UniProtKB - O60885 (BRD4_HUMAN)
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- BLAST>sp|O60885|BRD4_HUMAN Bromodomain-containing protein 4 OS=Homo sapiens OX=9606 GN=BRD4 PE=1 SV=2 MSAESGPGTRLRNLPVMGDGLETSQMSTTQAQAQPQPANAASTNPPPPETSNPNKPKRQT NQLQYLLRVVLKTLWKHQFAWPFQQPVDAVKLNLPDYYKIIKTPMDMGTIKKRLENNYYW NAQECIQDFNTMFTNCYIYNKPGDDIVLMAEALEKLFLQKINELPTEETEIMIVQAKGRG RGRKETGTAKPGVSTVPNTTQASTPPQTQTPQPNPPPVQATPHPFPAVTPDLIVQTPVMT VVPPQPLQTPPPVPPQPQPPPAPAPQPVQSHPPIIAATPQPVKTKKGVKRKADTTTPTTI DPIHEPPSLPPEPKTTKLGQRRESSRPVKPPKKDVPDSQQHPAPEKSSKVSEQLKCCSGI LKEMFAKKHAAYAWPFYKPVDVEALGLHDYCDIIKHPMDMSTIKSKLEAREYRDAQEFGA DVRLMFSNCYKYNPPDHEVVAMARKLQDVFEMRFAKMPDEPEEPVVAVSSPAVPPPTKVV APPSSSDSSSDSSSDSDSSTDDSEEERAQRLAELQEQLKAVHEQLAALSQPQQNKPKKKE KDKKEKKKEKHKRKEEVEENKKSKAKEPPPKKTKKNNSSNSNVSKKEPAPMKSKPPPTYE SEEEDKCKPMSYEEKRQLSLDINKLPGEKLGRVVHIIQSREPSLKNSNPDEIEIDFETLK PSTLRELERYVTSCLRKKRKPQAEKVDVIAGSSKMKGFSSSESESSSESSSSDSEDSETE MAPKSKKKGHPGREQKKHHHHHHQQMQQAPAPVPQQPPPPPQQPPPPPPPQQQQQPPPPP PPPSMPQQAAPAMKSSPPPFIATQVPVLEPQLPGSVFDPIGHFTQPILHLPQPELPPHLP QPPEHSTPPHLNQHAVVSPPALHNALPQQPSRPSNRAAALPPKPARPPAVSPALTQTPLL PQPPMAQPPQVLLEDEEPPAPPLTSMQMQLYLQQLQKVQPPTPLLPSVKVQSQPPPPLPP PPHPSVQQQLQQQPPPPPPPQPQPPPQQQHQPPPRPVHLQPMQFSTHIQQPPPPQGQQPP HPPPGQQPPPPQPAKPQQVIQHHHSPRHHKSDPYSTGHLREAPSPLMIHSPQMSQFQSLT HQSPPQQNVQPKKQELRAASVVQPQPLVVVKEEKIHSPIIRSEPFSPSLRPEPPKHPESI KAPVHLPQRPEMKPVDVGRPVIRPPEQNAPPPGAPDKDKQKQEPKTPVAPKKDLKIKNMG SWASLVQKHPTTPSSTAKSSSDSFEQFRRAAREKEEREKALKAQAEHAEKEKERLRQERM RSREDEDALEQARRAHEEARRRQEQQQQQRQEQQQQQQQQAAAVAAAATPQAQSSQPQSM LDQQRELARKREQERRRREAMAATIDMNFQSDLLSIFEENLF
- Align
Bromodomain-containing protein 4
BRD4
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.25"BRD4 is an atypical kinase that phosphorylates serine2 of the RNA polymerase II carboxy-terminal domain."
Devaiah B.N., Lewis B.A., Cherman N., Hewitt M.C., Albrecht B.K., Robey P.G., Ozato K., Sims R.J. III, Singer D.S.
Proc. Natl. Acad. Sci. U.S.A. 109:6927-6932(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION.
Miscellaneous
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.38"Selective inhibition of BET bromodomains."
Filippakopoulos P., Qi J., Picaud S., Shen Y., Smith W.B., Fedorov O., Morse E.M., Keates T., Hickman T.T., Felletar I., Philpott M., Munro S., McKeown M.R., Wang Y., Christie A.L., West N., Cameron M.J., Schwartz B. , Heightman T.D., La Thangue N., French C.A., Wiest O., Kung A.L., Knapp S., Bradner J.E.
Nature 468:1067-1073(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 44-168 IN COMPLEX WITH JQ1 INHIBITOR, SUBCELLULAR LOCATION. - Ref.39"Suppression of inflammation by a synthetic histone mimic."
Nicodeme E., Jeffrey K.L., Schaefer U., Beinke S., Dewell S., Chung C.W., Chandwani R., Marazzi I., Wilson P., Coste H., White J., Kirilovsky J., Rice C.M., Lora J.M., Prinjha R.K., Lee K., Tarakhovsky A.
Nature 468:1119-1123(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 44-168 IN COMPLEX WITH I-BET INHIBITOR. - Ref.41"Inhibition of BET recruitment to chromatin as an effective treatment for MLL-fusion leukaemia."
Dawson M.A., Prinjha R.K., Dittmann A., Giotopoulos G., Bantscheff M., Chan W.I., Robson S.C., Chung C.W., Hopf C., Savitski M.M., Huthmacher C., Gudgin E., Lugo D., Beinke S., Chapman T.D., Roberts E.J., Soden P.E., Auger K.R. , Mirguet O., Doehner K., Delwel R., Burnett A.K., Jeffrey P., Drewes G., Lee K., Huntly B.J., Kouzarides T.
Nature 478:529-533(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 44-168 IN COMPLEX WITH JQ1 INHIBITOR.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 140 | Acetylated histones1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 140 | Inhibitor | 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 433 | Acetylated histones1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 433 | Inhibitor | 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- chromatin binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- lysine-acetylated histone binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- p53 binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- RNA polymerase II core binding Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- cellular response to DNA damage stimulus Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- chromatin organization Source: UniProtKB-KW
- chromatin remodeling Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- negative regulation of DNA damage checkpoint Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of G2/M transition of mitotic cell cycle Source: MGI <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of transcription by RNA polymerase II Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of transcription elongation from RNA polymerase II promoter Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- regulation of inflammatory response Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- regulation of phosphorylation of RNA polymerase II C-terminal domain Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- regulation of transcription involved in G1/S transition of mitotic cell cycle Source: MGI <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- transcription, DNA-templated Source: UniProtKB-KW
- viral process Source: UniProtKB-KW
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Chromatin regulator |
| Biological process | DNA damage, Host-virus interaction, Transcription, Transcription regulation |
Enzyme and pathway databases
SIGNOR Signaling Network Open Resource More...SIGNORi | O60885 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Bromodomain-containing protein 4Alternative name(s): Protein HUNK1 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:BRD4 Synonyms:HUNK1 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
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Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000141867.17 |
Human Gene Nomenclature Database More...HGNCi | HGNC:13575 BRD4 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 608749 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_O60885 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Nucleus
Other locations
Note: Associates with acetylated chromatin. Released from chromatin upon deacetylation of histones that can be triggered by different signals such as activation of the JNK pathway or nocodazole treatment.
Cytosol
- cytosol Source: HPA
Nucleus
- condensed nuclear chromosome Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- nucleoplasm Source: HPA
- nucleus Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Other locations
- chromosome Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Chromosome, Nucleus<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"BRD4 bromodomain gene rearrangement in aggressive carcinoma with translocation t(15;19)."
French C.A., Miyoshi I., Aster J.C., Kubonishi I., Kroll T.G., Dal Cin P., Vargas S.O., Perez-Atayde A.R., Fletcher J.A.
Am. J. Pathol. 159:1987-1992(2001) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), DISEASE, CHROMOSOMAL TRANSLOCATION WITH NUT. - Ref.6"BRD4-NUT fusion oncogene: a novel mechanism in aggressive carcinoma."
