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O60885 (BRD4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bromodomain-containing protein 4
Alternative name(s):
Protein HUNK1
Gene names
Name:BRD4
Synonyms:HUNK1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1362 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation. Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure. During interphase, plays a key role in regulating the transcription of signal-inducible genes by associating with the P-TEFb complex and recruiting it to promoters: BRD4 is required to form the transcriptionally active P-TEFb complex by displacing negative regulators such as HEXIM1 and 7SKsnRNA complex from P-TEFb, thereby transforming it into an active form that can then phosphorylate the C-terminal domain (CTD) of RNA polymerase II. Promotes phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II. According to a report, directly acts as an atypical protein kinase and mediates phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II; these data however need additional evidences in vivo (Ref.25). In addition to acetylated histones, also recognizes and binds acetylated RELA, leading to further recruitment of the P-TEFb complex and subsequent activation of NF-kappa-B. Also acts as a regulator of p53/TP53-mediated transcription: following phosphorylation by CK2, recruited to p53/TP53 specific target promoters. Ref.7 Ref.8 Ref.15 Ref.16 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28

Isoform B:Acts as a chromatin insulator in the DNA damage response pathway. Inhibits DNA damage response signaling by recruiting the condensin-2 complex to acetylated histones, leading to chromatin structure remodeling, insulating the region from DNA damage response by limiting spreading of histone H2AFX/H2A.x phosphorylation. Ref.7 Ref.8 Ref.15 Ref.16 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28

Subunit structure

Interacts with p53/TP53; the interaction is direct. Interacts (via CTD region) with CDK9 and CCNT1, acting as an associated component of P-TEFb complex. Interacts with RELA (when acetylated at 'Lys-310'). Interacts (via NET domain) with WHSC1L1, JMJD6, CHD4, GLTSCR1 and ATAD5. Isoform B:interacts with NCAPD3 and SMC2. Interacts with bovine papillomavirus type 1 regulatory protein E2 and human herpes virus-8 (HHV-8) protein LANA. These interactions may serve for the tethering of viral genomes to host mitotic chromosomes allowing successful partitioning of the viral genome during cell division. Interacts with Epstein-Barr virus (EBV) protein EBNA1; this interaction facilitates transcriptional activation by EBNA1. Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.16 Ref.20 Ref.26 Ref.28

Subcellular location

Nucleus. Chromosome. 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. Ref.7 Ref.21 Ref.28 Ref.31

Tissue specificity

Ubiquitously expressed. Ref.6

Domain

The NET domain mediates interaction with a number of chromatin proteins involved in transcription regulation (WHSC1L1, JMJD6, CHD4, GLTSCR1 and ATAD5) (Ref.20).

The C-terminal (CTD) region mediates interaction and recruitment of CDK9 and CCNT1 subunits of the P-TEFb complex (Ref.7, Ref.8). It is also required for maintenance of higher-order chromatin structure (Ref.23).

The 2 bromo domains mediate specific binding to acetylated histones via Asn-140 and Asn-433, respectively (Ref.31). The exact combination of modified histone tails required to recruit BRD4 to target genes is still unclear. The first bromo domain has high affinity for acetylated histone H4 tail, whereas the second bromo domain recognizes multiply acetylated marks in histone H3 (Ref.39). A number of specific inhibitors bind competitively to acetyl-lysine-binding residues Asn-140 and Asn-433, promoting removal from acetylated histones. Many of these inhibitors are benzodiazepine derivatives (Ref.35, Ref.37, Ref.40, Ref.41).

Post-translational modification

Phosphorylation by CK2 disrupt the intramolecular binding between the bromo domain 2 and the NPS region and promotes binding between the NPS and the BID regions, leading to activate the protein and promote binding to acetylated histones. In absence of phosphorylation, BRD4 does not localize to p53/TP53 target gene promoters, phosphorylation promoting recruitment to p53/TP53 target promoters.

Involvement in disease

A chromosomal aberration involving BRD4 is found in a rare, aggressive, and lethal carcinoma arising in midline organs of young people. Translocation t(15;19)(q14;p13) with NUT which produces a BRD4-NUT fusion protein. Ref.1 Ref.6

Miscellaneous

Some specific inhibitors of BRD4 that prevent binding to acetylated histones by binding Asn-140 and Asn-433 are promising therapeutic molecules for the treatment of leukemias. JQ1, a thieno-triazolo-1,4-diazepine derivative, and I-BET, a benzodiazepine derivative, have been tested on tumors with success (Ref.31, Ref.32, Ref.34). Treatment with GSK1210151A (I-BET151, a I-BET derivative) has strong effets on mixed lineage leukemia and promotes myeloid differentiation and leukemia stem-cell depletion (Ref.34).

