CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008962
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peregrin 
Protein Synonyms/Alias
 Bromodomain and PHD finger-containing protein 1; Protein Br140 
Gene Name
 BRPF1 
Gene Synonyms/Alias
 BR140 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
476DEEEDEGKGWSSEKVacetylation[1]
580VGRDSEDKNWALKEQacetylation[1, 2, 3]
896RTSVLFSKKNPKTAGacetylation[1, 3, 4, 5]
897TSVLFSKKNPKTAGPacetylation[5]
900LFSKKNPKTAGPPKRacetylation[5]
1027PSKQGRGKPSFSRGTacetylation[3]
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] 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]
 [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] 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]
 [5] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224] 
Functional Description
 Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Positively regulates the transcription of RUNX1 and RUNX2. 
Sequence Annotation
 DOMAIN 645 715 Bromo.
 DOMAIN 1085 1168 PWWP.
 ZN_FING 21 47 C2H2-type.
 ZN_FING 273 323 PHD-type.
 ZN_FING 386 400 C4-type.
 REGION 59 222 Interaction with KAT6A and KAT6B.
 REGION 501 821 Interaction with MEAF6 and ING5.
 REGION 543 1079 Required for RUNX1 and RUNX2
 MOD_RES 120 120 Phosphoserine.
 MOD_RES 460 460 Phosphoserine.
 MOD_RES 462 462 Phosphoserine.
 MOD_RES 860 860 Phosphoserine.
 MOD_RES 1076 1076 Phosphoserine.
 MOD_RES 1187 1187 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Activator; Alternative splicing; Bromodomain; Chromatin regulator; Complete proteome; Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1214 AA 
Protein Sequence
MGVDFDVKTF CHNLRATKPP YECPVETCRK VYKSYSGIEY HLYHYDHDNP PPPQQTPLRK 60
HKKKGRQSRP ANKQSPSPSE VSQSPGREVM SYAQAQRMVE VDLHGRVHRI SIFDNLDVVS 120
EDEEAPEEAP ENGSNKENTE TPAATPKSGK HKNKEKRKDS NHHHHHNVSA STTPKLPEVV 180
YRELEQDTPD APPRPTSYYR YIEKSAEELD EEVEYDMDEE DYIWLDIMNE RRKTEGVSPI 240
PQEIFEYLMD RLEKESYFES HNKGDPNALV DEDAVCCICN DGECQNSNVI LFCDMCNLAV 300
HQECYGVPYI PEGQWLCRRC LQSPSRAVDC ALCPNKGGAF KQTDDGRWAH VVCALWIPEV 360
CFANTVFLEP IDSIEHIPPA RWKLTCYICK QRGSGACIQC HKANCYTAFH VTCAQQAGLY 420
MKMEPVRETG ANGTSFSVRK TAYCDIHTPP GSARRLPALS HSEGEEDEDE EEDEGKGWSS 480
EKVKKAKAKS RIKMKKARKI LAEKRAAAPV VSVPCIPPHR LSKITNRLTI QRKSQFMQRL 540
HSYWTLKRQS RNGVPLLRRL QTHLQSQRNC DQVGRDSEDK NWALKEQLKS WQRLRHDLER 600
ARLLVELIRK REKLKRETIK VQQIAMEMQL TPFLILLRKT LEQLQEKDTG NIFSEPVPLS 660
EVPDYLDHIK KPMDFFTMKQ NLEAYRYLNF DDFEEDFNLI VSNCLKYNAK DTIFYRAAVR 720
LREQGGAVLR QARRQAEKMG IDFETGMHIP HSLAGDEATH HTEDAAEEER LVLLENQKHL 780
PVEEQLKLLL ERLDEVNASK QSVGRSRRAK MIKKEMTALR RKLAHQRETG RDGPERHGPS 840
SRGSLTPHPA ACDKDGQTDS AAEESSSQET SKGLGPNMSS TPAHEVGRRT SVLFSKKNPK 900
TAGPPKRPGR PPKNRESQMT PSHGGSPVGP PQLPIMSSLR QRKRGRSPRP SSSSDSDSDK 960
STEDPPMDLP ANGFSGGNQP VKKSFLVYRN DCSLPRSSSD SESSSSSSSS AASDRTSTTP 1020
SKQGRGKPSF SRGTFPEDSS EDTSGTENEA YSVGTGRGVG HSMVRKSLGR GAGWLSEDED 1080
SPLDALDLVW AKCRGYPSYP ALIIDPKMPR EGMFHHGVPI PVPPLEVLKL GEQMTQEARE 1140
HLYLVLFFDN KRTWQWLPRT KLVPLGVNQD LDKEKMLEGR KSNIRKSVQI AYHRALQHRS 1200
KVQGEQSSET SDSD 1214 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
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.