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Q92794 (KAT6A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 155. 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·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone acetyltransferase KAT6A

EC=2.3.1.48
Alternative name(s):
MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3
Short name=MYST-3
Monocytic leukemia zinc finger protein
Runt-related transcription factor-binding protein 2
Zinc finger protein 220
Gene names
Name:KAT6A
Synonyms:MOZ, MYST3, RUNXBP2, ZNF220
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2004 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Histone acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May act as a transcriptional coactivator for RUNX1 and RUNX2. Acetylates p53/TP53 at 'Lys-120' and 'Lys-382' and controls its transcriptional activity via association with PML. Ref.6 Ref.8 Ref.10 Ref.12 Ref.19 Ref.21

Catalytic activity

Acetyl-CoA + [histone] = CoA + acetyl-[histone]. Ref.6 Ref.7 Ref.21

Subunit structure

Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3. Interacts with RUNX1; phosphorylation of RUNX1 enhances the interaction. Interacts with RUNX2. Interacts with p53/TP53. Interacts with PML (isoform PML-4)and this interaction positively regulates its acetylation activity towards p53/TP53. Ref.6 Ref.8 Ref.12 Ref.14 Ref.19

Subcellular location

Nucleus. Nucleusnucleolus. Nucleusnucleoplasm. NucleusPML body. Note: Recruited into PML body after DNA damage. Ref.6 Ref.11 Ref.14

Domain

The N-terminus is involved in transcriptional activation while the C-terminus is involved in transcriptional repression. Ref.7

Post-translational modification

Autoacetylation at Lys-604 is required for proper function By similarity. Autoacetylated. Ref.6

Phosphorylation at Thr-369 by PKB/AKT1 inhibits its interaction with PML and negatively regulates its acetylation activity towards p53/TP53. Ref.6

Involvement in disease

Chromosomal aberrations involving KAT6A may be a cause of acute myeloid leukemias. Translocation t(8;16)(p11;p13) with CREBBP; translocation t(8;22)(p11;q13) with EP300. KAT6A-CREBBP may induce leukemia by inhibiting RUNX1-mediated transcription. Inversion inv8(p11;q13) generates the KAT6A-NCOA2 oncogene, which consists of the N-terminal part of KAT6A and the C-terminal part of NCOA2/TIF2. KAT6A-NCOA2 binds to CREBBP and disrupts its function in transcription activation.

A chromosomal aberration involving KAT6A is a cause of therapy-related myelodysplastic syndrome. Translocation t(2;8)(p23;p11.2) with ASXL2 generates a KAT6A-ASXL2 fusion protein.

Sequence similarities

Belongs to the MYST (SAS/MOZ) family.

Contains 1 C2HC-type zinc finger.

Contains 1 H15 (linker histone H1/H5 globular) domain.

Contains 2 PHD-type zinc fingers.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityChromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionActivator
Acyltransferase
Chromatin regulator
Repressor
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA packaging

Traceable author statement Ref.1. Source: ProtInc

aorta morphogenesis

Inferred from electronic annotation. Source: Ensembl

cellular senescence

Inferred from mutant phenotype Ref.19. Source: UniProtKB

chromatin organization

Traceable author statement. Source: Reactome

embryonic hemopoiesis

Inferred from electronic annotation. Source: Ensembl

face morphogenesis

Inferred from electronic annotation. Source: Ensembl

heart morphogenesis

Inferred from electronic annotation. Source: Ensembl

histone H3 acetylation

Inferred from direct assay Ref.12. Source: UniProtKB

histone acetylation

Inferred from direct assay Ref.6Ref.21. Source: UniProtKB

myeloid cell differentiation

Inferred from direct assay Ref.6. Source: UniProtKB

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.6. Source: UniProtKB

nucleosome assembly

Inferred from electronic annotation. Source: InterPro

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.6Ref.8Ref.14. Source: UniProtKB

protein acetylation

Inferred from direct assay Ref.19. Source: UniProtKB

somatic stem cell maintenance

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

MOZ/MORF histone acetyltransferase complex

Inferred from direct assay Ref.12Ref.14. Source: UniProtKB

PML body

Inferred from direct assay Ref.19. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleosome

Inferred from electronic annotation. Source: InterPro

nucleus

Inferred from direct assay Ref.6Ref.14. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay Ref.21. Source: UniProtKB

acetyltransferase activity

Inferred from direct assay Ref.6. Source: UniProtKB

chromatin binding

Inferred from electronic annotation. Source: Ensembl

histone acetyltransferase activity

Inferred from direct assay Ref.6Ref.21. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.6Ref.8Ref.19. Source: UniProtKB

transcription coactivator activity

Traceable author statement Ref.14. Source: UniProtKB

transcription factor binding

Inferred from direct assay Ref.6Ref.8. Source: UniProtKB

zinc ion binding

Inferred from direct assay Ref.21. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

KMT2AQ0316410EBI-948013,EBI-2638616
WDR5P619644EBI-948013,EBI-540834

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20042004Histone acetyltransferase KAT6A
PRO_0000051572

Regions

Domain95 – 17177H15
Zinc finger206 – 26560PHD-type 1
Zinc finger259 – 31355PHD-type 2
Zinc finger538 – 56023C2HC-type
Region1 – 144144Required for activation of RUNX1-1
Region52 – 166115Required for nuclear localization
Region144 – 664521Interaction with PML
Region312 – 664353Interaction with RUNX1-1
Region488 – 778291Catalytic
Region507 – 810304Mediates interaction with BRPF1, required for histone H3 acetyltransferase activity
Region645 – 6495Acetyl-CoA binding
Region654 – 6607Acetyl-CoA binding
Region1517 – 1741225Interaction with PML
Region1517 – 1642126Interaction with RUNX1-2
Region1913 – 194836Required for activation of RUNX1-2
Compositional bias371 – 3799Poly-Ser
Compositional bias788 – 80114Poly-Glu
Compositional bias989 – 9957Poly-Glu
Compositional bias1019 – 10268Poly-Arg
Compositional bias1069 – 107810Poly-Glu
Compositional bias1147 – 11504Poly-Lys
Compositional bias1221 – 124222Glu-rich
Compositional bias1267 – 130236Glu-rich
Compositional bias1411 – 14144Poly-Glu
Compositional bias1593 – 15975Poly-Ser
Compositional bias1643 – 170462Gln/Pro-rich
Compositional bias1897 – 197781Met-rich

Sites

Active site6041 By similarity
Active site6461Nucleophile By similarity
Binding site6841Acetyl-CoA
Site813 – 8142Breakpoint for translocation to form KAT6A-ASXL2
Site1117 – 11182Breakpoint for translocation to form KAT6A-EP300 and KAT6A-NCOA2
Site1546 – 15472Breakpoint for translocation to form KAT6A-CREBBP

Amino acid modifications

Modified residue1721N6-acetyllysine By similarity
Modified residue3501N6-acetyllysine Ref.17
Modified residue3551N6-acetyllysine Ref.17
Modified residue3691Phosphothreonine; by PKB/AKT1 Ref.19
Modified residue4731Phosphoserine Ref.18
Modified residue6041N6-acetyllysine; by autocatalysis By similarity
Modified residue8151N6-acetyllysine By similarity
Modified residue8991Phosphotyrosine By similarity
Modified residue10071N6-acetyllysine Ref.17
Modified residue11131Phosphoserine Ref.15 Ref.16 Ref.18

Natural variations

Natural variant1341L → S.
Corresponds to variant rs3824276 [ dbSNP | Ensembl ].
VAR_047548

Experimental info

Mutagenesis5431C → G: Abrogates HAT activity. Ref.9
Mutagenesis5451K → A: Reduced affinity for DNA. Ref.21
Mutagenesis6571G → E: Abrogates HAT activity. Ref.9
Mutagenesis7271I → E: Slightly reduced affinity for DNA. Ref.21
Mutagenesis7321H → D: Reduced affinity for DNA. Ref.21
Sequence conflict4011K → R in AAC50662. Ref.1
Sequence conflict4011K → R in BAD00088. Ref.3

Secondary structure

...................................................................... 2004
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q92794 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 78357EFAC4698A5F

FASTA2,004225,028
        10         20         30         40         50         60 
MVKLANPLYT EWILEAIKKV KKQKQRPSEE RICNAVSSSH GLDRKTVLEQ LELSVKDGTI 

        70         80         90        100        110        120 
LKVSNKGLNS YKDPDNPGRI ALPKPRNHGK LDNKQNVDWN KLIKRAVEGL AESGGSTLKS 

       130        140        150        160        170        180 
IERFLKGQKD VSALFGGSAA SGFHQQLRLA IKRAIGHGRL LKDGPLYRLN TKATNVDGKE 

       190        200        210        220        230        240 
SCESLSCLPP VSLLPHEKDK PVAEPIPICS FCLGTKEQNR EKKPEELISC ADCGNSGHPS 

       250        260        270        280        290        300 
CLKFSPELTV RVKALRWQCI ECKTCSSCRD QGKNADNMLF CDSCDRGFHM ECCDPPLTRM 

       310        320        330        340        350        360 
PKGMWICQIC RPRKKGRKLL QKKAAQIKRR YTNPIGRPKN RLKKQNTVSK GPFSKVRTGP 

       370        380        390        400        410        420 
GRGRKRKITL SSQSASSSSE EGYLERIDGL DFCRDSNVSL KFNKKTKGLI DGLTKFFTPS 

       430        440        450        460        470        480 
PDGRKARGEV VDYSEQYRIR KRGNRKSSTS DWPTDNQDGW DGKQENEERL FGSQEIMTEK 

       490        500        510        520        530        540 
DMELFRDIQE QALQKVGVTG PPDPQVRCPS VIEFGKYEIH TWYSSPYPQE YSRLPKLYLC 

       550        560        570        580        590        600 
EFCLKYMKSR TILQQHMKKC GWFHPPANEI YRKNNISVFE VDGNVSTIYC QNLCLLAKLF 

       610        620        630        640        650        660 
LDHKTLYYDV EPFLFYVLTQ NDVKGCHLVG YFSKEKHCQQ KYNVSCIMIL PQYQRKGYGR 

       670        680        690        700        710        720 
FLIDFSYLLS KREGQAGSPE KPLSDLGRLS YMAYWKSVIL ECLYHQNDKQ ISIKKLSKLT 

       730        740        750        760        770        780 
GICPQDITST LHHLRMLDFR SDQFVIIRRE KLIQDHMAKL QLNLRPVDVD PECLRWTPVI 

       790        800        810        820        830        840 
VSNSVVSEEE EEEAEEGENE EPQCQERELE ISVGKSVSHE NKEQDSYSVE SEKKPEVMAP 

       850        860        870        880        890        900 
VSSTRLSKQV LPHDSLPANS QPSRRGRWGR KNRKTQERFG DKDSKLLLEE TSSAPQEQYG 

       910        920        930        940        950        960 
ECGEKSEATQ EQYTESEEQL VASEEQPSQD GKPDLPKRRL SEGVEPWRGQ LKKSPEALKC 

       970        980        990       1000       1010       1020 
RLTEGSERLP RRYSEGDRAV LRGFSESSEE EEEPESPRSS SPPILTKPTL KRKKPFLHRR 

      1030       1040       1050       1060       1070       1080 
RRVRKRKHHN SSVVTETISE TTEVLDEPFE DSDSERPMPR LEPTFEIDEE EEEEDENELF 

      1090       1100       1110       1120       1130       1140 
PREYFRRLSS QDVLRCQSSS KRKSKDEEED EESDDADDTP ILKPVSLLRK RDVKNSPLEP 

      1150       1160       1170       1180       1190       1200 
DTSTPLKKKK GWPKGKSRKP IHWKKRPGRK PGFKLSREIM PVSTQACVIE PIVSIPKAGR 

      1210       1220       1230       1240       1250       1260 
KPKIQESEET VEPKEDMPLP EERKEEEEMQ AEAEEAEEGE EEDAASSEVP AASPADSSNS 

      1270       1280       1290       1300       1310       1320 
PETETKEPEV EEEEEKPRVS EEQRQSEEEQ QELEEPEPEE EEDAAAETAQ NDDHDADDED 

      1330       1340       1350       1360       1370       1380 
DGHLESTKKK ELEEQPTRED VKEEPGVQES FLDANMQKSR EKIKDKEETE LDSEEEQPSH 

      1390       1400       1410       1420       1430       1440 
DTSVVSEQMA GSEDDHEEDS HTKEELIELK EEEEIPHSEL DLETVQAVQS LTQEESSEHE 

      1450       1460       1470       1480       1490       1500 
GAYQDCEETL AACQTLQSYT QADEDPQMSM VEDCHASEHN SPISSVQSHP SQSVRSVSSP 

      1510       1520       1530       1540       1550       1560 
NVPALESGYT QISPEQGSLS APSMQNMETS PMMDVPSVSD HSQQVVDSGF SDLGSIESTT 

      1570       1580       1590       1600       1610       1620 
ENYENPSSYD STMGGSICGN SSSQSSCSYG GLSSSSSLTQ SSCVVTQQMA SMGSSCSMMQ 

      1630       1640       1650       1660       1670       1680 
QSSVQPAANC SIKSPQSCVV ERPPSNQQQQ PPPPPPQQPQ PPPPQPQPAP QPPPPQQQPQ 

      1690       1700       1710       1720       1730       1740 
QQPQPQPQQP PPPPPPQQQP PLSQCSMNNS FTPAPMIMEI PESGSTGNIS IYERIPGDFG 

      1750       1760       1770       1780       1790       1800 
AGSYSQPSAT FSLAKLQQLT NTIMDPHAMP YSHSPAVTSY ATSVSLSNTG LAQLAPSHPL 

      1810       1820       1830       1840       1850       1860 
AGTPQAQATM TPPPNLASTT MNLTSPLLQC NMSATNIGIP HTQRLQGQMP VKGHISIRSK 

      1870       1880       1890       1900       1910       1920 
SAPLPSAAAH QQQLYGRSPS AVAMQAGPRA LAVQRGMNMG VNLMPTPAYN VNSMNMNTLN 

      1930       1940       1950       1960       1970       1980 
AMNSYRMTQP MMNSSYHSNP AYMNQTAQYP MQMQMGMMGS QAYTQQPMQP NPHGNMMYTG 

