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O15550 (KDM6A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:KDM6A
Synonyms:UTX
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1401 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.6 Ref.8

Cofactor

Ascorbate. Ref.8

Fe2+. Ref.8

Subunit structure

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. Ref.5 Ref.8

Subcellular location

Nucleus Probable.

Involvement in disease

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. Ref.11

Miscellaneous

Escapes X chromosome inactivation.

Sequence similarities

Belongs to the UTX family.

Contains 1 JmjC domain.

Contains 8 TPR repeats.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DiseaseMental retardation
   DomainRepeat
TPR repeat
   LigandIron
Metal-binding
Zinc
   Molecular functionChromatin regulator
Dioxygenase
Oxidoreductase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcanonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from electronic annotation. Source: Ensembl

histone H3-K4 methylation

Inferred from sequence or structural similarity PubMed 17178841. Source: UniProtKB

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

mesodermal cell differentiation

Inferred from electronic annotation. Source: Ensembl

neural tube closure

Inferred from electronic annotation. Source: Ensembl

notochord morphogenesis

Inferred from electronic annotation. Source: Ensembl

respiratory system process

Inferred from electronic annotation. Source: Ensembl

somite rostral/caudal axis specification

Inferred from electronic annotation. Source: Ensembl

   Cellular_componenthistone methyltransferase complex

Inferred from direct assay Ref.5. Source: MGI

nucleus

Inferred from direct assay Ref.5. Source: MGI

   Molecular_functionRNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

dioxygenase activity

Inferred from electronic annotation. Source: UniProtKB-KW

histone demethylase activity (H3-K27 specific)

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14011401Lysine-specific demethylase 6A
PRO_0000106409

Regions

Repeat93 – 12634TPR 1
Repeat130 – 16334TPR 2
Repeat170 – 19930TPR 3
Repeat205 – 23834TPR 4
Repeat250 – 28334TPR 5
Repeat284 – 31734TPR 6
Repeat318 – 35134TPR 7
Repeat352 – 38534TPR 8
Domain1095 – 1258164JmjC
Region1 – 10951095Interaction with SUPT6H By similarity
Compositional bias9 – 179Poly-Ala

Sites

Metal binding11461Iron
Metal binding11481Iron
Metal binding12261Iron
Metal binding13311Zinc
Metal binding13341Zinc
Metal binding13581Zinc
Metal binding13611Zinc

Amino acid modifications

Modified residue7691Phosphoserine Ref.10
Modified residue8291Phosphoserine Ref.10

Natural variations

Natural variant301A → T.
Corresponds to variant rs6529 [ dbSNP | Ensembl ].
VAR_014492
Natural variant2701I → V in a patient with chronic myelomonocytic leukemia. Ref.14
VAR_067225
Natural variant4971Q → H.
Corresponds to variant rs6530 [ dbSNP | Ensembl ].
VAR_014493
Natural variant5811T → A.
Corresponds to variant rs34922269 [ dbSNP | Ensembl ].
VAR_046527
Natural variant7261T → K. Ref.4
Corresponds to variant rs2230018 [ dbSNP | Ensembl ].
VAR_020313
Natural variant8341E → D in a patient with chronic myelomonocytic leukemia. Ref.14
VAR_067226
Natural variant9221R → K in a patient with chronic myelomonocytic leukemia. Ref.14
VAR_067227
Natural variant11061L → R in a colorectal cancer sample; somatic mutation. Ref.13
VAR_035871

Experimental info

Mutagenesis11461H → A: Abolishes histone demethylase activity. Ref.6 Ref.7 Ref.8
Sequence conflict1731L → V in AAC51839. Ref.1
Sequence conflict1731L → V in AAC51840. Ref.1
Sequence conflict5851L → R in AAC51839. Ref.1
Sequence conflict5851L → R in AAC51840. Ref.1
Sequence conflict6011S → N in AAC51839. Ref.1
Sequence conflict6011S → N in AAC51840. Ref.1
Sequence conflict6291E → K in AAC51839. Ref.1
Sequence conflict6291E → K in AAC51840. Ref.1

Secondary structure

................................................................................... 1401
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O15550 [UniParc].

Last modified September 23, 2008. Version 2.
Checksum: 9DD7EA6C61E79229

FASTA1,401154,177
        10         20         30         40         50         60 
MKSCGVSLAT AAAAAAAFGD EEKKMAAGKA SGESEEASPS LTAEEREALG GLDSRLFGFV 

        70         80         90        100        110        120 
RFHEDGARTK ALLGKAVRCY ESLILKAEGK VESDFFCQLG HFNLLLEDYP KALSAYQRYY 

       130        140        150        160        170        180 
SLQSDYWKNA AFLYGLGLVY FHYNAFQWAI KAFQEVLYVD PSFCRAKEIH LRLGLMFKVN 

       190        200        210        220        230        240 
TDYESSLKHF QLALVDCNPC TLSNAEIQFH IAHLYETQRK YHSAKEAYEQ LLQTENLSAQ 

       250        260        270        280        290        300 
VKATVLQQLG WMHHTVDLLG DKATKESYAI QYLQKSLEAD PNSGQSWYFL GRCYSSIGKV 

       310        320        330        340        350        360 
QDAFISYRQS IDKSEASADT WCSIGVLYQQ QNQPMDALQA YICAVQLDHG HAAAWMDLGT 

       370        380        390        400        410        420 
LYESCNQPQD AIKCYLNATR SKSCSNTSAL AARIKYLQAQ LCNLPQGSLQ NKTKLLPSIE 

