CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001560
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone acetyltransferase KAT7 
Protein Synonyms/Alias
 Histone acetyltransferase binding to ORC1; Lysine acetyltransferase 7; MOZ, YBF2/SAS3, SAS2 and TIP60 protein 2; MYST-2 
Gene Name
 KAT7 
Gene Synonyms/Alias
 HBO1; HBOa; MYST2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
155SHDESIAKDMSLKDSacetylation[1]
160IAKDMSLKDSGSDLSacetylation[2]
199SLGHLTGKHERHFSIacetylation[3]
338TEGSNMIKTIAFGRYubiquitination[4, 5]
376EFCLKYMKSQTILRRubiquitination[6]
524ISYRSYWKEVLLRYLubiquitination[4, 5]
537YLHNFQGKEISIKEIubiquitination[4, 5, 7]
609CLKWTPPKGT*****ubiquitination[6]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
Functional Description
 Component of the HBO1 complex which has a histone H4- specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Through chromatin acetylation it may regulate DNA replication and act as a coactivator of TP53-dependent transcription. Specifically represses AR-mediated transcription. 
Sequence Annotation
 ZN_FING 366 388 C2HC-type.
 REGION 482 488 Acetyl-CoA binding (By similarity).
 ACT_SITE 432 432 By similarity.
 ACT_SITE 474 474 Nucleophile (By similarity).
 BINDING 477 477 Acetyl-CoA (By similarity).
 BINDING 512 512 Acetyl-CoA (By similarity).
 MOD_RES 50 50 Phosphoserine.
 MOD_RES 57 57 Phosphoserine; by PLK1.
 MOD_RES 85 85 Phosphothreonine; by CDK1.
 MOD_RES 88 88 Phosphothreonine; by CDK1.
 MOD_RES 102 102 Phosphoserine.
 MOD_RES 124 124 Phosphoserine.
 MOD_RES 162 162 Phosphoserine.
 MOD_RES 164 164 Phosphoserine.
 MOD_RES 199 199 N6-acetyllysine.
 MOD_RES 432 432 N6-acetyllysine; by autocatalysis (By
 MOD_RES 506 506 Phosphoserine.  
Keyword
 Acetylation; Acyltransferase; Alternative splicing; Chromatin regulator; Complete proteome; DNA replication; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation; Transferase; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 611 AA 
Protein Sequence
MPRRKRNAGS SSDGTEDSDF STDLEHTDSS ESDGTSRRSA RVTRSSARLS QSSQDSSPVR 60
NLQSFGTEEP AYSTRRVTRS QQQPTPVTPK KYPLRQTRSS GSETEQVVDF SDRETKNTAD 120
HDESPPRTPT GNAPSSESDI DISSPNVSHD ESIAKDMSLK DSGSDLSHRP KRRRFHESYN 180
FNMKCPTPGC NSLGHLTGKH ERHFSISGCP LYHNLSADEC KVRAQSRDKQ IEERMLSHRQ 240
DDNNRHATRH QAPTERQLRY KEKVAELRKK RNSGLSKEQK EKYMEHRQTY GNTREPLLEN 300
LTSEYDLDLF RRAQARASED LEKLRLQGQI TEGSNMIKTI AFGRYELDTW YHSPYPEEYA 360
RLGRLYMCEF CLKYMKSQTI LRRHMAKCVW KHPPGDEIYR KGSISVFEVD GKKNKIYCQN 420
LCLLAKLFLD HKTLYYDVEP FLFYVMTEAD NTGCHLIGYF SKEKNSFLNY NVSCILTMPQ 480
YMRQGYGKML IDFSYLLSKV EEKVGSPERP LSDLGLISYR SYWKEVLLRY LHNFQGKEIS 540
IKEISQETAV NPVDIVSTLQ ALQMLKYWKG KHLVLKRQDL IDEWIAKEAK RSNSNKTMDP 600
SCLKWTPPKG T 611 
Gene Ontology
 GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
 GO:0004402; F:histone acetyltransferase activity; IEA:EC.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006260; P:DNA replication; IDA:UniProtKB.
 GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
 GO:0043983; P:histone H4-K12 acetylation; IDA:UniProtKB.
 GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
 GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; TAS:ProtInc.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR016181; Acyl_CoA_acyltransferase.
 IPR002717; MOZ_SAS.
 IPR015880; Znf_C2H2-like.
 IPR002515; Znf_C2HC. 
Pfam
 PF01853; MOZ_SAS
 PF01530; zf-C2HC 
SMART
 SM00355; ZnF_C2H2 
PROSITE
  
PRINTS