Primary Information |
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| BoMiProt ID | Bomi4329 |
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| Protein Name | Bromodomain-containing protein 2 |
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| Organism | Bos taurus |
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| Uniprot Id | Q32S26 |
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| Milk Fraction | Whey |
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| Ref Sequence Id | NP_001039331.1 |
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| Aminoacid Length | 803 |
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| Molecular Weight | 88122 |
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| Fasta Sequence | https://www.uniprot.org/uniprot/Q32S26.fasta |
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| Gene Name | BRD2 |
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| Gene Id | 505358 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| 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). |
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| 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. |
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| PTMs | Phosphorylation on Ser and Thr,Acetylation on Met |
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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
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| Predicted Disorder Regions | 48-67, 194-210, 269-287, 332-341, 469-527, 541-566, 581-597, 614-625, 714-719, 751-803 |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| 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. |
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