CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018373
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone acetyltransferase KAT6B 
Protein Synonyms/Alias
 Histone acetyltransferase MOZ2; MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4; MYST-4; Monocytic leukemia zinc finger protein-related factor 
Gene Name
 KAT6B 
Gene Synonyms/Alias
 KIAA0383; MORF; MOZ2; MYST4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
223CSFCLGTKESNREKKacetylation[1]
379PGRGQKTKVCTTPSSacetylation[1]
393SGHAASGKDSSSRLAacetylation[1]
440GLIDGLTKFFTPSPDacetylation[2]
440GLIDGLTKFFTPSPDubiquitination[3, 4]
590SKAHFFGKRDIRSRFacetylation[1]
638MLGRLKYKVTPQMGTacetylation[5]
650MGTPSPGKGSLTDGRacetylation[5]
785ANEIYRRKDLSVFEVubiquitination[3, 4]
970LILSHMEKLKTCSRAubiquitination[6]
1038NSRQSPAKVQSKNKYacetylation[2, 5]
1042SPAKVQSKNKYLHSPacetylation[1, 2, 5, 7]
1044AKVQSKNKYLHSPESacetylation[1, 2, 5, 7]
1115SSPPRLTKPQSVAIKacetylation[1]
1245NPEPLKCKQVWPKGTacetylation[1]
Reference
 [1] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [2] 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]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [7] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773
Functional Description
 Histone acetyltransferase which may be involved in both positive and negative regulation of transcription. Required for RUNX2-dependent transcriptional activation. May be involved in cerebral cortex development. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. 
Sequence Annotation
 DOMAIN 103 176 H15.
 ZN_FING 213 272 PHD-type 1.
 ZN_FING 269 320 PHD-type 2.
 ZN_FING 749 771 C2HC-type.
 REGION 361 717 Negatively regulates HAT activity.
 REGION 718 1008 Catalytic.
 REGION 752 1008 Interaction with BRPF1.
 REGION 856 860 Acetyl-CoA binding (By similarity).
 REGION 865 871 Acetyl-CoA binding (By similarity).
 REGION 1560 2073 Interaction with RUNX1 and RUNX2.
 ACT_SITE 815 815 By similarity.
 ACT_SITE 857 857 Nucleophile (By similarity).
 BINDING 895 895 Acetyl-CoA (By similarity).
 MOD_RES 815 815 N6-acetyllysine; by autocatalysis (By
 MOD_RES 1038 1038 N6-acetyllysine.
 MOD_RES 1042 1042 N6-acetyllysine.
 MOD_RES 1044 1044 N6-acetyllysine.  
Keyword
 Acetylation; Activator; Acyltransferase; Alternative splicing; Chromatin regulator; Chromosomal rearrangement; Complete proteome; Metal-binding; Nucleus; Polymorphism; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation; Transferase; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2073 AA 
Protein Sequence
MVKLANPLYT EWILEAIQKI KKQKQRPSEE RICHAVSTSH GLDKKTVSEQ LELSVQDGSV 60
LKVTNKGLAS YKDPDNPGRF SSVKPGTFPK SAKGSRGSCN DLRNVDWNKL LRRAIEGLEE 120
PNGSSLKNIE KYLRSQSDLT STTNNPAFQQ RLRLGAKRAV NNGRLLKDGP QYRVNYGSLD 180
GKGAPQYPSA FPSSLPPVSL LPHEKDQPRA DPIPICSFCL GTKESNREKK PEELLSCADC 240
GSSGHPSCLK FCPELTTNVK ALRWQCIECK TCSACRVQGR NADNMLFCDS CDRGFHMECC 300
DPPLSRMPKG MWICQVCRPK KKGRKLLHEK AAQIKRRYAK PIGRPKNKLK QRLLSVTSDE 360
GSMNAFTGRG SPGRGQKTKV CTTPSSGHAA SGKDSSSRLA VTDPTRPGAT TKITTTSTYI 420
SASTLKVNKK TKGLIDGLTK FFTPSPDGRR SRGEIIDFSK HYRPRKKVSQ KQSCTSHVLA 480
TGTTQKLKPP PSSLPPPTPI SGQSPSSQKS STATSSPSPQ SSSSQCSVPS LSSLTTNSQL 540
KALFDGLSHI YTTQGQSRKK GHPSYAPPKR MRRKTELSST AKSKAHFFGK RDIRSRFISH 600
SSSSSWGMAR GSIFKAIAHF KRTTFLKKHR MLGRLKYKVT PQMGTPSPGK GSLTDGRIKP 660
DQDDDTEIKI NIKQESADVN VIGNKDVVTE EDLDVFKQAQ ELSWEKIECE SGVEDCGRYP 720
SVIEFGKYEI QTWYSSPYPQ EYARLPKLYL CEFCLKYMKS KNILLRHSKK CGWFHPPANE 780
IYRRKDLSVF EVDGNMSKIY CQNLCLLAKL FLDHKTLYYD VEPFLFYVLT KNDEKGCHLV 840
GYFSKEKLCQ QKYNVSCIMI MPQHQRQGFG RFLIDFSYLL SRREGQAGSP EKPLSDLGRL 900
SYLAYWKSVI LEYLYHHHER HISIKAISRA TGMCPHDIAT TLQHLHMIDK RDGRFVIIRR 960
EKLILSHMEK LKTCSRANEL DPDSLRWTPI LISNAAVSEE EREAEKEAER LMEQASCWEK 1020
EEQEILSTRA NSRQSPAKVQ SKNKYLHSPE SRPVTGERGQ LLELSKESSE EEEEEEDEEE 1080
EEEEEEEEED EEEEEEEEEE EEEENIQSSP PRLTKPQSVA IKRKRPFVLK KKRGRKRRRI 1140
NSSVTTETIS ETTEVLNEPF DNSDEERPMP QLEPTCEIEV EEDGRKPVLR KAFQHQPGKK 1200
RQTEEEEGKD NHCFKNADPC RNNMNDDSSN LKEGSKDNPE PLKCKQVWPK GTKRGLSKWR 1260
QNKERKTGFK LNLYTPPETP MEPDEQVTVE EQKETSEGKT SPSPIRIEEE VKETGEALLP 1320
QEENRREETC APVSPNTSPG EKPEDDLIKP EEEEEEEEEE EEEEEEEEGE EEEGGGNVEK 1380
DPDGAKSQEK EEPEISTEKE DSARLDDHEE EEEEDEEPSH NEDHDADDED DSHMESAEVE 1440
KEELPRESFK EVLENQETFL DLNVQPGHSN PEVLMDCGVD LTASCNSEPK ELAGDPEAVP 1500
ESDEEPPPGE QAQKQDQKNS KEVDTEFKEG NPATMEIDSE TVQAVQSLTQ ESSEQDDTFQ 1560
DCAETQEACR SLQNYTRADQ SPQIATTLDD CQQSDHSSPV SSVHSHPGQS VRSVNSPSVP 1620
ALENSYAQIS PDQSAISVPS LQNMETSPMM DVPSVSDHSQ QVVDSGFSDL GSIESTTENY 1680
ENPSSYDSTM GGSICGNGSS QNSCSYSNLT SSSLTQSSCA VTQQMSNISG SCSMLQQTSI 1740
SSPPTCSVKS PQGCVVERPP SSSQQLAQCS MAANFTPPMQ LAEIPETSNA NIGLYERMGQ 1800
SDFGAGHYPQ PSATFSLAKL QQLTNTLIDH SLPYSHSAAV TSYANSASLS TPLSNTGLVQ 1860
LSQSPHSVPG GPQAQATMTP PPNLTPPPMN LPPPLLQRNM AASNIGISHS QRLQTQIASK 1920
GHISMRTKSA SLSPAAATHQ SQIYGRSQTV AMQGPARTLT MQRGMNMSVN LMPAPAYNVN 1980
SVNMNMNTLN AMNGYSMSQP MMNSGYHSNH GYMNQTPQYP MQMQMGMMGT QPYAQQPMQT 2040
PPHGNMMYTA PGHHGYMNTG MSKQSLNGSY MRR 2073 
Gene Ontology
 GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IDA:UniProtKB.
 GO:0000786; C:nucleosome; NAS:UniProtKB.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
 GO:0008134; F:transcription factor binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0006334; P:nucleosome assembly; NAS:UniProtKB.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR016181; Acyl_CoA_acyltransferase.
 IPR005818; Histone_H1/H5.
 IPR002717; MOZ_SAS.
 IPR011991; WHTH_DNA-bd_dom.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00538; Linker_histone
 PF01853; MOZ_SAS
 PF00628; PHD 
SMART
 SM00526; H15
 SM00249; PHD 
PROSITE
 PS51504; H15
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS