CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-038254
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Protein Brd1 
Protein Synonyms/Alias
  
Gene Name
 Brd1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
23PSSPCSIKHSPTRETacetylation[1, 2]
277DCVLCPNKGGAFKKTacetylation[1]
324NIPPARWKLTCYLCKacetylation[1, 2]
331KLTCYLCKQKGVGACacetylation[1]
368YMKMEPVKELTGGSAacetylation[1]
413MKNGVCRKESSVKTVacetylation[2]
418CRKESSVKTVRSTSKacetylation[2]
516RENDEEMKAAKEKLKacetylation[1]
519DEEMKAAKEKLKYWQacetylation[1]
554KLKREQVKVEQMAMEacetylation[1]
644NCMKYNAKDTVFYRAacetylation[1, 2]
887RTSVLFCKSKSVSPPacetylation[2]
1034IENGNYAKAARIAAEacetylation[1, 2]
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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Metal-binding; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1189 AA 
Protein Sequence
MRRKGRCHRG SAARHPSSPC SIKHSPTRET LTYAQAQRMV EIEIEGRLHR ISIFDPLEII 60
LEDDLTAQEM SECNSNKENS ERPPVCLRTK RHKNNRVKKK NEVLPSTHGT PASASALPEP 120
KVRIVEYSPP SAPRRPPVYY KFIEKSAEEL DNEVEYDMDE EDYAWLEIIN EKRKGDCVSA 180
VSQNMFEFLM DRFEKESYCE NQKQGEQQSL IDEDAVCCIC MDGECQNSNV ILFCDMCNLA 240
VHQECYGVPY IPEGQWLCRH CLQSRARPAD CVLCPNKGGA FKKTDDDRWG HVVCALWIPE 300
VGFANTVFIE PIDGVRNIPP ARWKLTCYLC KQKGVGACIQ CHKANCYTAF HVTCAQKAGL 360
YMKMEPVKEL TGGSATFSVR KTAYCDVHTP PGCTRRPLNI YGDVEMKNGV CRKESSVKTV 420
RSTSKVRKKA KKAKKTLAEP CAVLPTVCAP YIPPQRLNRI ANQVAIQRKK QFVERAHSYW 480
LLKRLSRNGA PLLRRLQSSL QSQRNTQQRE NDEEMKAAKE KLKYWQRLRH DLERARLLIE 540
LLRKREKLKR EQVKVEQMAM ELRLTPLTVL LRSVLEQLQE KDPAKIFAQP VSLKEVPDYL 600
DHIKHPMDFA TMRKRLEAQG YKNLHAFEED FNLIVDNCMK YNAKDTVFYR AAVRLRDQGG 660
VVLRQARREV ESIGLEEASG MHLPERPIAA PRRPFSWEEV DRLLDPANRA HMSLEEQLRE 720
LLDKLDLTCS MKSSGSRSKR AKLLKKEIAL LRNKLSQQHS QAPPTGAGTG GFEDEAAPLA 780
PDTAEEGANS PPKLEPSDAL PLPSNSETNS EPPTLNPVEL HPEQSKLFKR VTFDNESHST 840
CTQSALVSGH PPEPTLASSG DVPAAAASAV AEPSSDVNRR TSVLFCKSKS VSPPKSAKNT 900
ETQPTSPQLG TKTFLSVVLP RLETLLQPRK RSRSTCGDSE VEEESPGKRL DTGLTNGFGG 960
ARSEQEPGGG PGRKAAPRRR CASESSICSS NSPLCDSSFS TPKCGRGKPA LVRRHTLEDR 1020
SELISCIENG NYAKAARIAA EVGQSNMWIS TDAAASVLEP LKVVWAKCSG YPSYPALIID 1080
PKMPRVPGHH NGVTIPAPPL DVLKIGEHMQ TKSEEKLFLV LFFDNKRSWQ WLPKSKMVPL 1140
GVDETIDKLK MMEGRNSSIR KAVRIAFDRA MNHLSRVHGE PASDLSDID 1189 
Gene Ontology
 GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0043966; P:histone H3 acetylation; IEA:Compara. 
Interpro
 IPR001487; Bromodomain.
 IPR018359; Bromodomain_CS.
 IPR019542; Enhancer_polycomb-like_N.
 IPR000313; PWWP.
 IPR019786; Zinc_finger_PHD-type_CS.
 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 
PROSITE
 PS00633; BROMODOMAIN_1
 PS50014; BROMODOMAIN_2
 PS50812; PWWP
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS
 PR00503; BROMODOMAIN.