CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-030267
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Bromodomain and PHD finger containing, 1 
Protein Synonyms/Alias
 Brpf1 protein; Protein Brpf1 
Gene Name
 Brpf1 
Gene Synonyms/Alias
 mCG_132959 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
8MGVDFDVKTFCHNLRacetylation[1]
147ETPAATPKSGKHKNKacetylation[2]
579VGRDSDDKNWALKEQacetylation[2]
894RTSVLFSKKNPKTAGacetylation[1, 2, 3]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [3] 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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Metal-binding; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1212 AA 
Protein Sequence
MGVDFDVKTF CHNLRATKPP YECPVETCRK VYKSYSGIEY HLYHYDHDSP PPPQQTPLRK 60
HKKKGRQSRP ANKQSPSPSE VSQSPGREVM SYAQAQRMVE VDLHGRVHRI SIFDNLDVVS 120
EDEEAPEEAP ENGSNKENTE TPAATPKSGK HKNKEKRKDS NHHHHSAPAS AAPKLPEVVY 180
RELEQDTPDA PPRPTSYYRY IEKSAEELDE EVEYDMDEED YIWLDIMNER RKTEGVSPIP 240
QEIFEYLMDR LEKESYFESH NKGDPNALVD EDAVCCICND GECQNSNVIL FCDMCNLAVH 300
QECYGVPYIP EGQWLCRRCL QSPSRAVDCA LCPNKGGAFK QTDDGRWAHV VCALWIPEVC 360
FANTVFLEPI DSIEHIPPAR WKLTCYICKQ RGSGACIQCH KANCYTAFHV TCAQQAGLYM 420
KMEPVRETGA NGTSFSVRKT AYCDIHTPPG SARRLPALSH SEGEEEEDEE EDEGKSWSSE 480
KVKKAKAKSR IKMKKARKIL AEKRAAAPVV SVPCIPPHRL SKITNRLTIQ RKSQFMQRLH 540
SYWTLKRQSR NGVPLLRRLQ THLQSQRNCE QVGRDSDDKN WALKEQLKSW QRLRHDLERA 600
RLLVELIRKR EKLKRETIKI QQIAMEMQLT PFLILLRKTL EQLQEKDTGN IFSEPVPLSE 660
VPDYLDHIKK PMDFFTMKQN LEAYRYLNFD DFEEDFNLIV SNCLKYNAKD TIFYRAAVRL 720
REQGGAVLRQ ARRQAEKMGI DFETGMHIPH NLAGDEVSHH TEDVEEERLV LLENQKHLPV 780
EEQLKLLLER LDEVNASKQS VGRSRRAKMI KKEMTALRRK LAHQRETGRD GPERHGPSGR 840
GNLTPHPAAC DKDGQTDSAA EESSSQETSK GLGPNMSSTP AHEVGRRTSV LFSKKNPKTA 900
GPPKRPGRPP KNRESQMTPS HGGSPVGPPQ LPIMGSLRQR KRGRSPRPSS SSDSDSDKST 960
EDPPMDLPAN GFSSGNQPVK KSFLVYRNDC NLPRSSSDSE SSSSSSSSAA SDRTSTTPSK 1020
QGRGKPSFSR GTFPEDSSED TSGTENEAYS VGTGRGVGHS MVRKSLGRGA GWLSEDEDSP 1080
LDALDLVWAK CRGYPSYPAL IIDPKMPREG MFHHGVPIPV PPLEVLKLGE QMTQEAREHL 1140
YLVLFFDNKR TWQWLPRTKL VPLGVNQDLD KEKMLEGRKS NIRKSVQIAY HRALQHRSKV 1200
QGEQSSETSD SD 1212 
Gene Ontology
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR001487; Bromodomain.
 IPR018359; Bromodomain_CS.
 IPR019542; Enhancer_polycomb-like_N.
 IPR000313; PWWP.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR007087; Znf_C2H2.
 IPR015880; Znf_C2H2-like.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00439; Bromodomain
 PF10513; EPL1
 PF00855; PWWP 
SMART
 SM00297; BROMO
 SM00249; PHD
 SM00293; PWWP
 SM00355; ZnF_C2H2 
PROSITE
 PS00633; BROMODOMAIN_1
 PS50014; BROMODOMAIN_2
 PS50812; PWWP
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS
 PR00503; BROMODOMAIN.