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Lysine-specific demethylase 6A (EC 1.14.11.-) (Histone demethylase UTX) (Ubiquitously transcribed TPR protein on the X chromosome) (Ubiquitously transcribed X chromosome tetratricopeptide repeat protein)

 KDM6A_MOUSE             Reviewed;        1401 AA.
O70546; A2AID2; Q6DI80; Q7TSG4;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
09-JAN-2007, sequence version 2.
22-NOV-2017, entry version 144.
RecName: Full=Lysine-specific demethylase 6A;
EC=1.14.11.-;
AltName: Full=Histone demethylase UTX;
AltName: Full=Ubiquitously transcribed TPR protein on the X chromosome;
AltName: Full=Ubiquitously transcribed X chromosome tetratricopeptide repeat protein;
Name=Kdm6a; Synonyms=Utx;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 255-1401 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Embryonic germ cell, and Limb;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 69-1401 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=9499428; DOI=10.1093/hmg/7.4.737;
Greenfield A., Carrel L., Pennisi D., Phillippe C., Quaderi N.,
Siggers P., Steiner K., Tam P.P.L., Monaco A.P., Willard H.F.,
Koopman P.;
"The UTX gene escapes X inactivation in mice and humans.";
Hum. Mol. Genet. 7:737-742(1998).
[4]
INTERACTION WITH TLE1.
PubMed=9854018; DOI=10.1042/bj3370013;
Grbavec D., Lo R., Liu Y., Greenfield A., Stifani S.;
"Groucho/transducin-like enhancer of split (TLE) family members
interact with the yeast transcriptional co-repressor SSN6 and
mammalian SSN6-related proteins: implications for evolutionary
conservation of transcription repression mechanisms.";
Biochem. J. 337:13-17(1999).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-769; THR-827 AND
SER-829, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
FUNCTION, AND INTERACTION WITH SMARCA4.
PubMed=21095589; DOI=10.1016/j.molcel.2010.10.028;
Miller S.A., Mohn S.E., Weinmann A.S.;
"Jmjd3 and UTX play a demethylase-independent role in chromatin
remodeling to regulate T-box family member-dependent gene
expression.";
Mol. Cell 40:594-605(2010).
[8]
INTERACTION WITH SUPT6H.
PubMed=23503590; DOI=10.1038/emboj.2013.54;
Wang A.H., Zare H., Mousavi K., Wang C., Moravec C.E., Sirotkin H.I.,
Ge K., Gutierrez-Cruz G., Sartorelli V.;
"The histone chaperone Spt6 coordinates histone H3K27 demethylation
and myogenesis.";
EMBO J. 32:1075-1086(2013).
[9]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-519 AND ARG-549, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-
27' of histone H3, thereby playing a central role in histone code.
Demethylates trimethylated and dimethylated but not monomethylated
H3 'Lys-27'. Plays a central role in regulation of posterior
development, by regulating HOX gene expression. Demethylation of
'Lys-27' of histone H3 is concomitant with methylation of 'Lys-4'
of histone H3, and regulates the recruitment of the PRC1 complex
and monoubiquitination of histone H2A (By similarity). Plays a
demethylase-independent role in chromatin remodeling to regulate
T-box family member-dependent gene expression (PubMed:21095589).
{ECO:0000250|UniProtKB:O15550, ECO:0000269|PubMed:21095589}.
-!- COFACTOR:
Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
-!- SUBUNIT: Component of the MLL2/3 complex (also named ASCOM
complex), at least composed of KMT2D/MLL2 or KMT2C/MLL3, ASH2L,
RBBP5, WDR5, NCOA6, DPY30, KDM6A (or KDM6B), PAXIP1/PTIP, PAGR1
and alpha- and beta-tubulin (By similarity). Interacts with TLE1
(PubMed:9854018). Interacts with SUPT6H (PubMed:23503590).
Interacts with SMARCA4 (PubMed:21095589).
{ECO:0000250|UniProtKB:O15550, ECO:0000269|PubMed:21095589,
ECO:0000269|PubMed:23503590, ECO:0000269|PubMed:9854018}.
-!- INTERACTION:
Q61321:Six4; NbExp=2; IntAct=EBI-1573712, EBI-986524;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O70546-1; Sequence=Displayed;
Name=2;
IsoId=O70546-2; Sequence=VSP_022196;
-!- TISSUE SPECIFICITY: Expressed in brain, heart and spleen.
-!- DEVELOPMENTAL STAGE: Widely expressed at E13.5.
-!- MISCELLANEOUS: Escapes X chromosome inactivation.
-!- SIMILARITY: Belongs to the UTX family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH75703.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AL732451; CAM27157.1; -; Genomic_DNA.
EMBL; AL773547; CAM27157.1; JOINED; Genomic_DNA.
EMBL; AL773547; CAM18408.1; -; Genomic_DNA.
EMBL; AL732451; CAM18408.1; JOINED; Genomic_DNA.
EMBL; BC053433; AAH53433.1; -; mRNA.
EMBL; BC075703; AAH75703.1; ALT_INIT; mRNA.
EMBL; AJ002730; CAA05692.1; -; mRNA.
CCDS; CCDS30037.1; -. [O70546-2]
CCDS; CCDS81102.1; -. [O70546-1]
RefSeq; NP_001297373.1; NM_001310444.1. [O70546-1]
RefSeq; NP_033509.1; NM_009483.2. [O70546-2]
UniGene; Mm.257498; -.
UniGene; Mm.417709; -.
ProteinModelPortal; O70546; -.
SMR; O70546; -.
BioGrid; 204471; 4.
IntAct; O70546; 6.
MINT; MINT-4584348; -.
STRING; 10090.ENSMUSP00000061539; -.
iPTMnet; O70546; -.
PhosphoSitePlus; O70546; -.
EPD; O70546; -.
MaxQB; O70546; -.
PaxDb; O70546; -.
PeptideAtlas; O70546; -.
PRIDE; O70546; -.
Ensembl; ENSMUST00000044484; ENSMUSP00000045862; ENSMUSG00000037369. [O70546-1]
Ensembl; ENSMUST00000052368; ENSMUSP00000061539; ENSMUSG00000037369. [O70546-2]
GeneID; 22289; -.
KEGG; mmu:22289; -.
UCSC; uc009ssk.1; mouse. [O70546-1]
UCSC; uc009ssm.1; mouse. [O70546-2]
CTD; 7403; -.
MGI; MGI:1095419; Kdm6a.
eggNOG; KOG1124; Eukaryota.
eggNOG; KOG1246; Eukaryota.
eggNOG; COG0457; LUCA.
GeneTree; ENSGT00410000025758; -.
HOGENOM; HOG000220834; -.
InParanoid; O70546; -.
KO; K11447; -.
OMA; NHVHQVT; -.
OrthoDB; EOG091G0OL6; -.
TreeFam; TF317405; -.
Reactome; R-MMU-3214842; HDMs demethylate histones.
ChiTaRS; Kdm6a; mouse.
PRO; PR:O70546; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000037369; -.
Genevisible; O70546; MM.
GO; GO:0035097; C:histone methyltransferase complex; IDA:MGI.
GO; GO:0044666; C:MLL3/4 complex; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
GO; GO:0071558; F:histone demethylase activity (H3-K27 specific); IDA:MGI.
GO; GO:0042802; F:identical protein binding; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:MGI.
GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:MGI.
GO; GO:0072358; P:cardiovascular system development; IMP:MGI.
GO; GO:0006338; P:chromatin remodeling; IMP:UniProtKB.
GO; GO:0048568; P:embryonic organ development; IMP:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
GO; GO:0071557; P:histone H3-K27 demethylation; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0048333; P:mesodermal cell differentiation; IMP:MGI.
GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
GO; GO:0001843; P:neural tube closure; IMP:MGI.
GO; GO:0021915; P:neural tube development; IMP:MGI.
GO; GO:0048570; P:notochord morphogenesis; IMP:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0003016; P:respiratory system process; IMP:MGI.
GO; GO:0032525; P:somite rostral/caudal axis specification; IMP:MGI.
Gene3D; 1.25.40.10; -; 4.
InterPro; IPR003347; JmjC_dom.
InterPro; IPR029516; KDM6C.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR019734; TPR_repeat.
PANTHER; PTHR14017:SF9; PTHR14017:SF9; 2.
Pfam; PF02373; JmjC; 1.
Pfam; PF13181; TPR_8; 1.
SMART; SM00558; JmjC; 1.
SMART; SM00028; TPR; 6.
SUPFAM; SSF48452; SSF48452; 5.
PROSITE; PS51184; JMJC; 1.
PROSITE; PS50005; TPR; 7.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
Alternative splicing; Chromatin regulator; Complete proteome;
Dioxygenase; Iron; Metal-binding; Methylation; Nucleus;
Oxidoreductase; Phosphoprotein; Reference proteome; Repeat;
TPR repeat; Zinc.
CHAIN 1 1401 Lysine-specific demethylase 6A.
/FTId=PRO_0000106410.
REPEAT 95 128 TPR 1.
REPEAT 132 165 TPR 2.
REPEAT 169 203 TPR 3.
REPEAT 207 240 TPR 4.
REPEAT 245 285 TPR 5.
REPEAT 286 319 TPR 6.
REPEAT 321 353 TPR 7.
REPEAT 355 387 TPR 8.