       430        440        450        460        470        480 
EAWSLPIPAE LTSRQGAMNT AQQNTSDNWS GGHAVSHPPV QQQAHSWCLT PQKLQHLEQL 

       490        500        510        520        530        540 
RANRNNLNPA QKLMLEQLES QFVLMQQHQM RPTGVAQVRS TGIPNGPTAD SSLPTNSVSG 

       550        560        570        580        590        600 
QQPQLALTRV PSVSQPGVRP ACPGQPLANG PFSAGHVPCS TSRTLGSTDT ILIGNNHITG 

       610        620        630        640        650        660 
SGSNGNVPYL QRNALTLPHN RTNLTSSAEE PWKNQLSNST QGLHKGQSSH SAGPNGERPL 

       670        680        690        700        710        720 
SSTGPSQHLQ AAGSGIQNQN GHPTLPSNSV TQGAALNHLS SHTATSGGQQ GITLTKESKP 

       730        740        750        760        770        780 
SGNILTVPET SRHTGETPNS TASVEGLPNH VHQMTADAVC SPSHGDSKSP GLLSSDNPQL 

       790        800        810        820        830        840 
SALLMGKANN NVGTGTCDKV NNIHPAVHTK TDNSVASSPS SAISTATPSP KSTEQTTTNS 

       850        860        870        880        890        900 
VTSLNSPHSG LHTINGEGME ESQSPMKTDL LLVNHKPSPQ IIPSMSVSIY PSSAEVLKAC 

       910        920        930        940        950        960 
RNLGKNGLSN SSILLDKCPP PRPPSSPYPP LPKDKLNPPT PSIYLENKRD AFFPPLHQFC 

       970        980        990       1000       1010       1020 
TNPNNPVTVI RGLAGALKLD LGLFSTKTLV EANNEHMVEV RTQLLQPADE NWDPTGTKKI 

      1030       1040       1050       1060       1070       1080 
WHCESNRSHT TIAKYAQYQA SSFQESLREE NEKRSHHKDH SDSESTSSDN SGRRRKGPFK 

      1090       1100       1110       1120       1130       1140 
TIKFGTNIDL SDDKKWKLQL HELTKLPAFV RVVSAGNLLS HVGHTILGMN TVQLYMKVPG 

      1150       1160       1170       1180       1190       1200 
SRTPGHQENN NFCSVNINIG PGDCEWFVVP EGYWGVLNDF CEKNNLNFLM GSWWPNLEDL 

      1210       1220       1230       1240       1250       1260 
YEANVPVYRF IQRPGDLVWI NAGTVHWVQA IGWCNNIAWN VGPLTACQYK LAVERYEWNK 

      1270       1280       1290       1300       1310       1320 
LQSVKSIVPM VHLSWNMARN IKVSDPKLFE MIKYCLLRTL KQCQTLREAL IAAGKEIIWH 

      1330       1340       1350       1360       1370       1380 
GRTKEEPAHY CSICEVEVFD LLFVTNESNS RKTYIVHCQD CARKTSGNLE NFVVLEQYKM 

      1390       1400 
EDLMQVYDQF TLAPPLPSAS S 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A histone H3 lysine 27 demethylase regulates animal posterior development."
Lan F., Bayliss P.E., Rinn J.L., Whetstine J.R., Wang J.K., Chen S., Iwase S., Alpatov R., Issaeva I., Canaani E., Roberts T.M., Chang H.Y., Shi Y.
Nature 449:689-694(2007) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT02255.
RefSeqNP_066963.2. NM_021140.2.
UniGeneHs.522616.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3AVRX-ray1.80A880-1401[»]
3AVSX-ray1.85A880-1401[»]
ProteinModelPortalO15550.
SMRO15550. Positions 108-378, 886-1395.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113246. 23 interactions.
DIPDIP-46192N.
IntActO15550. 11 interactions.
MINTMINT-1188304.
STRING9606.ENSP00000367203.

Chemistry

ChEMBLCHEMBL2069164.

PTM databases

PhosphoSiteO15550.

Proteomic databases

PaxDbO15550.
PRIDEO15550.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000377967; ENSP00000367203; ENSG00000147050.
GeneID7403.
KEGGhsa:7403.
UCSCuc004dge.4. human.

Organism-specific databases

CTD7403.
GeneCardsGC0XP044732.
H-InvDBHIX0019137.
HGNCHGNC:12637. KDM6A.
HPAHPA000568.
HPA002111.
MIM300128. gene.
300867. phenotype.
neXtProtNX_O15550.
Orphanet2322. Kabuki syndrome.
PharmGKBPA37262.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0457.
InParanoidO15550.
KOK11447.
OrthoDBEOG7CG6Z5.
PhylomeDBO15550.
TreeFamTF317405.

Gene expression databases

ArrayExpressO15550.
BgeeO15550.
CleanExHS_UTX.
GenevestigatorO15550.

Family and domain databases

Gene3D1.25.40.10. 1 hit.
InterProIPR003347. JmjC_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamPF02373. JmjC. 1 hit.
PF00515. TPR_1. 3 hits.
PF13181. TPR_8. 1 hit.
[Graphical view]
SMARTSM00558. JmjC. 1 hit.
SM00028. TPR. 6 hits.
[Graphical view]
PROSITEPS51184. JMJC. 1 hit.
PS50005. TPR. 7 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKDM6A. human.
GeneWikiUTX_(gene).
GenomeRNAi7403.
NextBio28980.
PROO15550.
SOURCESearch...

Entry information

Entry nameKDM6A_HUMAN
AccessionPrimary (citable) accession number: O15550
Secondary accession number(s): Q52LL9, Q5JVQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: September 23, 2008
Last modified: April 16, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM