SMART: BROMO domain annotation

BROMO bromo domain

SMART accession number:	SM00297
Description:
Interpro abstract (IPR001487):	Bromodomains are found in a variety of mammalian, invertebrate and yeast DNA-binding proteins [(PUBMED:1350857)]. Bromodomains can interact with acetylated lysine [(PUBMED:9175470)]. In some proteins, the classical bromodomain has diverged to such an extent that parts of the region are either missing or contain an insertion (e.g., mammalian protein HRX, Caenorhabditis elegans hypothetical protein ZK783.4, yeast protein YTA7). The bromodomain may occur as a single copy, or in duplicate. The precise function of the domain is unclear, but it may be involved in protein-protein interactions and may play a role in assembly or activity of multi-component complexes involved in transcriptional activation [(PUBMED:7580139)].
GO function:	protein binding (GO:0005515)
Family alignment:	View or

There are 4494 BROMO domains in 3433 proteins in SMART's nrdb database.

Click on the following links for more information.

Evolution (species in which this domain is found)
Click on to expand nodes. To display all proteins with a BROMO domain in a specific node, click on it.

This tree shows only several representative species. The complete taxonomic breakdown of all proteins with BROMO domain is also avaliable.

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Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Kouzarides T
- Acetylation: a regulatory modification to rival phosphorylation?
- EMBO J. 2000; 19: 1176-9
- Display abstract
- The fact that histones are modified by acetylation has been known for almost 30 years. The recent identification of enzymes that regulate histone acetylation has revealed a broader use of this modification than was suspected previously. Acetylases are now known to modify a variety of proteins, including transcription factors, nuclear import factors and alpha-tubulin. Acetylation regulates many diverse functions, including DNA recognition, protein-protein interaction and protein stability. There is even a conserved structure, the bromodomain, that recognizes acetylated residues and may serve as a signalling domain. If you think all this sounds familiar, it should be. These are features characteristic of kinases. So, is acetylation a modification analogous to phosphorylation? This review sets out what we know about the broader substrate specificity and regulation of acetyl- ases and goes on to compare acetylation with the process of phosphorylation.
- Dhalluin C, Carlson JE, Zeng L, He C, Aggarwal AK, Zhou MM
- Structure and ligand of a histone acetyltransferase bromodomain.
- Nature. 1999; 399: 491-6
- Display abstract
- Histone acetylation is important in chromatin remodelling and gene activation. Nearly all known histone-acetyltransferase (HAT)-associated transcriptional co-activators contain bromodomains, which are approximately 110-amino-acid modules found in many chromatin-associated proteins. Despite the wide occurrence of these bromodomains, their three-dimensional structure and binding partners remain unknown. Here we report the solution structure of the bromodomain of the HAT co-activator P/CAF (p300/CBP-associated factor). The structure reveals an unusual left-handed up-and-down four-helix bundle. In addition, we show by a combination of structural and site-directed mutagenesis studies that bromodomains can interact specifically with acetylated lysine, making them the first known protein modules to do so. The nature of the recognition of acetyl-lysine by the P/CAF bromodomain is similar to that of acetyl-CoA by histone acetyltransferase. Thus, the bromodomain is functionally linked to the HAT activity of co-activators in the regulation of gene transcription.
Metabolism (metabolic pathways involving proteins which contain this domain)

Structure (3D structures containing this domain)

3D Structures of BROMO domains in PDB

PDB code	Main view	Title
1e6i		Bromodomain from gcn5 complexed with acetylated h4 peptide
1eqf		Crystal structure of the double bromodomain module from human tafii250
1f68		Nmr solution structure of the bromodomain from human gcn5
1jm4		Nmr structure of p/caf bromodomain in complex with hiv-1 tat peptide
1jsp		Nmr structure of cbp bromodomain in complex with p53 peptide
1n72		Structure and ligand of a histone acetyltransferase bromodomain
1wug		Complex structure of pcaf bromodomain with small chemical ligand np1
1wum		Complex structure of pcaf bromodomain with small chemical ligand np2
1x0j		Crystal structure analysis of the n-terminal bromodomain of human brd2
1zs5		Structure-based evaluation of selective and non-selective small molecules that block hiv-1 tat and pcaf association
2d82		Target structure-based discovery of small molecules that block human p53 and creb binding protein (cbp) association
2d9e		Solution structure of the bromodomain of peregrin
2dat		Solution structure of the bromodomain of human swi/snf related matrix associated actin dependent regulator of cromatin subfamily a member 2
2dkw		Solution structure of the bromodomain of human protein kiaa1240
2dvq		Crystal structure analysis of the n-terminal bromodomain of human brd2 complexed with acetylated histone h4 peptide
2dvr		Crystal structure analysis of the n-terminal bromodomain of human brd2 complexed with acetylated histone h4 peptide
2dvs		Crystal structure analysis of the n-terminal bromodomain of human brd2 complexed with acetylated histone h4 peptide
2dvv		Crystal structure of the second bromodomain of the human brd2 protein
2dww		Crystal structure of bromodomain-containing protein 4
2e3k		Crystal structure of the human brd2 second bromodomain in complexed with the acetylated histone h4 peptide
2e7n		Solution structure of the second bromodomain from human bromodomain-containing protein 3
2e7o		Solution structure of the bromodomain from human bromodomain adjacent to zinc finger domain 2b
2f6j		Crystal structure of phd finger-linker-bromodomain fragment of human bptf in the h3(1-15)k4me3 bound state
2f6n		Crystal structure of phd finger-linker-bromodomain fragment of human bptf in the free form
2fsa		Crystal structure of phd finger-linker-bromodomain fragment of human bptf in the h3(1-15)k4me2 bound state
2g4a		Solution structure of a bromodomain from ring3 protein
2grc		1.5 a structure of bromodomain from human brg1 protein, a central atpase of swi/snf remodeling complex
2h60		Solution structure of human brg1 bromodomain
2i7k		Solution structure of the bromodomain of human brd7 protein
2i8n		Solution structure of the second bromodomain of brd4
2nxb		Crystal structure of human bromodomain containing protein 3 (brd3)
2oo1		Crystal structure of the bromo domain 2 of human bromodomain containing protein 3 (brd3)
2oss		Crystal structure of the bromo domain 1 in human bromodomain containing protein 4 (brd4)
2ouo		Crystal structure of the bromo domain 2 in human bromodomain containing protein 4 (brd4)
2r0s		Crystal structure of the rsc4 tandem bromodomain
2r0v		Structure of the rsc4 tandem bromodomain acetylated at k25
2r0y		Structure of the rsc4 tandem bromodomain in complex with an acetylated h3 peptide
2r10		Structure of an acetylated rsc4 tandem bromodomain histone chimera
2rfj		Crystal structure of the bromo domain 1 in human bromodomain containing protein, testis specific (brdt)
2ri7		Crystal structure of phd finger-linker-bromodomain y17e mutant from human bptf in the h3(1-9)k4me2 bound state
2rnw		The structural basis for site-specific lysine-acetylated histone recognition by the bromodomains of the human transcriptional co-activators pcaf and cbp
2rnx		The structural basis for site-specific lysine-acetylated histone recognition by the bromodomains of the human transcriptional co-activators pcaf and cbp
2rny		Complex structures of cbp bromodomain with h4 ack20 peptide
2ro1		Nmr solution structures of human kap1 phd finger-bromodomain
2wp1		Structure of brdt bromodomain 2 bound to an acetylated histone h3 peptide
2wp2		Structure of brdt bromodomain bd1 bound to a diacetylated histone h4 peptide.
2yqd		Solution structure of the fifth bromodomain from mouse polybromo-1
2yw5		Solution structure of the bromodomain from human bromodomain containing protein 3
2yyn		Crystal sturcture of human bromodomain protein
3d7c		Crystal structure of the bromodomain of human gcn5, the general control of amino-acid synthesis protein 5-like 2
3dai		Crystal structure of the bromodomain of the human atad2 (casp target)
3dwy		Crystal structure of the bromodomain of human crebbp
3fkm		Plasmodium falciparum bromodomain-containing protein pf10_0328
3g0j		Crystal structure of the fifth bromodomain of human poly- bromodomain containing protein 1 (pb1)
3g0l		Crystal structure of human bromodomain adjacent to zinc finger domain 2b (baz2b)
3gg3		Crystal structure of the bromodomain of human pcaf
3hme		Crystal structure of human bromodomain containing 9 isoform (brd9)
3hmf		Crystal structure of the second bromodomain of human poly- bromodomain containing protein 1 (pb1)
3hmh		Crystal structure of the second bromodomain of human tbp- associated factor rna polymerase 1-like (taf1l)
3i3j		Crystal structure of the bromodomain of human ep300
3iu5		Crystal structure of the first bromodomain of human poly- bromodomain containing protein 1 (pb1)
3iu6		Crystal structure of the sixth bromodomain of human poly- bromodomain containing protein 1 (pb1)
3jvj		Crystal structure of the bromodomain 1 in mouse brd4
3jvk		Crystal structure of bromodomain 1 of mouse brd4 in complex with histone h3-k(ac)14
3jvl		Crystal structure of bromodomain 2 of mouse brd4
3jvm		Crystal structure of bromodomain 2 of mouse brd4
3k2j		Crystal structure of the 3rd bromodomain of human poly- bromodomain containing protein 1 (pb1)

Links (links to other resources describing this domain)
PFAM bromodomain
INTERPRO IPR001487
PROSITE BROMODOMAIN_2

PFAM	bromodomain
INTERPRO	IPR001487
PROSITE	BROMODOMAIN_2