Sequence similarities

Contains 2 bromo domains.

Contains 1 NET domain.

Sequence caution

The sequence AAC27978.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processDNA damage
Host-virus interaction
Transcription
Transcription regulation
   Cellular componentChromosome
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DomainBromodomain
Repeat
   Molecular functionChromatin regulator
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to DNA damage stimulus

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin remodeling

Inferred from direct assay Ref.28. Source: UniProtKB

chromosome segregation

Inferred from electronic annotation. Source: Ensembl

histone H3-K14 acetylation

Inferred from electronic annotation. Source: Ensembl

histone H4-K12 acetylation

Inferred from electronic annotation. Source: Ensembl

inner cell mass cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of DNA damage checkpoint

Inferred from mutant phenotype Ref.28. Source: UniProtKB

positive regulation of DNA binding

Inferred from electronic annotation. Source: Ensembl

positive regulation of G2/M transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 10938129. Source: MGI

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from direct assay Ref.16. Source: UniProtKB

positive regulation of transcription elongation from RNA polymerase II promoter

Inferred from direct assay Ref.16Ref.24. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.24Ref.26. Source: UniProtKB

protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of inflammatory response

Inferred from direct assay Ref.16. Source: UniProtKB

regulation of phosphorylation of RNA polymerase II C-terminal domain

Inferred from direct assay Ref.24. Source: UniProtKB

regulation of transcription involved in G1/S transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 18039861. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromosome

Inferred from direct assay Ref.28. Source: UniProtKB

condensed nuclear chromosome

Inferred from direct assay PubMed 10938129. Source: MGI

cytoplasm

Inferred from direct assay. Source: HPA

nuclear chromatin

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay Ref.31. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: Ensembl

chromatin binding

Inferred from direct assay Ref.31Ref.24Ref.26Ref.28. Source: UniProtKB

histone acetyl-lysine binding

Inferred from direct assay Ref.31Ref.24Ref.26Ref.28. Source: UniProtKB

p53 binding

Inferred from direct assay Ref.26. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

E2P031203EBI-723869,EBI-1779322From a different organism.
E2P040152EBI-723869,EBI-7010556From a different organism.
E2P173832EBI-723869,EBI-7010529From a different organism.
GRB2P629932EBI-723869,EBI-401755
JMJD6Q6NYC110EBI-723869,EBI-8464037
NCK1P163332EBI-723869,EBI-389883

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: O60885-1)

Also known as: Brd4L; Long;

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.
Isoform C (identifier: O60885-2)

Also known as: Brd4S; Short;

The sequence of this isoform differs from the canonical sequence as follows:
     720-722: EMA → GPA
     723-1362: Missing.
Isoform B (identifier: O60885-3)

The sequence of this isoform differs from the canonical sequence as follows:
     720-1362: EMAPKSKKKG...LLSIFEENLF → AFCTSGDFVS...ECARCCVGCS
Note: Does not contain the C-terminal (CTD) region required to recruit the P-TEFb complex.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13621362Bromodomain-containing protein 4
PRO_0000211183

Regions

Domain75 – 14773Bromo 1
Domain368 – 44073Bromo 2
Domain600 – 68283NET
Region484 – 50320NPS region
Region524 – 57956BID region
Region1047 – 1362316C-terminal (CTD) region
Compositional bias535 – 59460Lys-rich
Compositional bias692 – 71726Ser-rich
Compositional bias703 – 71412Poly-Ser
Compositional bias738 – 7436Poly-His
Compositional bias757 – 7615Poly-Pro
Compositional bias764 – 7707Poly-Pro
Compositional bias771 – 7755Poly-Gln
Compositional bias776 – 7838Poly-Pro
Compositional bias954 – 96411Poly-Pro
Compositional bias974 – 98613Poly-Pro
Compositional bias1011 – 10144Poly-Pro
Compositional bias1028 – 10336Poly-Pro
Compositional bias1283 – 130018Poly-Gln
Compositional bias1301 – 13088Poly-Ala
Compositional bias1335 – 13384Poly-Arg

Sites

Binding site1401Acetylated histones
Binding site1401Inhibitor
Binding site4331Acetylated histones
Binding site4331Inhibitor
Site719 – 7202Breakpoint for translocation to form BDR4-NUT fusion protein

Amino acid modifications

Modified residue4701Phosphoserine Ref.13
Modified residue4841Phosphoserine; by CK2 Ref.26
Modified residue4881Phosphoserine; by CK2 Ref.26
Modified residue4921Phosphoserine; by CK2 Ref.26
Modified residue4941Phosphoserine; by CK2 Ref.26
Modified residue4981Phosphoserine; by CK2 Ref.26
Modified residue4991Phosphoserine; by CK2 Ref.26
Modified residue5031Phosphoserine; by CK2 Ref.26
Modified residue6011Phosphoserine Ref.18 Ref.22
Modified residue11111N6-acetyllysine Ref.17
Modified residue11171Phosphoserine Ref.9 Ref.18 Ref.22

Natural variations

Alternative sequence720 – 1362643EMAPK…EENLF → AFCTSGDFVSPGPSPYHSHV QCGRFREMLRWFLVDVEQTA AGQPHRQSAAGPAITWAPAI AYPSPECARCCVGCS in isoform B.
VSP_047671
Alternative sequence720 – 7223EMA → GPA in isoform C.
VSP_010902
Alternative sequence723 – 1362640Missing in isoform C.
VSP_010903
Natural variant371P → S. Ref.29
Corresponds to variant rs35177876 [ dbSNP | Ensembl ].
VAR_041919
Natural variant3711A → G. Ref.29
Corresponds to variant rs55805532 [ dbSNP | Ensembl ].
VAR_041920
Natural variant5631S → N. Ref.29
Corresponds to variant rs55970906 [ dbSNP | Ensembl ].
VAR_041921
Natural variant5981T → S. Ref.29
Corresponds to variant rs34362023 [ dbSNP | Ensembl ].
VAR_041922
Natural variant6691R → H. Ref.29
Corresponds to variant rs35824241 [ dbSNP | Ensembl ].
VAR_041923
Natural variant10971R → H.
Corresponds to variant rs35676845 [ dbSNP | Ensembl ].
VAR_048427

Experimental info

Mutagenesis1401N → A: Abolishes binding to acetylated histones. Ref.28 Ref.39
Mutagenesis4331N → A: Abolishes binding to acetylated histones. Ref.39
Mutagenesis492 – 4943SSS → ASA: Impaired phosphorylation by CK2 and binding to acetylated histones. Ref.26
Mutagenesis498 – 5003SST → AAA: Impaired phosphorylation by CK2 and binding to acetylated histones. Ref.26
Mutagenesis5031S → A: Impaired phosphorylation by CK2 and binding to acetylated histones. Ref.26

Secondary structure

...................................... 1362
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform A (Brd4L) (Long) [UniParc].

Last modified January 31, 2002. Version 2.
Checksum: D52EFE1CF9960907

FASTA1,362152,219
        10         20         30         40         50         60 
MSAESGPGTR LRNLPVMGDG LETSQMSTTQ AQAQPQPANA ASTNPPPPET SNPNKPKRQT 

        70         80         90        100        110        120 
NQLQYLLRVV LKTLWKHQFA WPFQQPVDAV KLNLPDYYKI IKTPMDMGTI KKRLENNYYW 

       130        140        150        160        170        180 
NAQECIQDFN TMFTNCYIYN KPGDDIVLMA EALEKLFLQK INELPTEETE IMIVQAKGRG 

       190        200        210        220        230        240 
RGRKETGTAK PGVSTVPNTT QASTPPQTQT PQPNPPPVQA TPHPFPAVTP DLIVQTPVMT 

       250        260        270        280        290        300 
VVPPQPLQTP PPVPPQPQPP PAPAPQPVQS HPPIIAATPQ PVKTKKGVKR KADTTTPTTI 

       310        320        330        340        350        360 
DPIHEPPSLP PEPKTTKLGQ RRESSRPVKP PKKDVPDSQQ HPAPEKSSKV SEQLKCCSGI 

       370        380        390        400        410        420 
LKEMFAKKHA AYAWPFYKPV DVEALGLHDY CDIIKHPMDM STIKSKLEAR EYRDAQEFGA 

       430        440        450        460        470        480 
DVRLMFSNCY KYNPPDHEVV AMARKLQDVF EMRFAKMPDE PEEPVVAVSS PAVPPPTKVV 

       490        500        510        520        530        540 
APPSSSDSSS DSSSDSDSST DDSEEERAQR LAELQEQLKA VHEQLAALSQ PQQNKPKKKE 

