CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012486
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Bromodomain-containing protein 3 
Protein Synonyms/Alias
 RING3-like protein 
Gene Name
 BRD3 
Gene Synonyms/Alias
 KIAA0043; RING3L 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
75LNLPDYHKIIKNPMDubiquitination[1]
304EVPQHAGKKGKLSEHacetylation[2]
307QHAGKKGKLSEHLRYacetylation[2]
657KKQAAKSKEELAQEKacetylation[2]
Reference
 [1] 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]
 [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] 
Functional Description
 Binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling and interaction with transcription factors. Regulates transcription by promoting the binding of the transcription factor GATA1 to its targets (By similarity). Regulates transcription of the CCND1 gene. 
Sequence Annotation
 DOMAIN 51 123 Bromo 1.
 DOMAIN 326 398 Bromo 2.
 DOMAIN 562 644 NET.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 263 263 Phosphoserine.
 MOD_RES 563 563 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Bromodomain; Chromatin regulator; Chromosomal rearrangement; Coiled coil; Complete proteome; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 726 AA 
Protein Sequence
MSTATTVAPA GIPATPGPVN PPPPEVSNPS KPGRKTNQLQ YMQNVVVKTL WKHQFAWPFY 60
QPVDAIKLNL PDYHKIIKNP MDMGTIKKRL ENNYYWSASE CMQDFNTMFT NCYIYNKPTD 120
DIVLMAQALE KIFLQKVAQM PQEEVELLPP APKGKGRKPA AGAQSAGTQQ VAAVSSVSPA 180
TPFQSVPPTV SQTPVIAATP VPTITANVTS VPVPPAAAPP PPATPIVPVV PPTPPVVKKK 240
GVKRKADTTT PTTSAITASR SESPPPLSDP KQAKVVARRE SGGRPIKPPK KDLEDGEVPQ 300
HAGKKGKLSE HLRYCDSILR EMLSKKHAAY AWPFYKPVDA EALELHDYHD IIKHPMDLST 360
VKRKMDGREY PDAQGFAADV RLMFSNCYKY NPPDHEVVAM ARKLQDVFEM RFAKMPDEPV 420
EAPALPAPAA PMVSKGAESS RSSEESSSDS GSSDSEEERA TRLAELQEQL KAVHEQLAAL 480
SQAPVNKPKK KKEKKEKEKK KKDKEKEKEK HKVKAEEEKK AKVAPPAKQA QQKKAPAKKA 540
NSTTTAGRQL KKGGKQASAS YDSEEEEEGL PMSYDEKRQL SLDINRLPGE KLGRVVHIIQ 600
SREPSLRDSN PDEIEIDFET LKPTTLRELE RYVKSCLQKK QRKPFSASGK KQAAKSKEEL 660
AQEKKKELEK RLQDVSGQLS SSKKPARKEK PGSAPSGGPS RLSSSSSSES GSSSSSGSSS 720
DSSDSE 726 
Gene Ontology
 GO:0005634; C:nucleus; NAS:UniProtKB.
 GO:0003682; F:chromatin binding; IDA:UniProtKB.
 GO:0070577; F:histone acetyl-lysine binding; IDA:UniProtKB.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR001487; Bromodomain.
 IPR018359; Bromodomain_CS.
 IPR027353; NET_dom. 
Pfam
 PF00439; Bromodomain 
SMART
 SM00297; BROMO 
PROSITE
 PS00633; BROMODOMAIN_1
 PS50014; BROMODOMAIN_2
 PS51525; NET 
PRINTS
 PR00503; BROMODOMAIN.