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O15550

- KDM6A_HUMAN

UniProt

O15550 - KDM6A_HUMAN

Protein

Lysine-specific demethylase 6A

Gene

KDM6A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (23 Sep 2008)
      Previous versions | rss
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    Functioni

    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.2 Publications

    Cofactori

    Ascorbate.1 Publication
    Fe2+.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1146 – 11461Iron
    Metal bindingi1148 – 11481Iron
    Metal bindingi1226 – 12261Iron
    Metal bindingi1331 – 13311Zinc
    Metal bindingi1334 – 13341Zinc
    Metal bindingi1358 – 13581Zinc
    Metal bindingi1361 – 13611Zinc

    GO - Molecular functioni

    1. dioxygenase activity Source: UniProtKB-KW
    2. histone demethylase activity (H3-K27 specific) Source: Ensembl
    3. metal ion binding Source: UniProtKB-KW
    4. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl

    GO - Biological processi

    1. canonical Wnt signaling pathway Source: Ensembl
    2. heart development Source: Ensembl
    3. histone H3-K4 methylation Source: UniProtKB
    4. in utero embryonic development Source: Ensembl
    5. mesodermal cell differentiation Source: Ensembl
    6. neural tube closure Source: Ensembl
    7. notochord morphogenesis Source: Ensembl
    8. respiratory system process Source: Ensembl
    9. somite rostral/caudal axis specification Source: Ensembl

    Keywords - Molecular functioni

    Chromatin regulator, Dioxygenase, Oxidoreductase

    Keywords - Ligandi

    Iron, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysine-specific demethylase 6A (EC:1.14.11.-)
    Alternative name(s):
    Histone demethylase UTX
    Ubiquitously-transcribed TPR protein on the X chromosome
    Ubiquitously-transcribed X chromosome tetratricopeptide repeat protein
    Gene namesi
    Name:KDM6A
    Synonyms:UTX
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

    Organism-specific databases

    HGNCiHGNC:12637. KDM6A.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. histone methyltransferase complex Source: MGI
    2. nucleus Source: MGI

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Kabuki syndrome 2 (KABUK2) [MIM:300867]: A congenital mental retardation syndrome with additional features, including postnatal dwarfism, a peculiar facies characterized by long palpebral fissures with eversion of the lateral third of the lower eyelids, a broad and depressed nasal tip, large prominent earlobes, a cleft or high-arched palate, scoliosis, short fifth finger, persistence of fingerpads, radiographic abnormalities of the vertebrae, hands, and hip joints, and recurrent otitis media in infancy.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1146 – 11461H → A: Abolishes histone demethylase activity. 3 Publications

    Keywords - Diseasei

    Mental retardation

    Organism-specific databases

    MIMi300867. phenotype.
    Orphaneti2322. Kabuki syndrome.
    PharmGKBiPA37262.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14011401Lysine-specific demethylase 6APRO_0000106409Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei769 – 7691Phosphoserine1 Publication
    Modified residuei829 – 8291Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO15550.
    PaxDbiO15550.
    PRIDEiO15550.

    PTM databases

    PhosphoSiteiO15550.

    Expressioni

    Gene expression databases

    ArrayExpressiO15550.
    BgeeiO15550.
    CleanExiHS_UTX.
    GenevestigatoriO15550.

    Organism-specific databases

    HPAiHPA000568.
    HPA002111.

    Interactioni

    Subunit structurei

    Interacts with TLE1 By similarity. 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. Interacts with SUPT6H By similarity.By similarity

    Protein-protein interaction databases

    BioGridi113246. 23 interactions.
    DIPiDIP-46192N.
    IntActiO15550. 11 interactions.
    MINTiMINT-1188304.
    STRINGi9606.ENSP00000367203.

    Structurei

    Secondary structure

    1
    1401
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi893 – 9008
    Helixi933 – 9353
    Beta strandi942 – 9443
    Helixi948 – 9514
    Helixi954 – 9618
    Beta strandi966 – 9716
    Helixi973 – 9775
    Helixi981 – 9844
    Helixi986 – 9927
    Beta strandi997 – 10048
    Beta strandi1016 – 10194
    Beta strandi1025 – 10317
    Helixi1032 – 104514
    Beta strandi1081 – 10899
    Turni1093 – 10964
    Helixi1097 – 11026
    Helixi1103 – 11053
    Helixi1108 – 11103
    Helixi1118 – 11214
    Beta strandi1122 – 11243
    Turni1127 – 11293
    Beta strandi1133 – 11375
    Beta strandi1142 – 11465
    Helixi1149 – 11513
    Beta strandi1153 – 116210
    Beta strandi1164 – 11696
    Helixi1171 – 11733
    Helixi1174 – 118310
    Turni1188 – 11903
    Helixi1197 – 12026
    Beta strandi1208 – 12125
    Beta strandi1217 – 12204
    Beta strandi1225 – 124117
    Beta strandi1243 – 12453
    Helixi1246 – 126217
    Helixi1270 – 128011
    Helixi1286 – 131227
    Beta strandi1317 – 13193
    Turni1332 – 13343
    Beta strandi1340 – 13467
    Beta strandi1351 – 13577
    Helixi1359 – 13657
    Beta strandi1373 – 13764
    Helixi1380 – 13889

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3AVRX-ray1.80A880-1401[»]
    3AVSX-ray1.85A880-1401[»]
    ProteinModelPortaliO15550.
    SMRiO15550. Positions 108-378, 886-1395.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati93 – 12634TPR 1Add
    BLAST
    Repeati130 – 16334TPR 2Add
    BLAST
    Repeati170 – 19930TPR 3Add
    BLAST
    Repeati205 – 23834TPR 4Add
    BLAST
    Repeati250 – 28334TPR 5Add
    BLAST
    Repeati284 – 31734TPR 6Add
    BLAST
    Repeati318 – 35134TPR 7Add
    BLAST
    Repeati352 – 38534TPR 8Add
    BLAST
    Domaini1095 – 1258164JmjCPROSITE-ProRule annotationsAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 10951095Interaction with SUPT6HBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi9 – 179Poly-Ala

    Sequence similaritiesi

    Belongs to the UTX family.Curated
    Contains 1 JmjC domain.PROSITE-ProRule annotations
    Contains 8 TPR repeats.PROSITE-ProRule annotations

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiCOG0457.
    InParanoidiO15550.
    KOiK11447.
    OrthoDBiEOG7CG6Z5.
    PhylomeDBiO15550.
    TreeFamiTF317405.

    Family and domain databases

    Gene3Di1.25.40.10. 1 hit.
    InterProiIPR003347. JmjC_dom.
    IPR029517. KDM6A.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view]
    PANTHERiPTHR14017:SF9. PTHR14017:SF9. 1 hit.
    PfamiPF02373. JmjC. 1 hit.
    PF00515. TPR_1. 3 hits.
    PF13181. TPR_8. 1 hit.
    [Graphical view]
    SMARTiSM00558. JmjC. 1 hit.
    SM00028. TPR. 6 hits.
    [Graphical view]
    PROSITEiPS51184. JMJC. 1 hit.
    PS50005. TPR. 7 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Sequencei

    Sequence statusi: Complete.

