CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018822
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone acetyltransferase KAT6A 
Protein Synonyms/Alias
 MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3; MYST-3; Monocytic leukemia zinc finger protein; Runt-related transcription factor-binding protein 2; Zinc finger protein 220 
Gene Name
 KAT6A 
Gene Synonyms/Alias
 MOZ; MYST3; RUNXBP2; ZNF220 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
350KKQNTVSKGPFSKVRacetylation[1]
355VSKGPFSKVRTGPGRacetylation[1]
604AKLFLDHKTLYYDVEacetylation[1]
815ELEISVGKSVSHENKacetylation[2, 3]
1007SSPPILTKPTLKRKKacetylation[1]
1330HLESTKKKELEEQPTmethylation[4]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [3] Proteome-wide prediction of acetylation substrates.
 Basu A, Rose KL, Zhang J, Beavis RC, Ueberheide B, Garcia BA, Chait B, Zhao Y, Hunt DF, Segal E, Allis CD, Hake SB.
 Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13785-90. [PMID: 19666589]
 [4] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 95 171 H15.
 ZN_FING 206 265 PHD-type 1.
 ZN_FING 259 313 PHD-type 2.
 ZN_FING 538 560 C2HC-type.
 REGION 1 144 Required for activation of RUNX1-1.
 REGION 52 166 Required for nuclear localization.
 REGION 144 664 Interaction with PML.
 REGION 312 664 Interaction with RUNX1-1.
 REGION 488 778 Catalytic.
 REGION 507 810 Mediates interaction with BRPF1, required
 REGION 645 649 Acetyl-CoA binding.
 REGION 654 660 Acetyl-CoA binding.
 REGION 1517 1741 Interaction with PML.
 REGION 1517 1642 Interaction with RUNX1-2.
 REGION 1913 1948 Required for activation of RUNX1-2.
 ACT_SITE 604 604 By similarity.
 ACT_SITE 646 646 Nucleophile (By similarity).
 BINDING 684 684 Acetyl-CoA.
 MOD_RES 350 350 N6-acetyllysine.
 MOD_RES 355 355 N6-acetyllysine.
 MOD_RES 369 369 Phosphothreonine; by PKB/AKT1.
 MOD_RES 473 473 Phosphoserine.
 MOD_RES 604 604 N6-acetyllysine; by autocatalysis (By
 MOD_RES 899 899 Phosphotyrosine (By similarity).
 MOD_RES 1007 1007 N6-acetyllysine.
 MOD_RES 1113 1113 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Activator; Acyltransferase; Chromatin regulator; Chromosomal rearrangement; Complete proteome; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation; Transferase; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2004 AA 
Protein Sequence
MVKLANPLYT EWILEAIKKV KKQKQRPSEE RICNAVSSSH GLDRKTVLEQ LELSVKDGTI 60
LKVSNKGLNS YKDPDNPGRI ALPKPRNHGK LDNKQNVDWN KLIKRAVEGL AESGGSTLKS 120
IERFLKGQKD VSALFGGSAA SGFHQQLRLA IKRAIGHGRL LKDGPLYRLN TKATNVDGKE 180
SCESLSCLPP VSLLPHEKDK PVAEPIPICS FCLGTKEQNR EKKPEELISC ADCGNSGHPS 240
CLKFSPELTV RVKALRWQCI ECKTCSSCRD QGKNADNMLF CDSCDRGFHM ECCDPPLTRM 300
PKGMWICQIC RPRKKGRKLL QKKAAQIKRR YTNPIGRPKN RLKKQNTVSK GPFSKVRTGP 360
GRGRKRKITL SSQSASSSSE EGYLERIDGL DFCRDSNVSL KFNKKTKGLI DGLTKFFTPS 420
PDGRKARGEV VDYSEQYRIR KRGNRKSSTS DWPTDNQDGW DGKQENEERL FGSQEIMTEK 480
DMELFRDIQE QALQKVGVTG PPDPQVRCPS VIEFGKYEIH TWYSSPYPQE YSRLPKLYLC 540
EFCLKYMKSR TILQQHMKKC GWFHPPANEI YRKNNISVFE VDGNVSTIYC QNLCLLAKLF 600
LDHKTLYYDV EPFLFYVLTQ NDVKGCHLVG YFSKEKHCQQ KYNVSCIMIL PQYQRKGYGR 660
FLIDFSYLLS KREGQAGSPE KPLSDLGRLS YMAYWKSVIL ECLYHQNDKQ ISIKKLSKLT 720
GICPQDITST LHHLRMLDFR SDQFVIIRRE KLIQDHMAKL QLNLRPVDVD PECLRWTPVI 780
VSNSVVSEEE EEEAEEGENE EPQCQERELE ISVGKSVSHE NKEQDSYSVE SEKKPEVMAP 840
VSSTRLSKQV LPHDSLPANS QPSRRGRWGR KNRKTQERFG DKDSKLLLEE TSSAPQEQYG 900
ECGEKSEATQ EQYTESEEQL VASEEQPSQD GKPDLPKRRL SEGVEPWRGQ LKKSPEALKC 960
RLTEGSERLP RRYSEGDRAV LRGFSESSEE EEEPESPRSS SPPILTKPTL KRKKPFLHRR 1020
RRVRKRKHHN SSVVTETISE TTEVLDEPFE DSDSERPMPR LEPTFEIDEE EEEEDENELF 1080
PREYFRRLSS QDVLRCQSSS KRKSKDEEED EESDDADDTP ILKPVSLLRK RDVKNSPLEP 1140
DTSTPLKKKK GWPKGKSRKP IHWKKRPGRK PGFKLSREIM PVSTQACVIE PIVSIPKAGR 1200
KPKIQESEET VEPKEDMPLP EERKEEEEMQ AEAEEAEEGE EEDAASSEVP AASPADSSNS 1260
PETETKEPEV EEEEEKPRVS EEQRQSEEEQ QELEEPEPEE EEDAAAETAQ NDDHDADDED 1320
DGHLESTKKK ELEEQPTRED VKEEPGVQES FLDANMQKSR EKIKDKEETE LDSEEEQPSH 1380
DTSVVSEQMA GSEDDHEEDS HTKEELIELK EEEEIPHSEL DLETVQAVQS LTQEESSEHE 1440
GAYQDCEETL AACQTLQSYT QADEDPQMSM VEDCHASEHN SPISSVQSHP SQSVRSVSSP 1500
NVPALESGYT QISPEQGSLS APSMQNMETS PMMDVPSVSD HSQQVVDSGF SDLGSIESTT 1560
ENYENPSSYD STMGGSICGN SSSQSSCSYG GLSSSSSLTQ SSCVVTQQMA SMGSSCSMMQ 1620
QSSVQPAANC SIKSPQSCVV ERPPSNQQQQ PPPPPPQQPQ PPPPQPQPAP QPPPPQQQPQ 1680
QQPQPQPQQP PPPPPPQQQP PLSQCSMNNS FTPAPMIMEI PESGSTGNIS IYERIPGDFG 1740
AGSYSQPSAT FSLAKLQQLT NTIMDPHAMP YSHSPAVTSY ATSVSLSNTG LAQLAPSHPL 1800
AGTPQAQATM TPPPNLASTT MNLTSPLLQC NMSATNIGIP HTQRLQGQMP VKGHISIRSK 1860
SAPLPSAAAH QQQLYGRSPS AVAMQAGPRA LAVQRGMNMG VNLMPTPAYN VNSMNMNTLN 1920
AMNSYRMTQP MMNSSYHSNP AYMNQTAQYP MQMQMGMMGS QAYTQQPMQP NPHGNMMYTG 1980
PSHHSYMNAA GVPKQSLNGP YMRR 2004 
Gene Ontology
 GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0000786; C:nucleosome; IEA:InterPro.
 GO:0016605; C:PML body; IDA:UniProtKB.
 GO:0003677; F:DNA binding; IDA:UniProtKB.
 GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
 GO:0003713; F:transcription coactivator activity; TAS:UniProtKB.
 GO:0008134; F:transcription factor binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IDA:UniProtKB.
 GO:0090398; P:cellular senescence; IMP:UniProtKB.
 GO:0006323; P:DNA packaging; TAS:ProtInc.
 GO:0035162; P:embryonic hemopoiesis; IEA:Compara.
 GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
 GO:0030099; P:myeloid cell differentiation; IDA:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0006334; P:nucleosome assembly; IEA:InterPro.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0035019; P:somatic stem cell maintenance; IEA:Compara.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR016181; Acyl_CoA_acyltransferase.
 IPR005818; Histone_H1/H5.
 IPR002717; MOZ_SAS.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF01853; MOZ_SAS
 PF00628; PHD 
SMART
 SM00526; H15
 SM00249; PHD
 SM00184; RING 
PROSITE
 PS51504; H15
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS