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O15550

- KDM6A_HUMAN

UniProt

O15550 - KDM6A_HUMAN

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Protein

Lysine-specific demethylase 6A

Gene

KDM6A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 morphogenesis Source: Ensembl
  3. histone H3-K4 methylation Source: UniProtKB
  4. in utero embryonic development Source: Ensembl
  5. mesodermal cell differentiation Source: Ensembl
  6. multicellular organism growth Source: Ensembl
  7. neural tube closure Source: Ensembl
  8. notochord morphogenesis Source: Ensembl
  9. regulation of gene expression Source: Ensembl
  10. respiratory system process Source: Ensembl
  11. somite rostral/caudal axis specification Source: Ensembl
Complete GO annotation...

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
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:12637. KDM6A.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. histone methyltransferase complex Source: MGI
  2. nucleus Source: MGI
Complete GO annotation...

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

BgeeiO15550.
CleanExiHS_UTX.
ExpressionAtlasiO15550. baseline and differential.
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 – 9008Combined sources
Helixi933 – 9353Combined sources
Beta strandi942 – 9443Combined sources
Helixi948 – 9514Combined sources
Helixi954 – 9618Combined sources
Beta strandi966 – 9716Combined sources
Helixi973 – 9775Combined sources
Helixi981 – 9844Combined sources
Helixi986 – 9927Combined sources
Beta strandi997 – 10048Combined sources
Beta strandi1016 – 10194Combined sources
Beta strandi1025 – 10317Combined sources
Helixi1032 – 104514Combined sources
Beta strandi1081 – 10899Combined sources
Turni1093 – 10964Combined sources
Helixi1097 – 11026Combined sources
Helixi1103 – 11053Combined sources
Helixi1108 – 11103Combined sources
Helixi1118 – 11214Combined sources
Beta strandi1122 – 11243Combined sources
Turni1127 – 11293Combined sources
Beta strandi1133 – 11375Combined sources
Beta strandi1142 – 11465Combined sources
Helixi1149 – 11513Combined sources
Beta strandi1153 – 116210Combined sources
Beta strandi1164 – 11696Combined sources
Helixi1171 – 11733Combined sources
Helixi1174 – 118310Combined sources
Turni1188 – 11903Combined sources
Helixi1197 – 12026Combined sources
Beta strandi1208 – 12125Combined sources
Beta strandi1217 – 12204Combined sources
Beta strandi1225 – 124117Combined sources
Beta strandi1243 – 12453Combined sources
Helixi1246 – 126217Combined sources
Helixi1270 – 128011Combined sources
Helixi1286 – 131227Combined sources
Beta strandi1317 – 13193Combined sources
Turni1332 – 13343Combined sources
Beta strandi1340 – 13467Combined sources
Beta strandi1351 – 13577Combined sources
Helixi1359 – 13657Combined sources
Beta strandi1373 – 13764Combined sources
Helixi1380 – 13889Combined sources

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 annotationAdd
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 annotation
Contains 8 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG0457.
GeneTreeiENSGT00410000025758.
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_dom.
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]

Sequencei

Sequence statusi: Complete.

O15550-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKSCGVSLAT AAAAAAAFGD EEKKMAAGKA SGESEEASPS LTAEEREALG
60 70 80 90 100
GLDSRLFGFV RFHEDGARTK ALLGKAVRCY ESLILKAEGK VESDFFCQLG
110 120 130 140 150
HFNLLLEDYP KALSAYQRYY SLQSDYWKNA AFLYGLGLVY FHYNAFQWAI
160 170 180 190 200
KAFQEVLYVD PSFCRAKEIH LRLGLMFKVN TDYESSLKHF QLALVDCNPC
210 220 230 240 250
TLSNAEIQFH IAHLYETQRK YHSAKEAYEQ LLQTENLSAQ VKATVLQQLG
260 270 280 290 300
WMHHTVDLLG DKATKESYAI QYLQKSLEAD PNSGQSWYFL GRCYSSIGKV
310 320 330 340 350
QDAFISYRQS IDKSEASADT WCSIGVLYQQ QNQPMDALQA YICAVQLDHG
360 370 380 390 400
HAAAWMDLGT LYESCNQPQD AIKCYLNATR SKSCSNTSAL AARIKYLQAQ
410 420 430 440 450
LCNLPQGSLQ NKTKLLPSIE EAWSLPIPAE LTSRQGAMNT AQQNTSDNWS
460 470 480 490 500
GGHAVSHPPV QQQAHSWCLT PQKLQHLEQL RANRNNLNPA QKLMLEQLES
510 520 530 540 550
QFVLMQQHQM RPTGVAQVRS TGIPNGPTAD SSLPTNSVSG QQPQLALTRV
560 570 580 590 600
PSVSQPGVRP ACPGQPLANG PFSAGHVPCS TSRTLGSTDT ILIGNNHITG
610 620 630 640 650
SGSNGNVPYL QRNALTLPHN RTNLTSSAEE PWKNQLSNST QGLHKGQSSH
660 670 680 690 700
SAGPNGERPL SSTGPSQHLQ AAGSGIQNQN GHPTLPSNSV TQGAALNHLS
710 720 730 740 750
SHTATSGGQQ GITLTKESKP SGNILTVPET SRHTGETPNS TASVEGLPNH
760 770 780 790 800
VHQMTADAVC SPSHGDSKSP GLLSSDNPQL SALLMGKANN NVGTGTCDKV
810 820 830 840 850
NNIHPAVHTK TDNSVASSPS SAISTATPSP KSTEQTTTNS VTSLNSPHSG
860 870 880 890 900
LHTINGEGME ESQSPMKTDL LLVNHKPSPQ IIPSMSVSIY PSSAEVLKAC
910 920 930 940 950
RNLGKNGLSN SSILLDKCPP PRPPSSPYPP LPKDKLNPPT PSIYLENKRD
960 970 980 990 1000
AFFPPLHQFC TNPNNPVTVI RGLAGALKLD LGLFSTKTLV EANNEHMVEV
1010 1020 1030 1040 1050
RTQLLQPADE NWDPTGTKKI WHCESNRSHT TIAKYAQYQA SSFQESLREE
1060 1070 1080 1090 1100
NEKRSHHKDH SDSESTSSDN SGRRRKGPFK TIKFGTNIDL SDDKKWKLQL
1110 1120 1130 1140 1150
HELTKLPAFV RVVSAGNLLS HVGHTILGMN TVQLYMKVPG SRTPGHQENN
1160 1170 1180 1190 1200
NFCSVNINIG PGDCEWFVVP EGYWGVLNDF CEKNNLNFLM GSWWPNLEDL
1210 1220 1230 1240 1250
YEANVPVYRF IQRPGDLVWI NAGTVHWVQA IGWCNNIAWN VGPLTACQYK
1260 1270 1280 1290 1300
LAVERYEWNK LQSVKSIVPM VHLSWNMARN IKVSDPKLFE MIKYCLLRTL
1310 1320 1330 1340 1350
KQCQTLREAL IAAGKEIIWH GRTKEEPAHY CSICEVEVFD LLFVTNESNS
1360 1370 1380 1390 1400
RKTYIVHCQD CARKTSGNLE NFVVLEQYKM EDLMQVYDQF TLAPPLPSAS

S
Length:1,401
Mass (Da):154,177
Last modified:September 23, 2008 - v2
Checksum:i9DD7EA6C61E79229
GO

Experimental Info

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

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 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.
GeneTreei ENSGT00410000025758.
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

Bgeei O15550.
CleanExi HS_UTX.
ExpressionAtlasi O15550. baseline and differential.
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_dom.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 141 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