    O15550-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKSCGVSLAT AAAAAAAFGD EEKKMAAGKA SGESEEASPS LTAEEREALG     50
    GLDSRLFGFV RFHEDGARTK ALLGKAVRCY ESLILKAEGK VESDFFCQLG 100
    HFNLLLEDYP KALSAYQRYY SLQSDYWKNA AFLYGLGLVY FHYNAFQWAI 150
    KAFQEVLYVD PSFCRAKEIH LRLGLMFKVN TDYESSLKHF QLALVDCNPC 200
    TLSNAEIQFH IAHLYETQRK YHSAKEAYEQ LLQTENLSAQ VKATVLQQLG 250
    WMHHTVDLLG DKATKESYAI QYLQKSLEAD PNSGQSWYFL GRCYSSIGKV 300
    QDAFISYRQS IDKSEASADT WCSIGVLYQQ QNQPMDALQA YICAVQLDHG 350
    HAAAWMDLGT LYESCNQPQD AIKCYLNATR SKSCSNTSAL AARIKYLQAQ 400
    LCNLPQGSLQ NKTKLLPSIE EAWSLPIPAE LTSRQGAMNT AQQNTSDNWS 450
    GGHAVSHPPV QQQAHSWCLT PQKLQHLEQL RANRNNLNPA QKLMLEQLES 500
    QFVLMQQHQM RPTGVAQVRS TGIPNGPTAD SSLPTNSVSG QQPQLALTRV 550
    PSVSQPGVRP ACPGQPLANG PFSAGHVPCS TSRTLGSTDT ILIGNNHITG 600
    SGSNGNVPYL QRNALTLPHN RTNLTSSAEE PWKNQLSNST QGLHKGQSSH 650
    SAGPNGERPL SSTGPSQHLQ AAGSGIQNQN GHPTLPSNSV TQGAALNHLS 700
    SHTATSGGQQ GITLTKESKP SGNILTVPET SRHTGETPNS TASVEGLPNH 750
    VHQMTADAVC SPSHGDSKSP GLLSSDNPQL SALLMGKANN NVGTGTCDKV 800
    NNIHPAVHTK TDNSVASSPS SAISTATPSP KSTEQTTTNS VTSLNSPHSG 850
    LHTINGEGME ESQSPMKTDL LLVNHKPSPQ IIPSMSVSIY PSSAEVLKAC 900
    RNLGKNGLSN SSILLDKCPP PRPPSSPYPP LPKDKLNPPT PSIYLENKRD 950
    AFFPPLHQFC TNPNNPVTVI RGLAGALKLD LGLFSTKTLV EANNEHMVEV 1000
    RTQLLQPADE NWDPTGTKKI WHCESNRSHT TIAKYAQYQA SSFQESLREE 1050
    NEKRSHHKDH SDSESTSSDN SGRRRKGPFK TIKFGTNIDL SDDKKWKLQL 1100
    HELTKLPAFV RVVSAGNLLS HVGHTILGMN TVQLYMKVPG SRTPGHQENN 1150
    NFCSVNINIG PGDCEWFVVP EGYWGVLNDF CEKNNLNFLM GSWWPNLEDL 1200
    YEANVPVYRF IQRPGDLVWI NAGTVHWVQA IGWCNNIAWN VGPLTACQYK 1250
    LAVERYEWNK LQSVKSIVPM VHLSWNMARN IKVSDPKLFE MIKYCLLRTL 1300
    KQCQTLREAL IAAGKEIIWH GRTKEEPAHY CSICEVEVFD LLFVTNESNS 1350
    RKTYIVHCQD CARKTSGNLE NFVVLEQYKM EDLMQVYDQF TLAPPLPSAS 1400
    S 1401
    Length:1,401
    Mass (Da):154,177
    Last modified:September 23, 2008 - v2
    Checksum:i9DD7EA6C61E79229
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti30 – 301A → T.
    Corresponds to variant rs6529 [ dbSNP | Ensembl ].
    VAR_014492
    Natural varianti270 – 2701I → V in a patient with chronic myelomonocytic leukemia. 1 Publication
    VAR_067225
    Natural varianti497 – 4971Q → H.
    Corresponds to variant rs6530 [ dbSNP | Ensembl ].
    VAR_014493
    Natural varianti581 – 5811T → A.
    Corresponds to variant rs34922269 [ dbSNP | Ensembl ].
    VAR_046527
    Natural varianti726 – 7261T → K.1 Publication
    Corresponds to variant rs2230018 [ dbSNP | Ensembl ].
    VAR_020313
    Natural varianti834 – 8341E → D in a patient with chronic myelomonocytic leukemia. 1 Publication
    VAR_067226
    Natural varianti922 – 9221R → K in a patient with chronic myelomonocytic leukemia. 1 Publication
    VAR_067227
    Natural varianti1106 – 11061L → R in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035871

    Sequence conflict

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti173 – 1731L → V in AAC51839. (PubMed:9381176)Curated
    Sequence conflicti173 – 1731L → V in AAC51840. (PubMed:9381176)Curated
    Sequence conflicti585 – 5851L → R in AAC51839. (PubMed:9381176)Curated
    Sequence conflicti585 – 5851L → R in AAC51840. (PubMed:9381176)Curated
    Sequence conflicti601 – 6011S → N in AAC51839. (PubMed:9381176)Curated
    Sequence conflicti601 – 6011S → N in AAC51840. (PubMed:9381176)Curated
    Sequence conflicti629 – 6291E → K in AAC51839. (PubMed:9381176)Curated
    Sequence conflicti629 – 6291E → K in AAC51840. (PubMed:9381176)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF000992 mRNA. Translation: AAC51839.1.
    AF000993 mRNA. Translation: AAC51840.1.
    AL133545, AC136488, AL138744 Genomic DNA. Translation: CAI40508.1.
    AL138744, AC136488, AL133545 Genomic DNA. Translation: CAI41479.1.
    CH471141 Genomic DNA. Translation: EAW59368.1.
    BC093868 mRNA. Translation: AAH93868.1.
    BC113381 mRNA. Translation: AAI13382.1.
    CCDSiCCDS14265.1.
    PIRiT02255.
    RefSeqiNP_066963.2. NM_021140.3.
    UniGeneiHs.522616.

    Genome annotation databases

    EnsembliENST00000377967; ENSP00000367203; ENSG00000147050.
    GeneIDi7403.
    KEGGihsa:7403.
    UCSCiuc004dge.4. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF000992 mRNA. Translation: AAC51839.1 .
    AF000993 mRNA. Translation: AAC51840.1 .
    AL133545 , AC136488 , AL138744 Genomic DNA. Translation: CAI40508.1 .
    AL138744 , AC136488 , AL133545 Genomic DNA. Translation: CAI41479.1 .
    CH471141 Genomic DNA. Translation: EAW59368.1 .
    BC093868 mRNA. Translation: AAH93868.1 .
    BC113381 mRNA. Translation: AAI13382.1 .
    CCDSi CCDS14265.1.
    PIRi T02255.
    RefSeqi NP_066963.2. NM_021140.3.
    UniGenei Hs.522616.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3AVR X-ray 1.80 A 880-1401 [» ]
    3AVS X-ray 1.85 A 880-1401 [» ]
    ProteinModelPortali O15550.
    SMRi O15550. Positions 108-378, 886-1395.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113246. 23 interactions.
    DIPi DIP-46192N.
    IntActi O15550. 11 interactions.
    MINTi MINT-1188304.
    STRINGi 9606.ENSP00000367203.

    Chemistry

    ChEMBLi CHEMBL2069164.

    PTM databases

    PhosphoSitei O15550.

    Proteomic databases

    MaxQBi O15550.
    PaxDbi O15550.
    PRIDEi O15550.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000377967 ; ENSP00000367203 ; ENSG00000147050 .
    GeneIDi 7403.
    KEGGi hsa:7403.
    UCSCi uc004dge.4. human.

    Organism-specific databases

    CTDi 7403.
    GeneCardsi GC0XP044732.
    GeneReviewsi KDM6A.
    H-InvDB HIX0019137.
    HGNCi HGNC:12637. KDM6A.
    HPAi HPA000568.
    HPA002111.
    MIMi 300128. gene.
    300867. phenotype.
    neXtProti NX_O15550.
    Orphaneti 2322. Kabuki syndrome.
    PharmGKBi PA37262.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0457.
    InParanoidi O15550.
    KOi K11447.
    OrthoDBi EOG7CG6Z5.
    PhylomeDBi O15550.
    TreeFami TF317405.

    Miscellaneous databases

    ChiTaRSi KDM6A. human.
    GeneWikii UTX_(gene).
    GenomeRNAii 7403.
    NextBioi 28980.
    PROi O15550.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15550.
    Bgeei O15550.
    CleanExi HS_UTX.
    Genevestigatori O15550.

    Family and domain databases

    Gene3Di 1.25.40.10. 1 hit.
    InterProi IPR003347. JmjC_dom.
    IPR029517. KDM6A.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view ]
    PANTHERi PTHR14017:SF9. PTHR14017:SF9. 1 hit.
    Pfami PF02373. JmjC. 1 hit.
    PF00515. TPR_1. 3 hits.
    PF13181. TPR_8. 1 hit.
    [Graphical view ]
    SMARTi SM00558. JmjC. 1 hit.
    SM00028. TPR. 6 hits.
    [Graphical view ]
    PROSITEi PS51184. JMJC. 1 hit.
    PS50005. TPR. 7 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Functional coherence of the human Y chromosome."
      Lahn B.T., Page D.C.
      Science 278:675-680(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LYS-726.
      Tissue: Brain.
    5. "PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex."
      Cho Y.-W., Hong T., Hong S., Guo H., Yu H., Kim D., Guszczynski T., Dressler G.R., Copeland T.D., Kalkum M., Ge K.
      J. Biol. Chem. 282:20395-20406(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MLL2/3 COMPLEX.
    6. Cited for: FUNCTION, ENZYME ACTIVITY, MUTAGENESIS OF HIS-1146.
    7. "Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases."
      Hong S., Cho Y.W., Yu L.-R., Yu H., Veenstra T.D., Ge K.
      Proc. Natl. Acad. Sci. U.S.A. 104:18439-18444(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY, MUTAGENESIS OF HIS-1146.
    8. "Demethylation of H3K27 regulates polycomb recruitment and H2A ubiquitination."
      Lee M.G., Villa R., Trojer P., Norman J., Yan K.P., Reinberg D., Di Croce L., Shiekhattar R.
      Science 318:447-450(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME ACTIVITY, COFACTOR, MUTAGENESIS OF HIS-1146, IDENTIFICATION IN THE MLL2/3 COMPLEX.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-769 AND SER-829, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "Deletion of KDM6A, a histone demethylase interacting with MLL2, in three patients with Kabuki syndrome."
      Lederer D., Grisart B., Digilio M.C., Benoit V., Crespin M., Ghariani S.C., Maystadt I., Dallapiccola B., Verellen-Dumoulin C.
      Am. J. Hum. Genet. 90:119-124(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN KABUK2.
    12. "Structural basis for histone H3 Lys 27 demethylation by UTX/KDM6A."
      Sengoku T., Yokoyama S.
      Genes Dev. 25:2266-2277(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 880-1401 IN COMPLEX WITH HISTONE H3 PEPTIDE, IRON-BINDING SITES, ZINC-BINDING SITES.
    13. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-1106.
    14. "Mutational spectrum analysis of chronic myelomonocytic leukemia includes genes associated with epigenetic regulation: UTX, EZH2, and DNMT3A."
      Jankowska A.M., Makishima H., Tiu R.V., Szpurka H., Huang Y., Traina F., Visconte V., Sugimoto Y., Prince C., O'Keefe C., Hsi E.D., List A., Sekeres M.A., Rao A., McDevitt M.A., Maciejewski J.P.
      Blood 118:3932-3941(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VAL-270; ASP-834 AND LYS-922.

    Entry informationi

    Entry nameiKDM6A_HUMAN
    AccessioniPrimary (citable) accession number: O15550
    Secondary accession number(s): Q52LL9, Q5JVQ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: September 23, 2008
    Last modified: October 1, 2014
    This is version 140 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Escapes X chromosome inactivation.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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