O15550 (KDM6A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	KDM6A
Synonyms:	UTX

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1401 AA.
Sequence status	Complete.
Protein existence	Evidence 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 MLL2/ALR or MLL3, ASH2L, RBBP5, WDR5, NCOA6, DPY30, KDM6A (or KDM6B), PAXIP1/PTIP, PAGR1 and alpha- and beta-tubulin. 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.10
Miscellaneous	Escapes X chromosome inactivation.
Sequence similarities	Belongs to the UTX family. Contains 1 JmjC domain. Contains 8 TPR repeats.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Disease	Mental retardation
Domain	Repeat TPR repeat
Ligand	Iron Metal-binding Zinc
Molecular function	Chromatin regulator Dioxygenase Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone H3-K4 methylation Inferred from sequence or structural similarity PubMed 17178841. Source: UniProtKB
Cellular_component	histone methyltransferase complex Inferred from direct assay Ref.5. Source: MGI
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1401

1401

Lysine-specific demethylase 6A

PRO_0000106409

Regions

Repeat

93 – 126

34

TPR 1

Repeat

130 – 163

34

TPR 2

Repeat

170 – 199

30

TPR 3

Repeat

205 – 238

34

TPR 4

Repeat

250 – 283

34

TPR 5

Repeat

284 – 317

34

TPR 6

Repeat

318 – 351

34

TPR 7

Repeat

352 – 385

34

TPR 8

Domain

1095 – 1258

164

JmjC

Compositional bias

9 – 17

9

Poly-Ala

Sites

Metal binding

1146

1

Iron

Metal binding

1148

1

Iron

Metal binding

1226

1

Iron

Metal binding

1331

1

Zinc

Metal binding

1334

1

Zinc

Metal binding

1358

1

Zinc

Metal binding

1361

1

Zinc

Amino acid modifications

Modified residue

769

1

Phosphoserine Ref.9

Modified residue

829

1

Phosphoserine Ref.9

Modified residue

1061

1

Phosphoserine By similarity

Natural variations

Natural variant

30

1

A → T.
Corresponds to variant rs6529 [ dbSNP | Ensembl ].

VAR_014492

Natural variant

270

1

I → V in a patient with chronic myelomonocytic leukemia. Ref.13

VAR_067225

Natural variant

497

1

Q → H.
Corresponds to variant rs6530 [ dbSNP | Ensembl ].

VAR_014493

Natural variant

581

1

T → A.
Corresponds to variant rs34922269 [ dbSNP | Ensembl ].

VAR_046527

Natural variant

726

1

T → K. Ref.4
Corresponds to variant rs2230018 [ dbSNP | Ensembl ].

VAR_020313

Natural variant

834

1

E → D in a patient with chronic myelomonocytic leukemia. Ref.13

VAR_067226

Natural variant

922

1

R → K in a patient with chronic myelomonocytic leukemia. Ref.13

VAR_067227

Natural variant

1106

1

L → R in a colorectal cancer sample; somatic mutation. Ref.12

VAR_035871

Experimental info

Mutagenesis

1146

1

H → A: Abolishes histone demethylase activity. Ref.6 Ref.7 Ref.8

Sequence conflict

173

1

L → V in AAC51839. Ref.1

Sequence conflict

173

1

L → V in AAC51840. Ref.1

Sequence conflict

585

1

L → R in AAC51839. Ref.1

Sequence conflict

585

1

L → R in AAC51840. Ref.1

Sequence conflict

601

1

S → N in AAC51839. Ref.1

Sequence conflict

601

1

S → N in AAC51840. Ref.1

Sequence conflict

629

1

E → K in AAC51839. Ref.1

Sequence conflict

629

1

E → K in AAC51840. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1401

Helix Strand Turn

Details...

Helix

893 – 900

8

Helix

933 – 935

3

Beta strand

942 – 944

3

Helix

948 – 951

4

Helix

954 – 961

8

Beta strand

966 – 971

6

Helix

973 – 977

5

Helix

981 – 984

4

Helix

986 – 992

7

Beta strand

997 – 1004

8

Beta strand

1016 – 1019

4

Beta strand

1025 – 1031

7

Helix

1032 – 1045

14

Beta strand

1081 – 1089

9

Turn

1093 – 1096

4

Helix

1097 – 1102

6

Helix

1103 – 1105

3

Helix

1108 – 1110

3

Helix

1118 – 1121

4

Beta strand

1122 – 1124

3

Turn

1127 – 1129

3

Beta strand

1133 – 1137

5

Beta strand

1142 – 1146

5

Helix

1149 – 1151

3

Beta strand

1153 – 1162

10

Beta strand

1164 – 1169

6

Helix

1171 – 1173

3

Helix

1174 – 1183

10

Turn

1188 – 1190

3

Helix

1197 – 1202

6

Beta strand

1208 – 1212

5

Beta strand

1217 – 1220

4

Beta strand

1225 – 1241

17

Beta strand

1243 – 1245

3

Helix

1246 – 1262

17

Helix

1270 – 1280

11

Helix

1286 – 1312

27

Beta strand

1317 – 1319

3

Turn

1332 – 1334

3

Beta strand

1340 – 1346

7

Beta strand

1351 – 1357

7

Helix

1359 – 1365

7

Beta strand

1373 – 1376

4

Helix

1380 – 1388

9

Sequences

	Sequence		Length	Mass (Da)
	O15550 [UniParc]. Last modified September 23, 2008. Version 2. Checksum: 9DD7EA6C61E79229	FASTA	1,401	154,177
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"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.
[11]	"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.
[12]	"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. , 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.
[13]	"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.

IPI

IPI01012755.

PIR

T02255.

RefSeq

NP_066963.2. NM_021140.2.

UniGene

Hs.522616.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3AVR	X-ray	1.80	A	880-1401	[»]
3AVS	X-ray	1.85	A	880-1401	[»]

ProteinModelPortal

O15550.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46192N.

IntAct

O15550. 9 interactions.

MINT

MINT-1188304.

STRING

9606.ENSP00000367203.

PTM databases

PhosphoSite

O15550.

Proteomic databases

PaxDb

O15550.

PRIDE

O15550.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000377967; ENSP00000367203; ENSG00000147050.

GeneID

7403.

KEGG

hsa:7403.

UCSC

uc004dge.4. human.

Organism-specific databases

CTD

7403.

GeneCards

GC0XP044732.

H-InvDB

HIX0019137.

HGNC

HGNC:12637. KDM6A.

HPA

HPA000568.
HPA002111.

MIM

300128. gene.
300867. phenotype.

neXtProt

NX_O15550.

Orphanet

2322. Kabuki syndrome.

PharmGKB

PA37262.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0457.

InParanoid

O15550.

KO

K11447.

OrthoDB

EOG4M91QN.

PhylomeDB

O15550.

Gene expression databases

ArrayExpress

O15550.

Bgee

O15550.

CleanEx

HS_UTX.

Genevestigator

O15550.

GermOnline

ENSG00000147050. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.10. 1 hit.

InterPro

IPR003347. JmjC_dom.
IPR001440. TPR-1.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]

Pfam

PF02373. JmjC. 1 hit.
PF00515. TPR_1. 3 hits.
PF13181. TPR_8. 1 hit.
[Graphical view]

SMART

SM00558. JmjC. 1 hit.
SM00028. TPR. 6 hits.
[Graphical view]

PROSITE

PS51184. JMJC. 1 hit.
PS50005. TPR. 7 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

KDM6A. human.

GenomeRNAi

7403.

NextBio

28980.

SOURCE

Search...

Entry information

Entry name

KDM6A_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.