CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021487
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone acetyltransferase KAT8 
Protein Synonyms/Alias
 Lysine acetyltransferase 8; MOZ, YBF2/SAS3, SAS2 and TIP60 protein 1; MYST-1; hMOF 
Gene Name
 KAT8 
Gene Synonyms/Alias
 MOF; MYST1; PP7073 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
106RLDEWVDKNRLALTKubiquitination[1]
113KNRLALTKTVKDAVQacetylation[2]
113KNRLALTKTVKDAVQubiquitination[1]
116LALTKTVKDAVQKNSacetylation[3]
125AVQKNSEKYLSELAEubiquitination[1]
143RKITRNQKRKHDEINacetylation[4]
145ITRNQKRKHDEINHVacetylation[4]
154DEINHVQKTYAEMDPacetylation[4]
168PTTAALEKEHEAITKacetylation[3, 5]
175KEHEAITKVKYVDKIacetylation[4]
177HEAITKVKYVDKIHIacetylation[4]
238QWRQPPGKEIYRKSNacetylation[2]
274AKLFLDHKTLYFDVEacetylation[4, 6]
410LNMVKYWKGQHVICVacetylation[4]
427KLVEEHLKSAQYKKPubiquitination[1]
449CLKWAPPKHKQVKLSacetylation[4]
454PPKHKQVKLSKK***acetylation[4]
457HKQVKLSKK******acetylation[4]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [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] 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]
 [4] Autoacetylation of the MYST lysine acetyltransferase MOF protein.
 Yang C, Wu J, Sinha SH, Neveu JM, Zheng YG.
 J Biol Chem. 2012 Oct 12;287(42):34917-26. [PMID: 22918831]
 [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] Modulations of hMOF autoacetylation by SIRT1 regulate hMOF recruitment and activities on the chromatin.
 Lu L, Li L, Lv X, Wu XS, Liu DP, Liang CC.
 Cell Res. 2011 Aug;21(8):1182-95. [PMID: 21502975] 
Functional Description
 Histone acetyltransferase which may be involved in transcriptional activation. May influence the function of ATM. As part of the MSL complex it is involved in acetylation of nucleosomal histone H4 producing specifically H4K16ac. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. That activity is less specific than the one of the MSL complex. 
Sequence Annotation
 DOMAIN 69 123 Chromo.
 ZN_FING 208 230 C2HC-type.
 REGION 174 458 Sufficient for interaction with KANSL1.
 REGION 324 330 Acetyl-CoA binding.
 ACT_SITE 274 274
 ACT_SITE 316 316 Nucleophile (By similarity).
 BINDING 319 319 Acetyl-CoA.
 BINDING 354 354 Acetyl-CoA.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 37 37 Phosphoserine (By similarity).
 MOD_RES 42 42 Phosphoserine (By similarity).
 MOD_RES 113 113 N6-acetyllysine.
 MOD_RES 274 274 N6-acetyllysine; by autocatalysis.  
Keyword
 3D-structure; Acetylation; Activator; Acyltransferase; Alternative splicing; Chromatin regulator; Chromosome; Complete proteome; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation; Transferase; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 458 AA 
Protein Sequence
MAAQGAAAAV AAGTSGVAGE GEPGPGENAA AEGTAPSPGR VSPPTPARGE PEVTVEIGET 60
YLCRRPDSTW HSAEVIQSRV NDQEGREEFY VHYVGFNRRL DEWVDKNRLA LTKTVKDAVQ 120
KNSEKYLSEL AEQPERKITR NQKRKHDEIN HVQKTYAEMD PTTAALEKEH EAITKVKYVD 180
KIHIGNYEID AWYFSPFPED YGKQPKLWLC EYCLKYMKYE KSYRFHLGQC QWRQPPGKEI 240
YRKSNISVYE VDGKDHKIYC QNLCLLAKLF LDHKTLYFDV EPFVFYILTE VDRQGAHIVG 300
YFSKEKESPD GNNVACILTL PPYQRRGYGK FLIAFSYELS KLESTVGSPE KPLSDLGKLS 360
YRSYWSWVLL EILRDFRGTL SIKDLSQMTS ITQNDIISTL QSLNMVKYWK GQHVICVTPK 420
LVEEHLKSAQ YKKPPITVDS VCLKWAPPKH KQVKLSKK 458 
Gene Ontology
 GO:0000776; C:kinetochore; IEA:Compara.
 GO:0071339; C:MLL1 complex; IDA:UniProtKB.
 GO:0072487; C:MSL complex; IDA:UniProtKB.
 GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0035064; F:methylated histone residue binding; IDA:UniProtKB.
 GO:0008134; F:transcription factor binding; IDA:UniProtKB.
 GO:0043984; P:histone H4-K16 acetylation; IDA:UniProtKB.
 GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
 GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB.
 GO:0030099; P:myeloid cell differentiation; IDA:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA: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.
 IPR000953; Chromo_domain/shadow.
 IPR016197; Chromodomain-like.
 IPR002717; MOZ_SAS.
 IPR025995; Tudor-knot. 
Pfam
 PF01853; MOZ_SAS
 PF11717; Tudor-knot 
SMART
 SM00298; CHROMO 
PROSITE
 PS00598; CHROMO_1
 PS50013; CHROMO_2 
PRINTS