       550        560        570        580        590        600 
KDKKEKKKEK HKRKEEVEEN KKSKAKEPPP KKTKKNNSSN SNVSKKEPAP MKSKPPPTYE 

       610        620        630        640        650        660 
SEEEDKCKPM SYEEKRQLSL DINKLPGEKL GRVVHIIQSR EPSLKNSNPD EIEIDFETLK 

       670        680        690        700        710        720 
PSTLRELERY VTSCLRKKRK PQAEKVDVIA GSSKMKGFSS SESESSSESS SSDSEDSETE 

       730        740        750        760        770        780 
MAPKSKKKGH PGREQKKHHH HHHQQMQQAP APVPQQPPPP PQQPPPPPPP QQQQQPPPPP 

       790        800        810        820        830        840 
PPPSMPQQAA PAMKSSPPPF IATQVPVLEP QLPGSVFDPI GHFTQPILHL PQPELPPHLP 

       850        860        870        880        890        900 
QPPEHSTPPH LNQHAVVSPP ALHNALPQQP SRPSNRAAAL PPKPARPPAV SPALTQTPLL 

       910        920        930        940        950        960 
PQPPMAQPPQ VLLEDEEPPA PPLTSMQMQL YLQQLQKVQP PTPLLPSVKV QSQPPPPLPP 

       970        980        990       1000       1010       1020 
PPHPSVQQQL QQQPPPPPPP QPQPPPQQQH QPPPRPVHLQ PMQFSTHIQQ PPPPQGQQPP 

      1030       1040       1050       1060       1070       1080 
HPPPGQQPPP PQPAKPQQVI QHHHSPRHHK SDPYSTGHLR EAPSPLMIHS PQMSQFQSLT 

      1090       1100       1110       1120       1130       1140 
HQSPPQQNVQ PKKQELRAAS VVQPQPLVVV KEEKIHSPII RSEPFSPSLR PEPPKHPESI 

      1150       1160       1170       1180       1190       1200 
KAPVHLPQRP EMKPVDVGRP VIRPPEQNAP PPGAPDKDKQ KQEPKTPVAP KKDLKIKNMG 

      1210       1220       1230       1240       1250       1260 
SWASLVQKHP TTPSSTAKSS SDSFEQFRRA AREKEEREKA LKAQAEHAEK EKERLRQERM 

      1270       1280       1290       1300       1310       1320 
RSREDEDALE QARRAHEEAR RRQEQQQQQR QEQQQQQQQQ AAAVAAAATP QAQSSQPQSM 

      1330       1340       1350       1360 
LDQQRELARK REQERRRREA MAATIDMNFQ SDLLSIFEEN LF 

« Hide

Isoform C (Brd4S) (Short) [UniParc].

Checksum: FF040EE016B37F87
Show »

FASTA72280,463
Isoform B [UniParc].

Checksum: ACB01CC53AA4C431
Show »

