Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Histone acetyltransferase KAT6A  

UniProtKB / Swiss-Prot ID :  KAT6A_HUMAN

Gene Name (Synonyms) : 
KAT6A, MOZ, MYST3, RUNXBP2, ZNF220  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. Note=Partially concentrated in subnuclear foci distinct from PML bodies, and excluded from the nucleoli. 

Protein 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. 

Protein Sequence MVKLANPLYTEWILEAIKKVKKQKQRPSEERICNAVSSSHGLDRKTVLEQLELSVKDGTILKVSNKGLNS...
Predicted Secondary Structure  -
Protein Variant
LocationDescription
134L -> S (in dbSNP:rs3824276). VAR_047548
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
28PhosphoserineKQRPSEERI
55.04HPRD
Link-
350N6-acetyllysineNTVSKGPFS
67.29HPRD
Link-
350N6-acetyllysineNTVSKGPFS
67.29Phosphositeplus
Link-
350N6-acetyllysine.NTVSKGPFS
67.29UniProtKB
Link-
355N6-acetyllysineGPFSKVRTG
35.79HPRD
Link-
355N6-acetyllysineGPFSKVRTG
35.79Phosphositeplus
Link-
355N6-acetyllysine.GPFSKVRTG
35.79UniProtKB
Link-
415N6-acetyllysineDGLTKFFTP
43.45HPRD
Link-
415N6-acetyllysineDGLTKFFTP
43.45Phosphositeplus
Link-
418PhosphothreonineTKFFTPSPD
26.45HPRD
Link-
418PhosphothreonineTKFFTPSPD
26.45PhosphoELM
Link-
418PhosphothreonineTKFFTPSPD
26.45Phosphositeplus
Link-
418PhosphothreonineTKFFTPSPD
26.45SysPTM
Link-
418Phosphothreonine.TKFFTPSPD
26.45UniProtKB
Link-
420PhosphoserineFFTPSPDGR
32.34HPRD
Link-
420PhosphoserineFFTPSPDGR
32.34PhosphoELM
Link-
420PhosphoserineFFTPSPDGR
32.34Phosphositeplus
Link-
420PhosphoserineFFTPSPDGR
32.34SysPTM
Link-
420Phosphoserine.FFTPSPDGR
32.34UniProtKB
Link-
447PhosphoserineGNRKSSTSD
35.29HPRD
Link-
449PhosphothreonineRKSSTSDWP
37.48HPRD
Link-
449Phosphothreonine.RKSSTSDWP
37.48UniProtKB
Link-
473PhosphoserineRLFGSQEIM
19.80HPRD
Link-
473PhosphoserineRLFGSQEIM
19.80PhosphoELM
Link-
473PhosphoserineRLFGSQEIM
19.80Phosphositeplus
Link-
473Phosphoserine.RLFGSQEIM
19.80UniProtKB
Link-
604N6-acetyllysineFLDHKTLYY
39.63HPRD
Link-
604N6-acetyllysineFLDHKTLYY
39.63Phosphositeplus
Link-
604N6-acetyllysine.FLDHKTLYY
39.63UniProtKB
Link-
815N6-acetyllysineISVGKSVSH
45.59Phosphositeplus
Link-
815N6-acetyllysine.ISVGKSVSH
45.59UniProtKB
Link-
842PhosphoserineMAPVSSTRL
25.57HPRD
Link-
909PhosphothreonineKSEATQEQY
28.70HPRD
Link-
909PhosphothreonineKSEATQEQY
28.70PhosphoELM
Link-
909PhosphothreonineKSEATQEQY
28.70Phosphositeplus
Link-
909Phosphothreonine.KSEATQEQY
28.70UniProtKB
Link-
941PhosphoserineKRRLSEGVE
30.41HPRD
Link-
941PhosphoserineKRRLSEGVE
30.41PhosphoELM
Link-
941PhosphoserineKRRLSEGVE
30.41Phosphositeplus
Link-
941Phosphoserine.KRRLSEGVE
30.41UniProtKB
Link-
1007N6-acetyllysinePILTKPTLK
32.34HPRD
Link-
1007N6-acetyllysinePILTKPTLK
32.34Phosphositeplus
Link-
1007N6-acetyllysine.PILTKPTLK
32.34UniProtKB
Link-
1089PhosphoserineFRRLSSQDV
24.92HPRD
Link-
1089PhosphoserineFRRLSSQDV
24.92PhosphoELM
Link-
1089PhosphoserineFRRLSSQDV
24.92Phosphositeplus
Link-
1104PhosphoserineSKRKSKDEE
49.74HPRD
Link-
1104PhosphoserineSKRKSKDEE
49.74Phosphositeplus
Link-
1113PhosphoserineEDEESDDAD
38.45HPRD
Link-
1113PhosphoserineEDEESDDAD
38.45PhosphoELM
Link-
1113PhosphoserineEDEESDDAD
38.45Phosphositeplus
Link-
1113PhosphoserineEDEESDDAD
38.45SysPTM
Link-
1113Phosphoserine.EDEESDDAD
38.45UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
OMIM disease
Note=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 inv(8)(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.
616268
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-815, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-350; LYS-355; LYS-604 ANDLYS-1007, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1113, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473 AND THR-909, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-941, AND MASSSPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-418; SER-420 ANDSER-1113, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-449, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1113, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures