Search by BoMiProt ID - Bomi4329


Primary Information

BoMiProt ID Bomi4329
Protein Name Bromodomain-containing protein 2
Organism Bos taurus
Uniprot IdQ32S26
Milk FractionWhey
Ref Sequence Id NP_001039331.1
Aminoacid Length 803
Molecular Weight 88122
Fasta Sequence https://www.uniprot.org/uniprot/Q32S26.fasta
Gene Name BRD2
Gene Id 505358
Protein Existence Status reviewed

Secondary Information

Protein Function  a nuclear serine/threonine kinase involved in transcriptional regulation.BRD2 act as acetylated lysine readers and work in concert with HDACs, often found at active acetylated gene promoter and enhancer regions. inhibits adipogenesis via repressing PPARγ and C/EBPα (CCAAT/enhancer binding protein-α).
Biochemical Properties contains 2 bromo domains.C-terminal part is crucial for Brd2 association with chromatin.contains BET domain which helps to recognize acetylated chromatin.specifically recognizes the histone H4 tail acetylated at Lys12.The two acetyllysine-binding pockets and a negatively charged secondary binding pocket, produced at the dimer interface in BRD2-BD1, may be the unique features that allow BRD2 and BD1 to selectively bind to the acetylated H4 tail.
PTMs Phosphorylation on Ser and Thr,Acetylation on Met
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|Q32S26|BRD2_BOVIN Bromodomain-containing protein 2 OS=Bos taurus OX=9913 GN=BRD2 PE=3 SV=1 MLQNVT*6PHNKLPGEGNAGLLGLGPEAAAPGKRIRKPS*37LLYEGFESPTMASVPALQLTPAN PPPPEVSNPKKPGRVTNQLQYLHKVVMKALWKHQFAWPFRQPVDAVKLGLPDYHKIIKQP MDMGTIKRRLENNYYWAASECMQDFNTMFTNCYIYNKPTDDIVLMAQTLEKIFLQKVASM PQEEQELVVTIPKNSHKKGAKLAALQGSITSAHQVPAVSSVSHTALYTPPPEIPTTVLNI PHPSVISSPLLKSLHSAGPPLLAVSAAPPAQPLAKKKGVKRKADTTTPTPTAILAPGS*298PA S*301PPGGLEPKAARLPPVRRESGRPIKPPRKDLPDSQQQHQSSKKGKLSEQLKHCNGILKEL LSKKHAAYAWPFYKPVDASALGLHDYHDIIKHPMDLSTVKRKMENRDYRDAQEFAADVRL MFSNCYKYNPPDHDVVAMARKLQDVFEFRYAKMPDEPLEPGPLPVSTALPPGLAKSSSES SSEESSSESSSEEEEEEDEDEEEEEEESESSDSEEERAHRLAELQEQLRAVHEQLAALSQ GPISKPKRKREKKEKKKKRKAEKHRGRAGADEDDKGPRAPRPSQPKKSKKAGGGGSSGAA TLGPPGFGPSGGGATKLPKKATKTAPPALPAGYDS*635EEEEESRPMSYDEKRQLSLDINKLP GEKLGRVVHIIQAREPSLRDSNPEEIEIDFETLKPSTLRELERYVLSCLRKKPRKPYTIK KPVGKTKEELALEKKRELEKRLQDVSGQLNSTKKPPKKASEKTETSSAQQVAVSRLSASS SSSDSSSSSSSSSSSDTSDSDSG
Predicted Disorder Regions 48-67, 194-210, 269-287, 332-341, 469-527, 541-566, 581-597, 614-625, 714-719, 751-803
DisProt Annotation
TM Helix Prediction No TM helices
Bibliography 1.Hnilicová J, Hozeifi S, Stejskalová E, Dušková E, Poser I, Humpolíčková J, Hof M, Staněk D. The C-terminal domain of Brd2 is important for chromatin interaction and regulation of transcription and alternative splicing. Mol Biol Cell. 2013 Nov;24(22):3557-68. doi: 10.1091/mbc.E13-06-0303. Epub 2013 Sep 18. PMID: 24048450; PMCID: PMC3826993. 2.Zang K, Wang J, Dong M, Sun R, Wang Y, Huang Y, Liu X, Li Y, Wang F, Yu M. Brd2 inhibits adipogenesis via the ERK1/2 signaling pathway in 3T3-L1 adipocytes. PLoS One. 2013 Oct 23;8(10):e78536. doi: 10.1371/journal.pone.0078536. PMID: 24194944; PMCID: PMC3806839. 3.Nakamura Y, Umehara T, Nakano K, Jang MK, Shirouzu M, Morita S, Uda-Tochio H, Hamana H, Terada T, Adachi N, Matsumoto T, Tanaka A, Horikoshi M, Ozato K, Padmanabhan B, Yokoyama S. Crystal structure of the human BRD2 bromodomain: insights into dimerization and recognition of acetylated histone H4. J Biol Chem. 2007 Feb 9;282(6):4193-201. doi: 10.1074/jbc.M605971200. Epub 2006 Dec 5. PMID: 17148447.