SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O15550

- KDM6A_HUMAN

UniProt

O15550 - KDM6A_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Lysine-specific demethylase 6A

Gene
KDM6A, UTX
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 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
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 Inferred

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

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.2 Publications

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.

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 – 1258164JmjCAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 10951095Interaction with SUPT6H By similarityAdd
BLAST

Compositional bias

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

Sequence similaritiesi

Belongs to the UTX family.
Contains 1 JmjC domain.
Contains 8 TPR repeats.

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]

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. 1 Publication
Sequence conflicti173 – 1731L → V in AAC51840. 1 Publication
Sequence conflicti585 – 5851L → R in AAC51839. 1 Publication
Sequence conflicti585 – 5851L → R in AAC51840. 1 Publication
Sequence conflicti601 – 6011S → N in AAC51839. 1 Publication
Sequence conflicti601 – 6011S → N in AAC51840. 1 Publication
Sequence conflicti629 – 6291E → K in AAC51839. 1 Publication
Sequence conflicti629 – 6291E → K in AAC51840. 1 Publication

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

« 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: September 3, 2014
This is version 139 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

Similar proteinsi