FASTA79488,289

References

« Hide 'large scale' references
[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.
[2]Weber B.
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
Tissue: Placenta.
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
Tissue: Testis.
[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.
Tissue: Carcinoma.
[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.
[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.
[9]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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.
[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.
[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.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Control of inducible gene expression by signal-dependent transcriptional elongation."
Hargreaves D.C., Horng T., Medzhitov R.
Cell 138:129-145(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[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.
[17]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601 AND SER-1117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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.
[21]"Signal-induced Brd4 release from chromatin is essential for its role transition from chromatin targeting to transcriptional regulation."
Ai N., Hu X., Ding F., Yu B., Wang H., Lu X., Zhang K., Li Y., Han A., Lin W., Liu R., Chen R.
Nucleic Acids Res. 39:9592-9604(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[22]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601 AND SER-1117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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.
[24]"Bromodomain-containing protein 4 (BRD4) regulates RNA polymerase II serine 2 phosphorylation in human CD4+ T cells."
Zhang W., Prakash C., Sum C., Gong Y., Li Y., Kwok J.J., Thiessen N., Pettersson S., Jones S.J., Knapp S., Yang H., Chin K.C.
J. Biol. Chem. 287:43137-43155(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[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.
[26]"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.
[27]"BRD4 coordinates recruitment of pause release factor P-TEFb and the pausing complex NELF/DSIF to regulate transcription elongation of interferon-stimulated genes."
Patel M.C., Debrosse M., Smith M., Dey A., Huynh W., Sarai N., Heightman T.D., Tamura T., Ozato K.
Mol. Cell. Biol. 33:2497-2507(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[28]"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. expand/collapse author list , 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.
[29]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-37; GLY-371; ASN-563; SER-598 AND HIS-669.
[30]"Structural basis and binding properties of the second bromodomain of Brd4 with acetylated histone tails."
Liu Y., Wang X., Zhang J., Huang H., Ding B., Wu J., Shi Y.
Biochemistry 47:6403-6417(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 352-457.
[31]"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. expand/collapse author list , 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.
[32]"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.
[33]"Discovery and characterization of small molecule inhibitors of the BET family bromodomains."
Chung C.W., Coste H., White J.H., Mirguet O., Wilde J., Gosmini R.L., Delves C., Magny S.M., Woodward R., Hughes S.A., Boursier E.V., Flynn H., Bouillot A.M., Bamborough P., Brusq J.M., Gellibert F.J., Jones E.J., Riou A.M. expand/collapse author list , Homes P., Martin S.L., Uings I.J., Toum J., Clement C.A., Boullay A.B., Grimley R.L., Blandel F.M., Prinjha R.K., Lee K., Kirilovsky J., Nicodeme E.
J. Med. Chem. 54:3827-3838(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 44-168, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 333-460.
[34]"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. expand/collapse author list , 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.
[35]"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.
[36]"Down-regulation of NF-kappaB transcriptional activity in HIV-associated kidney disease by BRD4 inhibition."
Zhang G., Liu R., Zhong Y., Plotnikov A.N., Zhang W., Zeng L., Rusinova E., Gerona-Nevarro G., Moshkina N., Joshua J., Chuang P.Y., Ohlmeyer M., He J.C., Zhou M.M.
J. Biol. Chem. 287:28840-28851(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 44-168, STRUCTURE BY NMR OF 333-460.
[37]"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.
[38]"Identification of a chemical probe for bromo and extra C-terminal bromodomain inhibition through optimization of a fragment-derived hit."
Fish P.V., Filippakopoulos P., Bish G., Brennan P.E., Bunnage M.E., Cook A.S., Federov O., Gerstenberger B.S., Jones H., Knapp S., Marsden B., Nocka K., Owen D.R., Philpott M., Picaud S., Primiano M.J., Ralph M.J., Sciammetta N., Trzupek J.D.
J. Med. Chem. 55:9831-9837(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 44-168.
[39]"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]
Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 44-168; 333-460 AND 1343-1362 IN COMPLEX WITH ACETYLATED HISTONE, MUTAGENESIS OF ASN-140 AND ASN-433.
[40]"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.
[41]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_055114.1. NM_014299.2.
NP_490597.1. NM_058243.2.
UniGeneHs.187763.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2I8NNMR-A352-457[»]
2LSPNMR-B333-460[»]
2NNUX-ray1.59B1343-1362[»]
2OSSX-ray1.35A44-168[»]
2OUOX-ray1.89A333-460[»]
2YELX-ray1.65A44-168[»]
2YEMX-ray2.30A/B333-460[»]
3MXFX-ray1.60A44-168[»]
3P5OX-ray1.60A44-168[»]
3SVFX-ray1.98A44-168[»]
3SVGX-ray1.68A44-168[»]
3U5JX-ray1.60A44-168[»]
3U5KX-ray1.80A/B/C/D44-168[»]
3U5LX-ray1.39A44-168[»]
3UVWX-ray1.37A44-168[»]
3UVXX-ray1.91A44-168[»]
3UVYX-ray2.02A44-168[»]
3UW9X-ray2.30A/B/C/D44-168[»]
3ZYUX-ray1.50A/B44-168[»]
4A9LX-ray1.60A44-168[»]
4BJXX-ray1.59A44-168[»]
4BW1X-ray1.40A44-168[»]
4BW2X-ray1.92A44-168[»]
4BW3X-ray1.50A44-168[»]
4BW4X-ray1.67A44-168[»]
4C66X-ray1.87A44-167[»]
4C67X-ray1.55A44-168[»]
4CFKX-ray1.55A44-168[»]
4CFLX-ray1.32A44-168[»]
4DONX-ray1.52A44-166[»]
4E96X-ray1.92A44-168[»]
4F3IX-ray1.40A44-168[»]
4GPJX-ray1.60A44-168[»]
4HBVX-ray1.63A44-168[»]
4HBWX-ray1.69A44-168[»]
4HBXX-ray1.62A44-168[»]
4HBYX-ray1.59A44-168[»]
4HXKX-ray1.61A44-167[»]
4HXLX-ray1.52A44-167[»]
4HXMX-ray1.50A44-166[»]
4HXNX-ray1.49A44-167[»]
4HXOX-ray1.76A44-167[»]
4HXPX-ray1.73A44-166[»]
4HXRX-ray1.53A44-167[»]
4HXSX-ray1.43A44-166[»]
4IOOX-ray1.25A44-168[»]
4IOQX-ray1.50A44-168[»]
4IORX-ray1.40A44-168[»]
4J0RX-ray1.72A44-168[»]
4J0SX-ray1.84A44-168[»]
4J3IX-ray1.24A44-168[»]
4KV1X-ray1.50A/B41-168[»]
4KV4X-ray2.00A351-459[»]
4LR6X-ray1.29A42-168[»]
4LRGX-ray2.21A42-168[»]
4LYIX-ray1.30A44-168[»]
4LYSX-ray1.83A44-168[»]
4LYWX-ray1.95A44-168[»]
4LZRX-ray1.85A44-168[»]
4LZSX-ray2.20A44-168[»]
4MENX-ray1.81A44-168[»]
4MEOX-ray1.72A44-168[»]
4MEPX-ray1.85A44-168[»]
4MEQX-ray1.77A44-168[»]
4MR3X-ray1.68A44-168[»]
4MR4X-ray1.66A44-168[»]
4NQMX-ray1.58A44-168[»]
4NR8X-ray1.64A44-168[»]
4O70X-ray1.55A/B44-168[»]
4O71X-ray1.36A/B44-168[»]
4O72X-ray1.40A44-168[»]
4O73X-ray1.40A/B44-168[»]
4O74X-ray1.45A/B44-168[»]
4O75X-ray1.55A44-168[»]
4O76X-ray1.70A/B/C/D44-168[»]
4O77X-ray2.00A/B44-168[»]
4O78X-ray1.34A44-168[»]
4O7AX-ray1.34A44-168[»]
4O7BX-ray1.50A44-168[»]
4O7CX-ray1.55A44-168[»]
4O7EX-ray1.85A/B44-168[»]
4O7FX-ray1.80A/B44-168[»]
4OGIX-ray1.73A/B44-168[»]
4OGJX-ray1.65A/B44-168[»]
ProteinModelPortalO60885.
SMRO60885. Positions 42-166, 333-460, 605-682.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117036. 39 interactions.
DIPDIP-39776N.
IntActO60885. 21 interactions.
MINTMINT-1176376.
STRING9606.ENSP00000263377.

Chemistry

BindingDBO60885.
ChEMBLCHEMBL1163125.

PTM databases

PhosphoSiteO60885.

Proteomic databases

PaxDbO60885.
PeptideAtlasO60885.
PRIDEO60885.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263377; ENSP00000263377; ENSG00000141867. [O60885-1]
ENST00000360016; ENSP00000353112; ENSG00000141867. [O60885-3]
ENST00000371835; ENSP00000360901; ENSG00000141867. [O60885-2]
GeneID23476.
KEGGhsa:23476.
UCSCuc002nar.3. human. [O60885-1]
uc002nas.3. human. [O60885-2]
uc002nat.3. human.

Organism-specific databases

CTD23476.
GeneCardsGC19M015348.
HGNCHGNC:13575. BRD4.
HPAHPA015055.
MIM608749. gene.
neXtProtNX_O60885.
PharmGKBPA25416.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5076.
HOGENOMHOG000231200.
HOVERGENHBG004896.
InParanoidO60885.
KOK11722.
OMAFIATQVP.
PhylomeDBO60885.
TreeFamTF317345.

Gene expression databases

ArrayExpressO60885.
BgeeO60885.
CleanExHS_BRD4.
GenevestigatorO60885.

Family and domain databases

Gene3D1.20.920.10. 2 hits.
InterProIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR027353. NET_dom.
[Graphical view]
PfamPF00439. Bromodomain. 2 hits.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00297. BROMO. 2 hits.
[Graphical view]
SUPFAMSSF47370. SSF47370. 2 hits.
PROSITEPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 2 hits.
PS51525. NET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBRD4. human.
EvolutionaryTraceO60885.
GeneWikiBRD4.
GenomeRNAi23476.
NextBio45817.
PMAP-CutDBO60885.
PROO60885.
SOURCESearch...

Entry information

Entry nameBRD4_HUMAN
AccessionPrimary (citable) accession number: O60885
Secondary accession number(s): O60433 expand/collapse secondary AC list , Q4G0X8, Q86YS8, Q96PD3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 31, 2002
Last modified: April 16, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM