CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018839
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone acetyltransferase KAT2B 
Protein Synonyms/Alias
 Histone acetyltransferase PCAF; Histone acetylase PCAF; Lysine acetyltransferase 2B; P300/CBP-associated factor; P/CAF 
Gene Name
 KAT2B 
Gene Synonyms/Alias
 PCAF 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
78GSARIAVKKAQLRSAacetylation[1]
78GSARIAVKKAQLRSAmethylation[2]
79SARIAVKKAQLRSAPacetylation[1]
89LRSAPRAKKLEKLGVmethylation[2]
416GSSSPACKASSGLEAacetylation[3]
428LEANPGEKRKMTDSHacetylation[3]
430ANPGEKRKMTDSHVLacetylation[3]
441SHVLEEAKKPRVMGDacetylation[3]
442HVLEEAKKPRVMGDIacetylation[3]
638TKYVGYIKDYEGATLmethylation[2]
671KKQKEIIKKLIERKQmethylation[2]
672KQKEIIKKLIERKQAmethylation[2]
692YPGLSCFKDGVRQIPmethylation[2]
733DQLYSTLKSILQQVKacetylation[4]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [2] Multiple lysine methylation of PCAF by Set9 methyltransferase.
 Masatsugu T, Yamamoto K.
 Biochem Biophys Res Commun. 2009 Mar 27;381(1):22-6. [PMID: 19351588]
 [3] Mechanisms of P/CAF auto-acetylation.
 Santos-Rosa H, Valls E, Kouzarides T, Martínez-Balbás M.
 Nucleic Acids Res. 2003 Aug 1;31(15):4285-92. [PMID: 12888487]
 [4] 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] 
Functional Description
 Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles. Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. 
Sequence Annotation
 DOMAIN 503 651 N-acetyltransferase.
 DOMAIN 740 810 Bromo.
 MOD_RES 40 40 Phosphoserine (By similarity).  
Keyword
 3D-structure; Acyltransferase; Bromodomain; Cell cycle; Complete proteome; Host-virus interaction; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 832 AA 
Protein Sequence
MSEAGGAGPG GCGAGAGAGA GPGALPPQPA ALPPAPPQGS PCAAAAGGSG ACGPATAVAA 60
AGTAEGPGGG GSARIAVKKA QLRSAPRAKK LEKLGVYSAC KAEESCKCNG WKNPNPSPTP 120
PRADLQQIIV SLTESCRSCS HALAAHVSHL ENVSEEEMNR LLGIVLDVEY LFTCVHKEED 180
ADTKQVYFYL FKLLRKSILQ RGKPVVEGSL EKKPPFEKPS IEQGVNNFVQ YKFSHLPAKE 240
RQTIVELAKM FLNRINYWHL EAPSQRRLRS PNDDISGYKE NYTRWLCYCN VPQFCDSLPR 300
YETTQVFGRT LLRSVFTVMR RQLLEQARQE KDKLPLEKRT LILTHFPKFL SMLEEEVYSQ 360
NSPIWDQDFL SASSRTSQLG IQTVINPPPV AGTISYNSTS SSLEQPNAGS SSPACKASSG 420
LEANPGEKRK MTDSHVLEEA KKPRVMGDIP MELINEVMST ITDPAAMLGP ETNFLSAHSA 480
RDEAARLEER RGVIEFHVVG NSLNQKPNKK ILMWLVGLQN VFSHQLPRMP KEYITRLVFD 540
PKHKTLALIK DGRVIGGICF RMFPSQGFTE IVFCAVTSNE QVKGYGTHLM NHLKEYHIKH 600
DILNFLTYAD EYAIGYFKKQ GFSKEIKIPK TKYVGYIKDY EGATLMGCEL NPRIPYTEFS 660
VIIKKQKEII KKLIERKQAQ IRKVYPGLSC FKDGVRQIPI ESIPGIRETG WKPSGKEKSK 720
EPRDPDQLYS TLKSILQQVK SHQSAWPFME PVKRTEAPGY YEVIRFPMDL KTMSERLKNR 780
YYVSKKLFMA DLQRVFTNCK EYNPPESEYY KCANILEKFF FSKIKEAGLI DK 832 
Gene Ontology
 GO:0031672; C:A band; IEA:Compara.
 GO:0042641; C:actomyosin; IEA:Compara.
 GO:0005671; C:Ada2/Gcn5/Ada3 transcription activator complex; IDA:BHF-UCL.
 GO:0031674; C:I band; IEA:Compara.
 GO:0000776; C:kinetochore; IEA:Compara.
 GO:0000125; C:PCAF complex; NAS:UniProtKB.
 GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; ISS:UniProtKB.
 GO:0004402; F:histone acetyltransferase activity; IEA:EC.
 GO:0004468; F:lysine N-acetyltransferase activity; ISS:UniProtKB.
 GO:0019901; F:protein kinase binding; ISS:UniProtKB.
 GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
 GO:0007050; P:cell cycle arrest; TAS:ProtInc.
 GO:0032869; P:cellular response to insulin stimulus; IDA:BHF-UCL.
 GO:0006338; P:chromatin remodeling; NAS:UniProtKB.
 GO:0043966; P:histone H3 acetylation; IDA:BHF-UCL.
 GO:0018076; P:N-terminal peptidyl-lysine acetylation; IDA:UniProtKB.
 GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
 GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Compara.
 GO:0007219; P:Notch signaling pathway; TAS:Reactome.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
 GO:0010835; P:regulation of protein ADP-ribosylation; IDA:BHF-UCL.
 GO:0006361; P:transcription initiation from RNA polymerase I promoter; TAS:Reactome.
 GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR016181; Acyl_CoA_acyltransferase.
 IPR001487; Bromodomain.
 IPR018359; Bromodomain_CS.
 IPR000182; GNAT_dom.
 IPR016376; Hist_acetylase_PCAF.
 IPR009464; PCAF_N. 
Pfam
 PF13508; Acetyltransf_7
 PF00439; Bromodomain
 PF06466; PCAF_N 
SMART
 SM00297; BROMO 
PROSITE
 PS00633; BROMODOMAIN_1
 PS50014; BROMODOMAIN_2
 PS51186; GNAT 
PRINTS
 PR00503; BROMODOMAIN.