French C.A., Miyoshi I., Kubonishi I., Grier H.E., Perez-Atayde A.R., Fletcher J.A.
Cancer Res. 63:304-307(2003) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-719, DISEASE, CHROMOSOMAL TRANSLOCATION WITH NUT, TISSUE SPECIFICITY.
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 140 | N → A: Abolishes binding to acetylated histones. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 433 | N → A: Abolishes binding to acetylated histones. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 492 – 494 | SSS → ASA: Impaired phosphorylation by CK2 and binding to acetylated histones. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 3 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 498 – 500 | SST → AAA: Impaired phosphorylation by CK2 and binding to acetylated histones. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 3 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 503 | S → A: Impaired phosphorylation by CK2 and binding to acetylated histones. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 719 – 720 | Breakpoint for translocation to form BDR4-NUT fusion protein | 2 |
Organism-specific databases
DisGeNET More...DisGeNETi | 23476 |
MalaCards human disease database More...MalaCardsi | BRD4 |
Open Targets More...OpenTargetsi | ENSG00000141867 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA25416 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL1163125 |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 1945 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | BRD4 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000211183 | 1 – 1362 | Bromodomain-containing protein 4Add BLAST | 1362 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 99 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 470 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 484 | Phosphoserine; by CK21 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 488 | Phosphoserine; by CK21 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 492 | Phosphoserine; by CK21 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 494 | Phosphoserine; by CK21 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 498 | Phosphoserine; by CK21 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 499 | Phosphoserine; by CK21 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 503 | Phosphoserine; by CK21 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 585 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 601 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 645 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 694 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 1050 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1111 | N6-acetyllysine; alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 1111 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 1111 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1117 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1126 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 1197 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1201 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1204 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.27"Phospho switch triggers Brd4 chromatin binding and activator recruitment for gene-specific targeting."
Wu S.Y., Lee A.Y., Lai H.T., Zhang H., Chiang C.M.
Mol. Cell 49:843-857(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH TP53, PHOSPHORYLATION AT SER-484; SER-488; SER-492; SER-494; SER-498; SER-499 AND SER-503, MUTAGENESIS OF 492-SER--SER-494; 498-SER--THR-500 AND SER-503.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | O60885 |
MaxQB - The MaxQuant DataBase More...MaxQBi | O60885 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | O60885 |
PeptideAtlas More...PeptideAtlasi | O60885 |
PRoteomics IDEntifications database More...PRIDEi | O60885 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 49651 49652 [O60885-2] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | O60885 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | O60885 |
Miscellaneous databases
CutDB - Proteolytic event database More...PMAP-CutDBi | O60885 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.6"BRD4-NUT fusion oncogene: a novel mechanism in aggressive carcinoma."
French C.A., Miyoshi I., Kubonishi I., Grier H.E., Perez-Atayde A.R., Fletcher J.A.
Cancer Res. 63:304-307(2003) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-719, DISEASE, CHROMOSOMAL TRANSLOCATION WITH NUT, TISSUE SPECIFICITY.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000141867 |
CleanEx database of gene expression profiles More...CleanExi | HS_BRD4 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | O60885 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | O60885 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB068177 CAB068178 HPA015055 HPA061646 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"The bromodomain protein Brd4 is a positive regulatory component of P-TEFb and stimulates RNA polymerase II-dependent transcription."
Jang M.K., Mochizuki K., Zhou M., Jeong H.S., Brady J.N., Ozato K.
Mol. Cell 19:523-534(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH CDK9 AND CCNT1, IDENTIFICATION IN THE P-TEFB COMPLEX, SUBCELLULAR LOCATION. - Ref.8"Recruitment of P-TEFb for stimulation of transcriptional elongation by the bromodomain protein Brd4."
Yang Z., Yik J.H., Chen R., He N., Jang M.K., Ozato K., Zhou Q.
Mol. Cell 19:535-545(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH CDK9 AND CCNT1, IDENTIFICATION IN THE P-TEFB COMPLEX. - Ref.16"Brd4 coactivates transcriptional activation of NF-kappaB via specific binding to acetylated RelA."
Huang B., Yang X.D., Zhou M.M., Ozato K., Chen L.F.
Mol. Cell. Biol. 29:1375-1387(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH RELA. - Ref.20"The Brd4 extraterminal domain confers transcription activation independent of pTEFb by recruiting multiple proteins, including NSD3."
Rahman S., Sowa M.E., Ottinger M., Smith J.A., Shi Y., Harper J.W., Howley P.M.
Mol. Cell. Biol. 31:2641-2652(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH WHSC1L1; JMJD6; CHD4; GLTSCR1 AND ATAD5. - Ref.27"Phospho switch triggers Brd4 chromatin binding and activator recruitment for gene-specific targeting."
Wu S.Y., Lee A.Y., Lai H.T., Zhang H., Chiang C.M.
Mol. Cell 49:843-857(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH TP53, PHOSPHORYLATION AT SER-484; SER-488; SER-492; SER-494; SER-498; SER-499 AND SER-503, MUTAGENESIS OF 492-SER--SER-494; 498-SER--THR-500 AND SER-503. - Ref.29"The bromodomain protein Brd4 insulates chromatin from DNA damage signalling."
Floyd S.R., Pacold M.E., Huang Q., Clarke S.M., Lam F.C., Cannell I.G., Bryson B.D., Rameseder J., Lee M.J., Blake E.J., Fydrych A., Ho R., Greenberger B.A., Chen G.C., Maffa A., Del Rosario A.M., Root D.E., Carpenter A.E. , Hahn W.C., Sabatini D.M., Chen C.C., White F.M., Bradner J.E., Yaffe M.B.
Nature 498:246-250(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (ISOFORM B), SUBCELLULAR LOCATION (ISOFORM B), INTERACTION WITH NCAPD3 AND SMC2, MUTAGENESIS OF ASN-140. - Ref.38"Selective inhibition of BET bromodomains."
Filippakopoulos P., Qi J., Picaud S., Shen Y., Smith W.B., Fedorov O., Morse E.M., Keates T., Hickman T.T., Felletar I., Philpott M., Munro S., McKeown M.R., Wang Y., Christie A.L., West N., Cameron M.J., Schwartz B. , Heightman T.D., La Thangue N., French C.A., Wiest O., Kung A.L., Knapp S., Bradner J.E.
Nature 468:1067-1073(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 44-168 IN COMPLEX WITH JQ1 INHIBITOR, SUBCELLULAR LOCATION. - Ref.39"Suppression of inflammation by a synthetic histone mimic."
Nicodeme E., Jeffrey K.L., Schaefer U., Beinke S., Dewell S., Chung C.W., Chandwani R., Marazzi I., Wilson P., Coste H., White J., Kirilovsky J., Rice C.M., Lora J.M., Prinjha R.K., Lee K., Tarakhovsky A.
Nature 468:1119-1123(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 44-168 IN COMPLEX WITH I-BET INHIBITOR. - Ref.41"Inhibition of BET recruitment to chromatin as an effective treatment for MLL-fusion leukaemia."
Dawson M.A., Prinjha R.K., Dittmann A., Giotopoulos G., Bantscheff M., Chan W.I., Robson S.C., Chung C.W., Hopf C., Savitski M.M., Huthmacher C., Gudgin E., Lugo D., Beinke S., Chapman T.D., Roberts E.J., Soden P.E., Auger K.R. , Mirguet O., Doehner K., Delwel R., Burnett A.K., Jeffrey P., Drewes G., Lee K., Huntly B.J., Kouzarides T.
Nature 478:529-533(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 44-168 IN COMPLEX WITH JQ1 INHIBITOR. - Ref.42"Benzodiazepines and benzotriazepines as protein interaction inhibitors targeting bromodomains of the BET family."
Filippakopoulos P., Picaud S., Fedorov O., Keller M., Wrobel M., Morgenstern O., Bracher F., Knapp S.
