEQYK MEDLMQVYDQ FTLAPPLPSA
     SS
//