DOMAIN 1095 1258 JmjC. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
REGION 1 1095 Interaction with SUPT6H.
{ECO:0000269|PubMed:23503590}.
COMPBIAS 9 19 Poly-Ala.
COMPBIAS 919 941 Pro-rich.
METAL 1146 1146 Iron. {ECO:0000250}.
METAL 1148 1148 Iron. {ECO:0000250}.
METAL 1226 1226 Iron. {ECO:0000250|UniProtKB:O14607}.
METAL 1331 1331 Zinc. {ECO:0000250}.
METAL 1334 1334 Zinc. {ECO:0000250}.
METAL 1358 1358 Zinc. {ECO:0000250}.
METAL 1361 1361 Zinc. {ECO:0000250}.
MOD_RES 519 519 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 549 549 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 769 769 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 827 827 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 829 829 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1393 1401 APPLPSASS -> VSEINMLLHYHPPHLDIVPWTLNMRPFL
LFRK (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_022196.
CONFLICT 321 321 D -> G (in Ref. 2; AAH75703).
{ECO:0000305}.
CONFLICT 1198 1198 E -> G (in Ref. 2; AAH75703).
{ECO:0000305}.
SEQUENCE 1401 AA; 154355 MW; 293DA417F49EECFF CRC64;
MKSCGVSLAT AAAAAAAAAF GDEEKKMAAG KASGESEEAS PSLTAEEREA LGGLDSRLFG
FVRFHEDGAR MKALLGKAVR CYESLILKAE GKVESDFFCQ LGHFNLLLED YPKALSAYQR
YYSLQSDYWK NAAFLYGLGL VYFHYNAFQW AIKAFQEVLY VDPSFCRAKE IHLRLGLMFK
VNTDYESSLK HFQLALVDCN PCTLSNAEIQ FHIAHLYETQ RKYHSAKEAY EQLLQTENLS
AQVKATILQQ LGWMHHTVDL LGDKATKESY AIQYLQKSLE ADPNSGQSWY FLGRCYSSIG
KVQDAFISYR QSIDKSEASA DTWCSIGVLY QQQNQPMDAL QAYICAVQLD HGHAAAWMDL
GTLYESCNQP QDAIKCYLNA TRSKNCSNTS GLAARIKYLQ AQLCNLPQGS LQNKTKLLPS
IEEAWSLPIP AELTSRQGAM NTAQQNTSDN WSGGNAPPPV EQQTHSWCLT PQKLQHLEQL
RANRNNLNPA QKLMLEQLES QFVLMQQHQM RQTGVAQVRP TGILNGPTVD SSLPTNSVSG
QQPQLPLTRM PSVSQPGVHT ACPRQTLANG PFSAGHVPCS TSRTLGSTDT VLIGNNHVTG
SGSNGNVPYL QRNAPTLPHN RTNLTSSTEE PWKNQLSNST QGLHKGPSSH LAGPNGERPL
SSTGPSQHLQ AAGSGIQNQN GHPTLPSNSV TQGAALNHLS SHTATSGGQQ GITLTKESKP
SGNTLTVPET SRQTGETPNS TASVEGLPNH VHQVMADAVC SPSHGDSKSP GLLSSDNPQL
SALLMGKANN NVGPGTCDKV NNIHPTVHTK TDNSVASSPS SAISTATPSP KSTEQTTTNS
VTSLNSPHSG LHTINGEGME ESQSPIKTDL LLVSHRPSPQ IIPSMSVSIY PSSAEVLKAC
RNLGKNGLSN SSILLDKCPP PRPPSSPYPP LPKDKLNPPT PSIYLENKRD AFFPPLHQFC
TNPNNPVTVI RGLAGALKLD LGLFSTKTLV EANNEHMVEV RTQLLQPADE NWDPTGTKKI
WHCESNRSHT TIAKYAQYQA SSFQESLREE NEKRSHHKDH SDSESTSSDN SGKRRKGPFK
TIKFGTNIDL SDDKKWKLQL HELTKLPAFV RVVSAGNLLS HVGHTILGMN TVQLYMKVPG
SRTPGHQENN NFCSVNINIG PGDCEWFVVP EGYWGVLNDF CEKNNLNFLM GSWWPNLEDL
YEANVPVYRF IQRPGDLVWI NAGTVHWVQA IGWCNNIAWN VGPLTACQYK LAVERYEWNK
LQNVKSIVPM VHLSWNMARN IKVSDPKLFE MIKYCLLRTL KQCQTLREAL IAAGKEIIWH
GRTKEEPAHY CSICEVEVFD LLFVTNESNS RKTYIVHCQD CARKTSGNLE NFVVLEQYKM
EDLMQVYDQF TLAPPLPSAS S


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