Bioorg. Med. Chem. 20:1878-1886(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 44-168 IN COMPLEX WITH BENZODIAZEPINES AND BENZOTRIAZEPINES INHIBITORS. - Ref.44"Fragment-based discovery of bromodomain inhibitors part 1: inhibitor binding modes and implications for lead discovery."
Chung C.W., Dean A.W., Woolven J.M., Bamborough P.
J. Med. Chem. 55:576-586(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 44-168 IN COMPLEX WITH BENZODIAZEPINES INHIBITORS. - Ref.46"Histone recognition and large-scale structural analysis of the human bromodomain family."
Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P., Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T., Gingras A.C., Arrowsmith C.H., Knapp S.
Cell 149:214-231(2012) [PubMed] [Europe PMC] [Abstract] - Ref.47"Optimization of 3,5-dimethylisoxazole derivatives as potent bromodomain ligands."
Hewings D.S., Fedorov O., Filippakopoulos P., Martin S., Picaud S., Tumber A., Wells C., Olcina M.M., Freeman K., Gill A., Ritchie A.J., Sheppard D.W., Russell A.J., Hammond E.M., Knapp S., Brennan P.E., Conway S.J.
J. Med. Chem. 56:3217-3227(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 44-168 IN COMPLEX WITH 3,5-DIMETHYLISOXAZOLE INHIBITOR. - Ref.48"Fragment-based drug discovery of 2-thiazolidinones as inhibitors of the histone reader BRD4 bromodomain."
Zhao L., Cao D., Chen T., Wang Y., Miao Z., Xu Y., Chen W., Wang X., Li Y., Du Z., Xiong B., Li J., Xu C., Zhang N., He J., Shen J.
J. Med. Chem. 56:3833-3851(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 44-167 IN COMPLEX WITH 2-THIAZOLIDINONE INHIBITOR.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"ChlR1 is required for loading papillomavirus E2 onto mitotic chromosomes and viral genome maintenance."
Parish J.L., Bean A.M., Park R.B., Androphy E.J.
Mol. Cell 24:867-876(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH BOVINE PAPILLOMAVIRUS TYPE 1 REGULATORY PROTEIN E2.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.12"The EBNA1 protein of Epstein-Barr virus functionally interacts with Brd4."
Lin A., Wang S., Nguyen T., Shire K., Frappier L.
J. Virol. 82:12009-12019(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH EPSTEIN-BARR VIRUS PROTEIN EBNA1.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"Kaposi's sarcoma-associated herpesvirus latency-associated nuclear antigen interacts with bromodomain protein Brd4 on host mitotic chromosomes."
You J., Srinivasan V., Denis G.V., Harrington W.J. Jr., Ballestas M.E., Kaye K.M., Howley P.M.
J. Virol. 80:8909-8919(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH KSHV PROTEIN LANA (MICROBIAL INFECTION).
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- lysine-acetylated histone binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- p53 binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- RNA polymerase II core binding Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 117036, 98 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | O60885 |
Database of interacting proteins More...DIPi | DIP-39776N |
Protein interaction database and analysis system More...IntActi | O60885, 45 interactors |
Molecular INTeraction database More...MINTi | O60885 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000263377 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | O60885 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 53 – 55 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 61 – 68 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 70 – 75 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 81 – 83 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 89 – 93 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 97 – 100 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 107 – 115 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 122 – 139 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 18 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 145 – 161 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 342 – 346 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 350 – 364 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 367 – 369 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 370 – 373 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 374 – 376 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 382 – 385 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 390 – 393 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 400 – 408 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 412 – 414 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 415 – 432 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 18 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 435 – 437 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 438 – 454 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 602 – 605 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 612 – 624 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 627 – 640 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 642 – 644 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 651 – 655 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 656 – 658 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 661 – 675 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 676 – 678 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 1345 – 1354 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 1355 – 1357 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | O60885 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | O60885 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | O60885 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 75 – 147 | Bromo 1PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 73 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 368 – 440 | Bromo 2PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 73 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 600 – 682 | NETPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 83 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 484 – 503 | NPS regionAdd BLAST | 20 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 524 – 579 | BID regionAdd BLAST | 56 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 1047 – 1362 | C-terminal (CTD) regionAdd BLAST | 316 |
Compositional bias
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 535 – 594 | Lys-richAdd BLAST | 60 | |
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 692 – 717 | Ser-richAdd BLAST | 26 | |
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 703 – 714 | Poly-SerAdd BLAST | 12 | |
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 738 – 743 | Poly-His | 6 | |
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 757 – 761 | Poly-Pro | 5 | |
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 764 – 770 | Poly-Pro | 7 | |
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 771 – 775 | Poly-Gln | 5 | |
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 776 – 783 | Poly-Pro | 8 | |
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 954 – 964 | Poly-ProAdd BLAST | 11 | |
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 974 – 986 | Poly-ProAdd BLAST | 13 | |
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 1011 – 1014 | Poly-Pro | 4 | |
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 1028 – 1033 | Poly-Pro | 6 | |
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 1283 – 1300 | Poly-GlnAdd BLAST | 18 | |
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 1301 – 1308 | Poly-Ala | 8 | |
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 1335 – 1338 | Poly-Arg | 4 |
<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.20"The Brd4 extraterminal domain confers transcription activation independent of pTEFb by recruiting multiple proteins, including NSD3."
Rahman S., Sowa M.E., Ottinger M., Smith J.A., Shi Y., Harper J.W., Howley P.M.
Mol. Cell. Biol. 31:2641-2652(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH WHSC1L1; JMJD6; CHD4; GLTSCR1 AND ATAD5.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"The bromodomain protein Brd4 is a positive regulatory component of P-TEFb and stimulates RNA polymerase II-dependent transcription."
Jang M.K., Mochizuki K., Zhou M., Jeong H.S., Brady J.N., Ozato K.
Mol. Cell 19:523-534(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH CDK9 AND CCNT1, IDENTIFICATION IN THE P-TEFB COMPLEX, SUBCELLULAR LOCATION. - Ref.8"Recruitment of P-TEFb for stimulation of transcriptional elongation by the bromodomain protein Brd4."
Yang Z., Yik J.H., Chen R., He N., Jang M.K., Ozato K., Zhou Q.
Mol. Cell 19:535-545(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH CDK9 AND CCNT1, IDENTIFICATION IN THE P-TEFB COMPLEX. - Ref.23"Bromodomain protein Brd4 associated with acetylated chromatin is important for maintenance of higher-order chromatin structure."
Wang R., Li Q., Helfer C.M., Jiao J., You J.
J. Biol. Chem. 287:10738-10752(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.38"Selective inhibition of BET bromodomains."
Filippakopoulos P., Qi J., Picaud S., Shen Y., Smith W.B., Fedorov O., Morse E.M., Keates T., Hickman T.T., Felletar I., Philpott M., Munro S., McKeown M.R., Wang Y., Christie A.L., West N., Cameron M.J., Schwartz B. , Heightman T.D., La Thangue N., French C.A., Wiest O., Kung A.L., Knapp S., Bradner J.E.
Nature 468:1067-1073(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 44-168 IN COMPLEX WITH JQ1 INHIBITOR, SUBCELLULAR LOCATION. - Ref.42"Benzodiazepines and benzotriazepines as protein interaction inhibitors targeting bromodomains of the BET family."
Filippakopoulos P., Picaud S., Fedorov O., Keller M., Wrobel M., Morgenstern O., Bracher F., Knapp S.
Bioorg. Med. Chem. 20:1878-1886(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 44-168 IN COMPLEX WITH BENZODIAZEPINES AND BENZOTRIAZEPINES INHIBITORS. - Ref.44"Fragment-based discovery of bromodomain inhibitors part 1: inhibitor binding modes and implications for lead discovery."
Chung C.W., Dean A.W., Woolven J.M., Bamborough P.
J. Med. Chem. 55:576-586(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 44-168 IN COMPLEX WITH BENZODIAZEPINES INHIBITORS. - Ref.46"Histone recognition and large-scale structural analysis of the human bromodomain family."
Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P., Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T., Gingras A.C., Arrowsmith C.H., Knapp S.
Cell 149:214-231(2012) [PubMed] [Europe PMC] [Abstract] - Ref.47"Optimization of 3,5-dimethylisoxazole derivatives as potent bromodomain ligands."
Hewings D.S., Fedorov O., Filippakopoulos P., Martin S., Picaud S., Tumber A., Wells C., Olcina M.M., Freeman K., Gill A., Ritchie A.J., Sheppard D.W., Russell A.J., Hammond E.M., Knapp S., Brennan P.E., Conway S.J.
J. Med. Chem. 56:3217-3227(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 44-168 IN COMPLEX WITH 3,5-DIMETHYLISOXAZOLE INHIBITOR. - Ref.48"Fragment-based drug discovery of 2-thiazolidinones as inhibitors of the histone reader BRD4 bromodomain."
Zhao L., Cao D., Chen T., Wang Y., Miao Z., Xu Y., Chen W., Wang X., Li Y., Du Z., Xiong B., Li J., Xu C., Zhang N., He J., Shen J.
J. Med. Chem. 56:3833-3851(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 44-167 IN COMPLEX WITH 2-THIAZOLIDINONE INHIBITOR.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
Bromodomain, RepeatPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1474 Eukaryota COG5076 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00920000148952 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000231200 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG004896 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | O60885 |
KEGG Orthology (KO) More...KOi | K11722 |
Identification of Orthologs from Complete Genome Data More...OMAi | RPPEQNA |
Database of Orthologous Groups More...OrthoDBi | EOG091G01QC |
Database for complete collections of gene phylogenies More...PhylomeDBi | O60885 |
TreeFam database of animal gene trees More...TreeFami | TF317345 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.20.1270.220, 1 hit 1.20.920.10, 2 hits |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR031354 BRD4_CDT IPR001487 Bromodomain IPR036427 Bromodomain-like_sf IPR018359 Bromodomain_CS IPR027353 NET_dom IPR038336 NET_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF17035 BET, 1 hit PF17105 BRD4_CDT, 1 hit PF00439 Bromodomain, 2 hits |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00503 BROMODOMAIN |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00297 BROMO, 2 hits |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF47370 SSF47370, 2 hits |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00633 BROMODOMAIN_1, 1 hit PS50014 BROMODOMAIN_2, 2 hits PS51525 NET, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MSAESGPGTR LRNLPVMGDG LETSQMSTTQ AQAQPQPANA ASTNPPPPET
60 70 80 90 100
SNPNKPKRQT NQLQYLLRVV LKTLWKHQFA WPFQQPVDAV KLNLPDYYKI
110 120 130 140 150
IKTPMDMGTI KKRLENNYYW NAQECIQDFN TMFTNCYIYN KPGDDIVLMA
160 170 180 190 200
EALEKLFLQK INELPTEETE IMIVQAKGRG RGRKETGTAK PGVSTVPNTT
210 220 230 240 250
QASTPPQTQT PQPNPPPVQA TPHPFPAVTP DLIVQTPVMT VVPPQPLQTP
260 270 280 290 300
PPVPPQPQPP PAPAPQPVQS HPPIIAATPQ PVKTKKGVKR KADTTTPTTI
310 320 330 340 350
DPIHEPPSLP PEPKTTKLGQ RRESSRPVKP PKKDVPDSQQ HPAPEKSSKV
360 370 380 390 400
SEQLKCCSGI LKEMFAKKHA AYAWPFYKPV DVEALGLHDY CDIIKHPMDM
410 420 430 440 450
STIKSKLEAR EYRDAQEFGA DVRLMFSNCY KYNPPDHEVV AMARKLQDVF
460 470 480 490 500
EMRFAKMPDE PEEPVVAVSS PAVPPPTKVV APPSSSDSSS DSSSDSDSST
510 520 530 540 550
DDSEEERAQR LAELQEQLKA VHEQLAALSQ PQQNKPKKKE KDKKEKKKEK
560 570 580 590 600
HKRKEEVEEN KKSKAKEPPP KKTKKNNSSN SNVSKKEPAP MKSKPPPTYE
610 620 630 640 650
SEEEDKCKPM SYEEKRQLSL DINKLPGEKL GRVVHIIQSR EPSLKNSNPD
660 670 680 690 700
EIEIDFETLK PSTLRELERY VTSCLRKKRK PQAEKVDVIA GSSKMKGFSS
710 720 730 740 750
SESESSSESS SSDSEDSETE MAPKSKKKGH PGREQKKHHH HHHQQMQQAP
760 770 780 790 800
APVPQQPPPP PQQPPPPPPP QQQQQPPPPP PPPSMPQQAA PAMKSSPPPF
810 820 830 840 850
IATQVPVLEP QLPGSVFDPI GHFTQPILHL PQPELPPHLP QPPEHSTPPH
860 870 880 890 900
LNQHAVVSPP ALHNALPQQP SRPSNRAAAL PPKPARPPAV SPALTQTPLL
910 920 930 940 950
PQPPMAQPPQ VLLEDEEPPA PPLTSMQMQL YLQQLQKVQP PTPLLPSVKV
960 970 980 990 1000
QSQPPPPLPP PPHPSVQQQL QQQPPPPPPP QPQPPPQQQH QPPPRPVHLQ
1010 1020 1030 1040 1050
PMQFSTHIQQ PPPPQGQQPP HPPPGQQPPP PQPAKPQQVI QHHHSPRHHK
1060 1070 1080 1090 1100
SDPYSTGHLR EAPSPLMIHS PQMSQFQSLT HQSPPQQNVQ PKKQELRAAS
1110 1120 1130 1140 1150
VVQPQPLVVV KEEKIHSPII RSEPFSPSLR PEPPKHPESI KAPVHLPQRP
1160 1170 1180 1190 1200
EMKPVDVGRP VIRPPEQNAP PPGAPDKDKQ KQEPKTPVAP KKDLKIKNMG
1210 1220 1230 1240 1250
SWASLVQKHP TTPSSTAKSS SDSFEQFRRA AREKEEREKA LKAQAEHAEK
1260 1270 1280 1290 1300
EKERLRQERM RSREDEDALE QARRAHEEAR RRQEQQQQQR QEQQQQQQQQ
1310 1320 1330 1340 1350
AAAVAAAATP QAQSSQPQSM LDQQRELARK REQERRRREA MAATIDMNFQ
1360
SDLLSIFEEN LF
The sequence of this isoform differs from the canonical sequence as follows:
720-722: EMA → GPA
723-1362: Missing.
10 20 30 40 50
MSAESGPGTR LRNLPVMGDG LETSQMSTTQ AQAQPQPANA ASTNPPPPET
60 70 80 90 100
SNPNKPKRQT NQLQYLLRVV LKTLWKHQFA WPFQQPVDAV KLNLPDYYKI
110 120 130 140 150
IKTPMDMGTI KKRLENNYYW NAQECIQDFN TMFTNCYIYN KPGDDIVLMA
160 170 180 190 200
EALEKLFLQK INELPTEETE IMIVQAKGRG RGRKETGTAK PGVSTVPNTT
210 220 230 240 250
QASTPPQTQT PQPNPPPVQA TPHPFPAVTP DLIVQTPVMT VVPPQPLQTP
260 270 280 290 300
PPVPPQPQPP PAPAPQPVQS HPPIIAATPQ PVKTKKGVKR KADTTTPTTI
310 320 330 340 350
DPIHEPPSLP PEPKTTKLGQ RRESSRPVKP PKKDVPDSQQ HPAPEKSSKV
360 370 380 390 400
SEQLKCCSGI LKEMFAKKHA AYAWPFYKPV DVEALGLHDY CDIIKHPMDM
410 420 430 440 450
STIKSKLEAR EYRDAQEFGA DVRLMFSNCY KYNPPDHEVV AMARKLQDVF
460 470 480 490 500
EMRFAKMPDE PEEPVVAVSS PAVPPPTKVV APPSSSDSSS DSSSDSDSST
510 520 530 540 550
DDSEEERAQR LAELQEQLKA VHEQLAALSQ PQQNKPKKKE KDKKEKKKEK
560 570 580 590 600
HKRKEEVEEN KKSKAKEPPP KKTKKNNSSN SNVSKKEPAP MKSKPPPTYE
610 620 630 640 650
SEEEDKCKPM SYEEKRQLSL DINKLPGEKL GRVVHIIQSR EPSLKNSNPD
660 670 680 690 700
EIEIDFETLK PSTLRELERY VTSCLRKKRK PQAEKVDVIA GSSKMKGFSS
710 720
SESESSSESS SSDSEDSETG PA
The sequence of this isoform differs from the canonical sequence as follows:
720-1362: EMAPKSKKKG...LLSIFEENLF → AFCTSGDFVS...ECARCCVGCS
10 20 30 40 50
MSAESGPGTR LRNLPVMGDG LETSQMSTTQ AQAQPQPANA ASTNPPPPET
60 70 80 90 100
SNPNKPKRQT NQLQYLLRVV LKTLWKHQFA WPFQQPVDAV KLNLPDYYKI
110 120 130 140 150
IKTPMDMGTI KKRLENNYYW NAQECIQDFN TMFTNCYIYN KPGDDIVLMA
160 170 180 190 200
EALEKLFLQK INELPTEETE IMIVQAKGRG RGRKETGTAK PGVSTVPNTT
210 220 230 240 250
QASTPPQTQT PQPNPPPVQA TPHPFPAVTP DLIVQTPVMT VVPPQPLQTP
260 270 280 290 300
PPVPPQPQPP PAPAPQPVQS HPPIIAATPQ PVKTKKGVKR KADTTTPTTI
310 320 330 340 350
DPIHEPPSLP PEPKTTKLGQ RRESSRPVKP PKKDVPDSQQ HPAPEKSSKV
360 370 380 390 400
SEQLKCCSGI LKEMFAKKHA AYAWPFYKPV DVEALGLHDY CDIIKHPMDM
410 420 430 440 450
STIKSKLEAR EYRDAQEFGA DVRLMFSNCY KYNPPDHEVV AMARKLQDVF
460 470 480 490 500
EMRFAKMPDE PEEPVVAVSS PAVPPPTKVV APPSSSDSSS DSSSDSDSST
510 520 530 540 550
DDSEEERAQR LAELQEQLKA VHEQLAALSQ PQQNKPKKKE KDKKEKKKEK
560 570 580 590 600
HKRKEEVEEN KKSKAKEPPP KKTKKNNSSN SNVSKKEPAP MKSKPPPTYE
610 620 630 640 650
SEEEDKCKPM SYEEKRQLSL DINKLPGEKL GRVVHIIQSR EPSLKNSNPD
660 670 680 690 700
EIEIDFETLK PSTLRELERY VTSCLRKKRK PQAEKVDVIA GSSKMKGFSS
710 720 730 740 750
SESESSSESS SSDSEDSETA FCTSGDFVSP GPSPYHSHVQ CGRFREMLRW
760 770 780 790
FLVDVEQTAA GQPHRQSAAG PAITWAPAIA YPSPECARCC VGCS
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_041919 | 37 | P → S1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_041920 | 371 | A → G1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_041921 | 563 | S → N1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_041922 | 598 | T → S1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_041923 | 669 | R → H1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_048427 | 1097 | R → H. Corresponds to variant dbSNP:rs35676845Ensembl. | 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_047671 | 720 – 1362 | EMAPK…EENLF → AFCTSGDFVSPGPSPYHSHV QCGRFREMLRWFLVDVEQTA AGQPHRQSAAGPAITWAPAI AYPSPECARCCVGCS in isoform B. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 643 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_010902 | 720 – 722 | EMA → GPA in isoform C. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 3 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_010903 | 723 – 1362 | Missing in isoform C. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 640 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AF386649 mRNA Translation: AAL26987.1 Y12059 mRNA Translation: CAA72780.1 AC004798 Genomic DNA Translation: AAC27978.1 Different initiation. AC003111 Genomic DNA No translation available. AC005776 Genomic DNA No translation available. CH471106 Genomic DNA Translation: EAW84470.1 BC035266 mRNA Translation: AAH35266.1 AY166680 mRNA Translation: AAO22237.1 Different termination. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS12328.1 [O60885-1] CCDS46004.1 [O60885-2] CCDS82307.1 [O60885-3] |
NCBI Reference Sequences More...RefSeqi | NP_001317313.1, NM_001330384.1 [O60885-3] NP_055114.1, NM_014299.2 [O60885-2] NP_490597.1, NM_058243.2 [O60885-1] XP_011526156.1, XM_011527854.1 [O60885-1] XP_011526158.1, XM_011527856.2 [O60885-2] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.187763 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000263377; ENSP00000263377; ENSG00000141867 [O60885-1] ENST00000360016; ENSP00000353112; ENSG00000141867 [O60885-3] ENST00000371835; ENSP00000360901; ENSG00000141867 [O60885-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 23476 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:23476 |
UCSC genome browser More...UCSCi | uc002nar.4 human [O60885-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing, Chromosomal rearrangement, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| O60885 | BRD4 isoform 7 | 1362 | |||
| Bromodomain-containing protein 4 (Fragment) | 572 | ||||
| BRD4 isoform 5 (Fragment) | 572 | ||||
| O60885-2 | BRD4 isoform 6 | 722 | |||
| BRD4 isoform 4 | 720 |
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| O60885 | BRD4 isoform 7 | 1362 | |||
| Bromodomain-containing protein 4 (Fragment) | 572 | ||||
| Bromodomain containing 4 | 1420 | ||||
| Bromodomain-containing protein 4 (Fragment) | 255 | ||||
| UPI000BB80163 | 1412 | ||||
| +65 | |||||
| O60885-2 | BRD4 isoform 6 | 722 | |||
| UPI00045E1577 | 825 | ||||
| Bromodomain containing 4, isoform CRA_b | 794 | ||||
| BRD4 isoform 1 | 794 | ||||
| Bromodomain containing 4 | 792 | ||||
| +94 | |||||
| O60885-3 | BRD4 isoform 6 | 722 | |||
| UPI00045E1577 | 825 | ||||
| Bromodomain containing 4, isoform CRA_b | 794 | ||||
| BRD4 isoform 1 | 794 | ||||
| Bromodomain containing 4 | 792 | ||||
| +94 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| O60885 | BRD4 isoform 7 | 1362 | |||
| Bromodomain-containing protein 4 (Fragment) | 572 | ||||
| Bromodomain containing 4 | 1420 | ||||
| Bromodomain-containing protein 4 (Fragment) | 255 | ||||
| UPI000BB80163 | 1412 | ||||
| +141 | |||||
| O60885-2 | BRD4 isoform 6 | 722 | |||
| UPI00045E1577 | 825 | ||||
| BRD4 isoform 1 | 794 | ||||
| Bromodomain containing 4, isoform CRA_b | 794 | ||||
| Bromodomain containing 4 | 792 | ||||
| +117 | |||||
| O60885-3 | BRD4 isoform 6 | 722 | |||
| UPI00045E1577 | 825 | ||||
| BRD4 isoform 1 | 794 | ||||
| Bromodomain containing 4, isoform CRA_b | 794 | ||||
| Bromodomain containing 4 | 792 | ||||
| +117 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| Atlas of Genetics and Cytogenetics in Oncology and Haematology |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AF386649 mRNA Translation: AAL26987.1 Y12059 mRNA Translation: CAA72780.1 AC004798 Genomic DNA Translation: AAC27978.1 Different initiation. AC003111 Genomic DNA No translation available. AC005776 Genomic DNA No translation available. CH471106 Genomic DNA Translation: EAW84470.1 BC035266 mRNA Translation: AAH35266.1 AY166680 mRNA Translation: AAO22237.1 Different termination. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS12328.1 [O60885-1] CCDS46004.1 [O60885-2] CCDS82307.1 [O60885-3] |
NCBI Reference Sequences More...RefSeqi | NP_001317313.1, NM_001330384.1 [O60885-3] NP_055114.1, NM_014299.2 [O60885-2] NP_490597.1, NM_058243.2 [O60885-1] XP_011526156.1, XM_011527854.1 [O60885-1] XP_011526158.1, XM_011527856.2 [O60885-2] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.187763 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2I8N | NMR | - | A | 352-457 | [»] | |
| 2LSP | NMR | - | B | 333-460 | [»] | |
| 2MJV | NMR | - | B | 333-460 | [»] | |
| 2N3K | NMR | - | A | 600-678 | [»] | |
| 2NCZ | NMR | - | A | 601-683 | [»] | |
| 2ND0 | NMR | - | A | 601-683 | [»] | |
| 2ND1 | NMR | - | A | 601-683 | [»] | |
| 2NNU | X-ray | 1.59 | B | 1343-1362 | [»] | |
| 2OSS | X-ray | 1.35 | A | 44-168 | [»] | |
| 2OUO | X-ray | 1.89 | A | 333-460 | [»] | |
| 2YEL | X-ray | 1.65 | A | 44-168 | [»] | |
| 2YEM | X-ray | 2.30 | A/B | 333-460 | [»] | |
| 3MXF | X-ray | 1.60 | A | 42-168 | [»] | |
| 3P5O | X-ray | 1.60 | A | 44-168 | [»] | |
| 3SVF | X-ray | 1.98 | A | 44-168 | [»] | |
| 3SVG | X-ray | 1.68 | A | 44-168 | [»] | |
| 3U5J | X-ray | 1.60 | A | 44-168 | [»] | |
| 3U5K | X-ray | 1.80 | A/B/C/D | 44-168 | [»] | |
| 3U5L | X-ray | 1.39 | A | 44-168 | [»] | |
| 3UVW | X-ray | 1.37 | A | 44-168 | [»] | |
| 3UVX | X-ray | 1.91 | A | 44-168 | [»] | |
| 3UVY | X-ray | 2.02 | A | 44-168 | [»] | |
| 3UW9 | X-ray | 2.30 | A/B/C/D | 44-168 | [»] | |
| 3ZYU | X-ray | 1.50 | A/B | 44-168 | [»] | |
| 4A9L | X-ray | 1.60 | A | 44-168 | [»] | |
| 4BJX | X-ray | 1.59 | A | 44-168 | [»] | |
| 4BW1 | X-ray | 1.40 | A | 44-168 | [»] | |
| 4BW2 | X-ray | 1.92 | A | 44-168 | [»] | |
| 4BW3 | X-ray | 1.50 | A | 44-168 | [»] | |
| 4BW4 | X-ray | 1.67 | A | 44-168 | [»] | |
| 4C66 | X-ray | 1.87 | A | 44-167 | [»] | |
| 4C67 | X-ray | 1.55 | A | 44-168 | [»] | |
| 4CFK | X-ray | 1.55 | A | 44-168 | [»] | |
| 4CFL | X-ray | 1.32 | A | 44-168 | [»] | |
| 4CL9 | X-ray | 1.40 | A | 44-168 | [»] | |
| 4CLB | X-ray | 1.60 | A | 44-168 | [»] | |
| 4DON | X-ray | 1.52 | A | 44-166 | [»] | |
| 4E96 | X-ray | 1.92 | A | 44-168 | [»] | |
| 4F3I | X-ray | 1.40 | A | 44-168 | [»] | |
| 4GPJ | X-ray | 1.60 | A | 44-168 | [»] | |
| 4HBV | X-ray | 1.63 | A | 42-168 | [»] | |
| 4HBW | X-ray | 1.69 | A | 42-168 | [»] | |
| 4HBX | X-ray | 1.62 | A | 42-168 | [»] | |
| 4HBY | X-ray | 1.59 | A | 44-168 | [»] | |
| 4HXK | X-ray | 1.61 | A | 44-167 | [»] | |
| 4HXL | X-ray | 1.52 | A | 44-167 | [»] | |
| 4HXM | X-ray | 1.50 | A | 44-166 | [»] | |
| 4HXN | X-ray | 1.49 | A | 44-167 | [»] | |
| 4HXO | X-ray | 1.76 | A | 44-167 | [»] | |
| 4HXP | X-ray | 1.73 | A | 44-166 | [»] | |
| 4HXR | X-ray | 1.53 | A | 44-167 | [»] | |
| 4HXS | X-ray | 1.43 | A | 44-166 | [»] | |
| 4IOO | X-ray | 1.25 | A | 44-168 | [»] | |
| 4IOQ | X-ray | 1.50 | A | 44-168 | [»] | |
| 4IOR | X-ray | 1.40 | A | 44-168 | [»] | |
| 4J0R | X-ray | 1.72 | A | 44-168 | [»] | |
| 4J0S | X-ray | 1.84 | A | 44-168 | [»] | |
| 4J3I | X-ray | 1.24 | A | 44-168 | [»] | |
| 4KV1 | X-ray | 1.50 | A/B | 41-168 | [»] | |
| 4KV4 | X-ray | 2.00 | A | 351-459 | [»] | |
| 4LR6 | X-ray | 1.29 | A | 42-168 | [»] | |
| 4LRG | X-ray | 2.21 | A | 42-168 | [»] | |
| 4LYI | X-ray | 1.30 | A | 44-168 | [»] | |
| 4LYS | X-ray | 1.83 | A | 44-168 | [»] | |
| 4LYW | X-ray | 1.95 | A | 44-168 | [»] | |
| 4LZR | X-ray | 1.85 | A | 44-168 | [»] | |
| 4LZS | X-ray | 2.20 | A | 44-168 | [»] | |
| 4MEN | X-ray | 1.81 | A | 44-168 | [»] | |
| 4MEO | X-ray | 1.72 | A | 44-168 | [»] | |
| 4MEP | X-ray | 1.85 | A | 44-168 | [»] | |
| 4MEQ | X-ray | 1.77 | A | 44-168 | [»] | |
| 4MR3 | X-ray | 1.68 | A | 44-168 | [»] | |
| 4MR4 | X-ray | 1.66 | A | 44-168 | [»] | |
| 4NQM | X-ray | 1.58 | A | 44-168 | [»] | |
| 4NR8 | X-ray | 1.64 | A | 44-168 | [»] | |
| 4NUC | X-ray | 1.40 | A | 44-168 | [»] | |
| 4NUD | X-ray | 1.20 | A | 44-168 | [»] | |
| 4NUE | X-ray | 1.30 | A | 44-168 | [»] | |
| 4O70 | X-ray | 1.55 | A/B | 44-168 | [»] | |
| 4O71 | X-ray | 1.36 | A/B | 44-168 | [»] | |
| 4O72 | X-ray | 1.40 | A | 44-168 | [»] | |
| 4O74 | X-ray | 1.45 | A/B | 44-168 | [»] | |
| 4O75 | X-ray | 1.55 | A | 44-168 | [»] | |
| 4O76 | X-ray | 1.70 | A/B/C/D | 44-168 | [»] | |
| 4O77 | X-ray | 2.00 | A/B | 44-168 | [»] | |
| 4O78 | X-ray | 1.34 | A | 44-168 | [»] | |
| 4O7A | X-ray | 1.34 | A | 44-168 | [»] | |
| 4O7B | X-ray | 1.50 | A | 44-168 | [»] | |
| 4O7C | X-ray | 1.55 | A | 44-168 | [»] | |
| 4O7E | X-ray | 1.85 | A/B | 44-168 | [»] | |
| 4O7F | X-ray | 1.80 | A/B | 44-168 | [»] | |
| 4OGI | X-ray | 1.73 | A/B | 44-168 | [»] | |
| 4OGJ | X-ray | 1.65 | A/B | 44-168 | [»] | |
| 4PCE | X-ray | 1.29 | A | 44-168 | [»] | |
| 4PCI | X-ray | 1.25 | A | 44-168 | [»] | |
| 4PS5 | X-ray | 1.40 | A/B | 44-168 | [»] | |
| 4QB3 | X-ray | 0.94 | A | 44-168 | [»] | |
| 4QR3 | X-ray | 1.37 | A | 44-166 | [»] | |
| 4QR4 | X-ray | 1.28 | A | 44-166 | [»] | |
| 4QR5 | X-ray | 1.41 | A | 44-166 | [»] | |
| 4QZS | X-ray | 1.45 | A | 44-168 | [»] | |
| 4UIX | X-ray | 1.58 | A/B/C | 44-168 | [»] | |
| 4UIY | X-ray | 1.30 | A | 44-168 | [»] | |
| 4UIZ | X-ray | 1.19 | A | 44-168 | [»] | |
| 4UYD | X-ray | 1.37 | A | 44-183 | [»] | |
| 4WHW | X-ray | 1.34 | A | 44-168 | [»] | |
| 4WIV | X-ray | 1.56 | A | 44-168 | [»] | |
| 4X2I | X-ray | 1.20 | A | 42-166 | [»] | |
| 4XY9 | X-ray | 1.83 | A | 42-168 | [»] | |
| 4XYA | X-ray | 2.05 | A | 42-168 | [»] | |
| 4YH3 | X-ray | 1.60 | A | 44-170 | [»] | |
| 4YH4 | X-ray | 1.33 | A | 44-170 | [»] | |
| 4Z1Q | X-ray | 1.40 | A/B | 42-167 | [»] | |
| 4Z1S | X-ray | 1.06 | A/B | 42-166 | [»] | |
| 4Z93 | X-ray | 1.27 | A | 349-460 | [»] | |
| 4ZC9 | X-ray | 0.99 | A | 44-168 | [»] | |
| 4ZW1 | X-ray | 1.75 | A | 44-168 | [»] | |
| 5A5S | X-ray | 1.36 | A | 44-168 | [»] | |
| 5A85 | X-ray | 1.72 | A | 44-168 | [»] | |
| 5ACY | X-ray | 2.01 | A/B | 44-168 | [»] | |
| 5AD2 | X-ray | 2.01 | A/B | 44-168 | [»] | |
| 5AD3 | X-ray | 1.49 | A/B | 44-168 | [»] | |
| 5BT4 | X-ray | 1.50 | A/B/C | 44-168 | [»] | |
| 5CFW | X-ray | 1.15 | A | 44-168 | [»] | |
| 5COI | X-ray | 1.62 | A | 44-168 | [»] | |
| 5CP5 | X-ray | 1.79 | A | 44-168 | [»] | |
| 5CPE | X-ray | 1.62 | A | 44-168 | [»] | |
| 5CQT | X-ray | 1.60 | A | 44-168 | [»] | |
| 5CRM | X-ray | 1.99 | A | 44-168 | [»] | |
| 5CRZ | X-ray | 2.12 | A | 44-168 | [»] | |
| 5CS8 | X-ray | 1.62 | A | 44-168 | [»] | |
| 5CTL | X-ray | 2.51 | A | 44-168 | [»] | |
| 5CY9 | X-ray | 1.55 | A | 44-168 | [»] | |
| 5D0C | X-ray | 1.49 | A | 44-168 | [»] | |
| 5D24 | X-ray | 1.65 | A | 43-168 | [»] | |
| 5D25 | X-ray | 1.70 | A | 43-168 | [»] | |
| 5D26 | X-ray | 1.82 | A | 42-168 | [»] | |
| 5D3H | X-ray | 1.70 | A | 44-168 | [»] | |
| 5D3J | X-ray | 1.70 | A | 43-168 | [»] | |
| 5D3L | X-ray | 1.50 | A | 42-168 | [»] | |
| 5D3N | X-ray | 2.15 | A | 43-168 | [»] | |
| 5D3P | X-ray | 1.95 | A | 42-168 | [»] | |
| 5D3R | X-ray | 2.20 | A | 42-168 | [»] | |
| 5D3S | X-ray | 1.75 | A | 44-168 | [»] | |
| 5D3T | X-ray | 1.93 | A | 42-168 | [»] | |
| 5DLX | X-ray | 1.90 | A | 44-168 | [»] | |
| 5DLZ | X-ray | 1.70 | A | 44-168 | [»] | |
| 5DW2 | X-ray | 1.12 | A | 44-170 | [»] | |
| 5DX4 | X-ray | 2.30 | A | 44-168 | [»] | |
| 5E0R | X-ray | 1.35 | A | 44-168 | [»] | |
| 5EGU | X-ray | 2.21 | A/B/C/D | 44-168 | [»] | |
| 5EI4 | X-ray | 1.05 | A | 44-168 | [»] | |
| 5EIS | X-ray | 1.60 | A | 44-168 | [»] | |
| 5F5Z | X-ray | 1.76 | A | 44-168 | [»] | |
| 5F60 | X-ray | 1.35 | A | 44-168 | [»] | |
| 5F61 | X-ray | 1.45 | A/B | 44-168 | [»] | |
| 5F62 | X-ray | 1.35 | A | 44-168 | [»] | |
| 5F63 | X-ray | 1.45 | A | 44-168 | [»] | |
| 5FBX | X-ray | 1.85 | A | 44-168 | [»] | |
| 5H21 | X-ray | 1.59 | A | 44-167 | [»] | |
| 5HCL | X-ray | 1.50 | A | 44-168 | [»] | |
| 5HLS | X-ray | 2.18 | A | 42-168 | [»] | |
| 5HM0 | X-ray | 1.40 | A | 42-168 | [»] | |
| 5HQ5 | X-ray | 1.60 | A | 44-168 | [»] | |
| 5HQ6 | X-ray | 1.95 | A | 44-166 | [»] | |
| 5HQ7 | X-ray | 1.90 | A | 44-167 | [»] | |
| 5I80 | X-ray | 1.45 | A | 42-167 | [»] | |
| 5I88 | X-ray | 1.40 | A | 42-167 | [»] | |
| 5IGK | X-ray | 1.70 | A | 44-168 | [»] | |
| 5JWM | X-ray | 1.71 | A/B | 333-460 | [»] | |
| 5KDH | X-ray | 1.50 | A | 44-168 | [»] | |
| 5KHM | X-ray | 1.48 | A/B | 44-168 | [»] | |
| 5KJ0 | X-ray | 1.51 | A | 44-168 | [»] | |
| 5KU3 | X-ray | 1.14 | A | 42-167 | [»] | |
| 5LJ1 | X-ray | 1.90 | A | 42-168 | [»] | |
| 5LJ2 | X-ray | 1.19 | A | 42-168 | [»] | |
| 5LRQ | X-ray | 1.70 | A | 42-163 | [»] | |
| 5LUU | X-ray | 1.61 | A | 44-168 | [»] | |
| 5M39 | X-ray | 1.38 | A/B | 42-168 | [»] | |
| 5M3A | X-ray | 1.65 | A | 44-168 | [»] | |
| 5MKZ | X-ray | 1.62 | A | 44-168 | [»] | |
| 5MLI | X-ray | 1.63 | A | 42-168 | [»] | |
| 5N2M | X-ray | 1.54 | A | 44-168 | [»] | |
| 5NNC | X-ray | 2.22 | A/B | 44-168 | [»] | |
| 5NND | X-ray | 1.82 | A/B | 44-168 | [»] | |
| 5NNE | X-ray | 1.15 | A | 44-168 | [»] | |
| 5NNF | X-ray | 1.15 | A | 44-168 | [»] | |
| 5NNG | X-ray | 1.20 | A | 44-168 | [»] | |
| 5T35 | X-ray | 2.70 | A/E | 333-460 | [»] | |
| 5TI2 | X-ray | 1.65 | A | 44-168 | [»] | |
| 5TI3 | X-ray | 1.70 | A | 44-168 | [»] | |
| 5TI4 | X-ray | 1.62 | A | 44-168 | [»] | |
| 5TI5 | X-ray | 1.83 | A | 44-168 | [»] | |
| 5TI6 | X-ray | 1.70 | A | 44-168 | [»] | |
| 5TI7 | X-ray | 1.65 | A | 44-168 | [»] | |
| 5U28 | X-ray | 1.80 | A | 44-180 | [»] | |
| 5U2C | X-ray | 3.30 | A/B | 342-460 | [»] | |
| 5U2E | X-ray | 1.99 | A/B | 42-180 | [»] | |
| 5U2F | X-ray | 2.52 | A/B | 42-180 | [»] | |
| 5UEO | X-ray | 1.85 | A/B | 352-457 | [»] | |
| 5UEP | X-ray | 1.77 | A | 352-457 | [»] | |
| 5UEQ | X-ray | 1.70 | A | 352-457 | [»] | |
| 5UER | X-ray | 1.87 | A | 352-457 | [»] | |
| 5UES | X-ray | 1.62 | A | 352-457 | [»] | |
| 5UET | X-ray | 2.29 | A | 352-457 | [»] | |
| 5UEU | X-ray | 2.26 | A/B | 352-457 | [»] | |
| 5UEV | X-ray | 1.94 | A | 352-457 | [»] | |
| 5UEX | X-ray | 2.29 | A | 352-457 | [»] | |
| 5UEY | X-ray | 2.41 | A | 352-457 | [»] | |
| 5UEZ | X-ray | 1.51 | A | 352-457 | [»] | |
| 5UF0 | X-ray | 1.35 | A | 352-457 | [»] | |
| 5ULA | X-ray | 1.50 | A/B | 44-168 | [»] | |
| 5UOO | X-ray | 1.69 | A | 333-460 | [»] | |
| 5UVS | X-ray | 2.15 | A | 352-457 | [»] | |
| 5UVT | X-ray | 1.67 | A | 352-457 | [»] | |
| 5UVU | X-ray | 1.66 | A | 352-457 | [»] | |
| 5UVV | X-ray | 1.99 | A/B | 352-457 | [»] | |
| 5UVW | X-ray | 2.14 | A/B/C | 57-165 | [»] | |
| 5UVX | X-ray | 1.53 | A/B | 352-457 | [»] | |
| 5UVY | X-ray | 2.25 | A | 352-457 | [»] | |
| 5UVZ | X-ray | 1.63 | A | 352-457 | [»] | |
| 5V67 | X-ray | 1.78 | A | 44-168 | [»] | |
| 5VBO | X-ray | 1.30 | A | 44-168 | [»] | |
| 5VBP | X-ray | 1.83 | A/B | 44-168 | [»] | |
| 5VOM | X-ray | 1.67 | A/B | 44-168 | [»] | |
| 5VZS | X-ray | 1.71 | A/B | 42-168 | [»] | |
| 5WUU | X-ray | 1.72 | A | 44-167 | [»] | |
| 5XHY | X-ray | 1.98 | A | 44-166 | [»] | |
| 5XI2 | X-ray | 1.91 | A | 44-166 | [»] | |
| 5XI3 | X-ray | 1.67 | A | 44-166 | [»] | |
| 5XI4 | X-ray | 1.49 | A | 44-166 | [»] | |
| 5Y1Y | X-ray | 1.91 | A | 44-167 | [»] | |
| 5Z9C | NMR | - | A | 53-168 | [»] | |
| 6BN7 | X-ray | 3.50 | C | 42-168 | [»] | |
| 6BN8 | X-ray | 3.99 | C | 42-168 | [»] | |
| 6BN9 | X-ray | 4.38 | C | 42-168 | [»] | |
| 6BNB | X-ray | 6.34 | C | 42-168 | [»] | |
| 6BNH | NMR | - | A | 601-683 | [»] | |
| 6BOY | X-ray | 3.33 | C | 42-168 | [»] | |
| 6CKR | X-ray | 1.62 | A/B | 44-168 | [»] | |
| 6CKS | X-ray | 1.72 | A | 44-168 | [»] | |
| 6FSY | X-ray | 1.34 | A | 42-168 | [»] | |
| 6FT3 | X-ray | 1.28 | A | 42-168 | [»] | |
| 6FT4 | X-ray | 1.34 | A | 42-168 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | O60885 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | O60885 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 117036, 98 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | O60885 |
Database of interacting proteins More...DIPi | DIP-39776N |
Protein interaction database and analysis system More...IntActi | O60885, 45 interactors |
Molecular INTeraction database More...MINTi | O60885 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000263377 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | O60885 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL1163125 |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 1945 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | O60885 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | O60885 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | BRD4 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | O60885 |
MaxQB - The MaxQuant DataBase More...MaxQBi | O60885 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | O60885 |
PeptideAtlas More...PeptideAtlasi | O60885 |
PRoteomics IDEntifications database More...PRIDEi | O60885 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 49651 49652 [O60885-2] |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000263377; ENSP00000263377; ENSG00000141867 [O60885-1] ENST00000360016; ENSP00000353112; ENSG00000141867 [O60885-3] ENST00000371835; ENSP00000360901; ENSG00000141867 [O60885-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 23476 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:23476 |
UCSC genome browser More...UCSCi | uc002nar.4 human [O60885-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 23476 |
DisGeNET More...DisGeNETi | 23476 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000141867.17 |
GeneCards: human genes, protein and diseases More...GeneCardsi | BRD4 |
Human Gene Nomenclature Database More...HGNCi | HGNC:13575 BRD4 |
Human Protein Atlas More...HPAi | CAB068177 CAB068178 HPA015055 HPA061646 |
MalaCards human disease database More...MalaCardsi | BRD4 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 608749 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_O60885 |
Open Targets More...OpenTargetsi | ENSG00000141867 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA25416 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1474 Eukaryota COG5076 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00920000148952 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000231200 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG004896 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | O60885 |
KEGG Orthology (KO) More...KOi | K11722 |
Identification of Orthologs from Complete Genome Data More...OMAi | RPPEQNA |
Database of Orthologous Groups More...OrthoDBi | EOG091G01QC |
Database for complete collections of gene phylogenies More...PhylomeDBi | O60885 |
TreeFam database of animal gene trees More...TreeFami | TF317345 |
Enzyme and pathway databases
SIGNOR Signaling Network Open Resource More...SIGNORi | O60885 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | BRD4 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | O60885 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | BRD4 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 23476 |
CutDB - Proteolytic event database More...PMAP-CutDBi | O60885 |
Protein Ontology More...PROi | PR:O60885 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000141867 |
CleanEx database of gene expression profiles More...CleanExi | HS_BRD4 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | O60885 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | O60885 HS |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.20.1270.220, 1 hit 1.20.920.10, 2 hits |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR031354 BRD4_CDT IPR001487 Bromodomain IPR036427 Bromodomain-like_sf IPR018359 Bromodomain_CS IPR027353 NET_dom IPR038336 NET_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF17035 BET, 1 hit PF17105 BRD4_CDT, 1 hit PF00439 Bromodomain, 2 hits |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00503 BROMODOMAIN |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00297 BROMO, 2 hits |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF47370 SSF47370, 2 hits |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00633 BROMODOMAIN_1, 1 hit PS50014 BROMODOMAIN_2, 2 hits PS51525 NET, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | BRD4_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | O60885Primary (citable) accession number: O60885 Secondary accession number(s): O60433 , Q4G0X8, Q86YS8, Q96PD3 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 11, 2001 |
| Last sequence update: | January 31, 2002 | |
| Last modified: | July 18, 2018 | |
| This is version 175 of the entry and version 2 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 19
Human chromosome 19: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references