      1990       2000 
PSHHSYMNAA GVPKQSLNGP YMRR 

« Hide

References

« Hide 'large scale' references
[1]"The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein."
Borrow J., Stanton V.P. Jr., Andresen J.M., Becher R., Behm F.G., Chaganti R.S.K., Civin C.I., Disteche C., Dube I., Frischauf A.M., Horsman D., Mitelman F., Volinia S., Watmore A.E., Housman D.E.
Nat. Genet. 14:33-41(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHROMOSOMAL TRANSLOCATION WITH CREBBP.
[2]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"MOZ is fused to a novel Polycomb group gene in a therapy-related myelodysplastic syndrome with t(2;8)(p23;p11.2)."
Hosoda F., Kitabayashi I., Kakazu N., Fukushima M., Aikawa Y., Abe T., Hibi S., Yagi T., Ohki M.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-813, CHROMOSOMAL TRANSLOCATION WITH ASXL2.
Tissue: Bone marrow.
[4]"A novel fusion between MOZ and the nuclear receptor coactivator TIF2 in acute myeloid leukemia."
Carapeti M., Aguiar R.C.T., Goldman J.M., Cross N.C.P.
Blood 91:3127-3133(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1089-1117, CHROMOSOMAL TRANSLOCATION WITH NCOA2.
[5]"MOZ is fused to p300 in an acute monocytic leukemia with t(8;22)."
Chaffanet M., Gressin L., Preudhomme C., Soenen-Cornu V., Birnbaum D., Pebusque M.-J.
Genes Chromosomes Cancer 28:138-144(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1111-1128, CHROMOSOMAL TRANSLOCATION WITH EP300.
[6]"Activation of AML1-mediated transcription by MOZ and inhibition by the MOZ-CBP fusion protein."
Kitabayashi I., Aikawa Y., Nguyen L.A., Yokoyama A., Ohki M.
EMBO J. 20:7184-7196(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RUNX1, SUBCELLULAR LOCATION, ENZYME ACTIVITY, ACETYLATION, CHROMOSOMAL TRANSLOCATION WITH CREBBP, FUNCTION.
[7]"The monocytic leukemia zinc finger protein MOZ is a histone acetyltransferase."
Champagne N., Pelletier N., Yang X.-J.
Oncogene 20:404-409(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY, DOMAIN.
[8]"MOZ and MORF histone acetyltransferases interact with the Runt-domain transcription factor Runx2."
Pelletier N., Champagne N., Stifani S., Yang X.-J.
Oncogene 21:2729-2740(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RUNX2, FUNCTION.
[9]"MOZ-TIF2-induced acute myeloid leukemia requires the MOZ nucleosome binding motif and TIF2-mediated recruitment of CBP."
Deguchi K., Ayton P.M., Carapeti M., Kutok J.L., Snyder C.S., Williams I.R., Cross N.C.P., Glass C.K., Cleary M.L., Gilliland D.G.
Cancer Cell 3:259-271(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH NCOA2, MUTAGENESIS OF CYS-543 AND GLY-657.
[10]"Transcriptional regulation of the human MIP-1alpha promoter by RUNX1 and MOZ."
Bristow C.A.P., Shore P.
Nucleic Acids Res. 31:2735-2744(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"MOZ-TIF2 inhibits transcription by nuclear receptors and p53 by impairment of CBP function."
Kindle K.B., Troke P.J.F., Collins H.M., Matsuda S., Bossi D., Bellodi C., Kalkhoven E., Salomoni P., Pelicci P.G., Minucci S., Heery D.M.
Mol. Cell. Biol. 25:988-1002(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, CHROMOSOMAL TRANSLOCATION WITH NCOA2.
[12]"ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation."
Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J.
Mol. Cell 21:51-64(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE MOZ/MORF COMPLEX.
[13]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[14]"Molecular architecture of quartet MOZ/MORF histone acetyltransferase complexes."
Ullah M., Pelletier N., Xiao L., Zhao S.P., Wang K., Degerny C., Tahmasebi S., Cayrou C., Doyon Y., Goh S.-L., Champagne N., Cote J., Yang X.-J.
Mol. Cell. Biol. 28:6828-6843(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE MOZ/MORF COMPLEX, INTERACTION WITH BRPF1, SUBCELLULAR LOCATION.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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-1113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-350; LYS-355 AND LYS-1007, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473 AND SER-1113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"MOZ increases p53 acetylation and premature senescence through its complex formation with PML."
Rokudai S., Laptenko O., Arnal S.M., Taya Y., Kitabayashi I., Prives C.
Proc. Natl. Acad. Sci. U.S.A. 110:3895-3900(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PML AND TP53, PHOSPHORYLATION AT THR-369.
[20]"Solution structure of a CCCCCHC zinc finger from MOZ."
Kwan A.H.Y., Gell D.A., Liew C.K., Mackay J.P.
Submitted (JUN-2002) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 531-563.
[21]"The human monocytic leukemia zinc finger histone acetyltransferase domain contains DNA-binding activity implicated in chromatin targeting."
Holbert M.A., Sikorski T., Carten J., Snowflack D., Hodawadekar S., Marmorstein R.
J. Biol. Chem. 282:36603-36613(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 501-784 IN COMPLEXES WITH ACETYL COENZYME A; HISTONE H3 AND HISTONE H4 AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY, DNA-BINDING, MUTAGENESIS OF LYS-545; ILE-727 AND HIS-732.
[22]"The crystal structure of human MYST histone acetyltransferase 3 in complex with acetylcoenzyme A."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 497-780 IN COMPLEX WITH ACETYLCOENZYME A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U47742 mRNA. Translation: AAC50662.1.
AC090571 Genomic DNA. No translation available.
AB084281 mRNA. Translation: BAD00088.1. Different termination.
CCDSCCDS6124.1.
RefSeqNP_001092882.1. NM_001099412.1.
NP_001092883.1. NM_001099413.1.
NP_006757.2. NM_006766.3.
UniGeneHs.491577.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M36NMR-A533-563[»]
2LN0NMR-A204-313[»]
2OZUX-ray2.30A497-780[»]
2RC4X-ray3.00A501-784[»]
3V43X-ray1.47A204-313[»]
4LJNX-ray3.00A194-323[»]
4LK9X-ray1.60A194-323[»]
4LKAX-ray1.61A194-323[»]
4LLBX-ray2.50A/B194-323[»]
ProteinModelPortalQ92794.
SMRQ92794. Positions 204-313, 507-779.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113703. 30 interactions.
IntActQ92794. 6 interactions.
STRING9606.ENSP00000265713.

PTM databases

PhosphoSiteQ92794.

Polymorphism databases

DMDM215274095.

Proteomic databases

MaxQBQ92794.
PaxDbQ92794.
PRIDEQ92794.

Protocols and materials databases

DNASU7994.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265713; ENSP00000265713; ENSG00000083168.
ENST00000396930; ENSP00000380136; ENSG00000083168.
ENST00000406337; ENSP00000385888; ENSG00000083168.
GeneID7994.
KEGGhsa:7994.
UCSCuc003xon.4. human.

Organism-specific databases

CTD7994.
GeneCardsGC08M041786.
HGNCHGNC:13013. KAT6A.
HPACAB017023.
HPA049811.
HPA053523.
MIM601408. gene.
neXtProtNX_Q92794.
Orphanet370026. Acute myeloid leukemia with t(8;16)(p11;p13) translocation.
PharmGKBPA37592.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5027.
HOGENOMHOG000234365.
HOVERGENHBG052563.
InParanoidQ92794.
KOK11305.
OMAGAYQDCE.
OrthoDBEOG7WHH8N.
PhylomeDBQ92794.
TreeFamTF106483.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.

Gene expression databases

ArrayExpressQ92794.
BgeeQ92794.
CleanExHS_MYST3.
GenevestigatorQ92794.

Family and domain databases

Gene3D3.30.40.10. 2 hits.
3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR005818. Histone_H1/H5_H15.
IPR002717. MOZ_SAS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF01853. MOZ_SAS. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTSM00526. H15. 1 hit.
SM00249. PHD. 2 hits.
SM00184. RING. 2 hits.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
SSF57903. SSF57903. 2 hits.
PROSITEPS51504. H15. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKAT6A. human.
EvolutionaryTraceQ92794.
GeneWikiMYST3.
GenomeRNAi7994.
NextBio30540.
PROQ92794.
SOURCESearch...

Entry information

Entry nameKAT6A_HUMAN
AccessionPrimary (citable) accession number: Q92794
Secondary accession number(s): Q76L81
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 155 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 8

Human chromosome 8: entries, gene names and cross-references to MIM