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UniProtKB - O60885 (BRD4_HUMAN)

Protein

Bromodomain-containing protein 4

Gene

BRD4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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 (PubMed:22509028). 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.1 Publication
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.

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 (PubMed:20871596, PubMed:21068722, PubMed:21964340). 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 (PubMed:21964340).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei140Acetylated histones1 Publication1
Binding sitei140Inhibitor1
Binding sitei433Acetylated histones1 Publication1
Binding sitei433Inhibitor1

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • lysine-acetylated histone binding Source: UniProtKB
  • p53 binding Source: UniProtKB
  • RNA polymerase II CTD heptapeptide repeat kinase activity Source: MGI
  • RNA polymerase II C-terminal domain binding Source: MGI
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionChromatin regulator
Biological processDNA damage, Host-virus interaction, Transcription, Transcription regulation

Enzyme and pathway databases

SIGNORiO60885

Names & Taxonomyi

Protein namesi
Recommended name:
Bromodomain-containing protein 4
Alternative name(s):
Protein HUNK1
Gene namesi
Name:BRD4
Synonyms:HUNK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000141867.17
HGNCiHGNC:13575 BRD4
MIMi608749 gene
neXtProtiNX_O60885

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi140N → A: Abolishes binding to acetylated histones. 2 Publications1
Mutagenesisi433N → A: Abolishes binding to acetylated histones. 1 Publication1
Mutagenesisi492 – 494SSS → ASA: Impaired phosphorylation by CK2 and binding to acetylated histones. 1 Publication3
Mutagenesisi498 – 500SST → AAA: Impaired phosphorylation by CK2 and binding to acetylated histones. 1 Publication3
Mutagenesisi503S → A: Impaired phosphorylation by CK2 and binding to acetylated histones. 1 Publication1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei719 – 720Breakpoint for translocation to form BDR4-NUT fusion protein2

Organism-specific databases

DisGeNETi23476
MalaCardsiBRD4
OpenTargetsiENSG00000141867
Orphaneti443167 NUT midline carcinoma
PharmGKBiPA25416

Chemistry databases

ChEMBLiCHEMBL1163125
GuidetoPHARMACOLOGYi1945

Polymorphism and mutation databases

BioMutaiBRD4

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002111831 – 1362Bromodomain-containing protein 4Add BLAST1362

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki99Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei470PhosphoserineCombined sources1
Modified residuei484Phosphoserine; by CK21 Publication1
Modified residuei488Phosphoserine; by CK21 Publication1
Modified residuei492Phosphoserine; by CK21 Publication1
Modified residuei494Phosphoserine; by CK21 Publication1
Modified residuei498Phosphoserine; by CK21 Publication1
Modified residuei499Phosphoserine; by CK21 Publication1
Modified residuei503Phosphoserine; by CK21 Publication1
Cross-linki585Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei601PhosphoserineCombined sources1
Cross-linki645Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki694Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1050Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1111N6-acetyllysine; alternateCombined sources1
Cross-linki1111Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki1111Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei1117PhosphoserineCombined sources1
Modified residuei1126PhosphoserineCombined sources1
Cross-linki1197Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1201PhosphoserineCombined sources1
Modified residuei1204PhosphoserineCombined sources1

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO60885
MaxQBiO60885
PaxDbiO60885
PeptideAtlasiO60885
PRIDEiO60885
ProteomicsDBi49651
49652 [O60885-2]

PTM databases

iPTMnetiO60885
PhosphoSitePlusiO60885

Miscellaneous databases

PMAP-CutDBiO60885

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiENSG00000141867 Expressed in 239 organ(s), highest expression level in amniotic fluid
CleanExiHS_BRD4
ExpressionAtlasiO60885 baseline and differential
GenevisibleiO60885 HS

Organism-specific databases

HPAiCAB068177
CAB068178
HPA015055
HPA061646

Interactioni

Subunit structurei

Interacts with p53/TP53; the interaction is direct (PubMed:23317504). Interacts (via CTD region) with CDK9 and CCNT1, acting as an associated component of P-TEFb complex (PubMed:16109376, PubMed:16109377). Interacts with RELA (when acetylated at 'Lys-310')(PubMed:19103749). Interacts (via NET domain) with WHSC1L1, JMJD6, CHD4, BICRA and ATAD5 (PubMed:21555454). The interaction with BICRA bridges BRD4 to the GBAF complex (PubMed:29374058, PubMed:16109376, PubMed:16109377, PubMed:19103749, PubMed:21555454, PubMed:23317504). Isoform B: interacts with NCAPD3 and SMC2 (PubMed:23728299).7 Publications
(Microbial infection) Interacts with bovine papillomavirus type 1 regulatory protein E2. This interactions may serve for the tethering of viral genomes to host mitotic chromosomes allowing successful partitioning of the viral genome during cell division.1 Publication
(Microbial infection) Interacts with Epstein-Barr virus (EBV) protein EBNA1; this interaction facilitates transcriptional activation by EBNA1.1 Publication
(Microbial infection) Interacts with human herpes virus-8 (HHV-8) protein LANA.1 Publication

Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi117036, 98 interactors
CORUMiO60885
DIPiDIP-39776N
IntActiO60885, 45 interactors
MINTiO60885
STRINGi9606.ENSP00000263377

Chemistry databases

BindingDBiO60885

Structurei

Secondary structure

11362
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliO60885
SMRiO60885
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60885

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini75 – 147Bromo 1PROSITE-ProRule annotationAdd BLAST73
Domaini368 – 440Bromo 2PROSITE-ProRule annotationAdd BLAST73
Domaini600 – 682NETPROSITE-ProRule annotationAdd BLAST83

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni484 – 503NPS regionAdd BLAST20
Regioni524 – 579BID regionAdd BLAST56
Regioni1047 – 1362C-terminal (CTD) regionAdd BLAST316

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi535 – 594Lys-richAdd BLAST60
Compositional biasi692 – 717Ser-richAdd BLAST26
Compositional biasi703 – 714Poly-SerAdd BLAST12
Compositional biasi738 – 743Poly-His6
Compositional biasi757 – 761Poly-Pro5
Compositional biasi764 – 770Poly-Pro7
Compositional biasi771 – 775Poly-Gln5
Compositional biasi776 – 783Poly-Pro8
Compositional biasi954 – 964Poly-ProAdd BLAST11
Compositional biasi974 – 986Poly-ProAdd BLAST13
Compositional biasi1011 – 1014Poly-Pro4
Compositional biasi1028 – 1033Poly-Pro6
Compositional biasi1283 – 1300Poly-GlnAdd BLAST18
Compositional biasi1301 – 1308Poly-Ala8
Compositional biasi1335 – 1338Poly-Arg4

Domaini

The NET domain mediates interaction with a number of chromatin proteins involved in transcription regulation (WHSC1L1, JMJD6, CHD4, GLTSCR1 and ATAD5).1 Publication
The C-terminal (CTD) region mediates interaction and recruitment of CDK9 and CCNT1 subunits of the P-TEFb complex (PubMed:16109376, PubMed:16109377). It is also required for maintenance of higher-order chromatin structure (PubMed:22334664).3 Publications
The 2 bromo domains mediate specific binding to acetylated histones via Asn-140 and Asn-433, respectively (PubMed:20871596). 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 (PubMed:22464331). 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 (PubMed:22137933, PubMed:22136404, PubMed:23517011, PubMed:23530754).6 Publications

Keywords - Domaini

Bromodomain, Repeat

Phylogenomic databases

eggNOGiKOG1474 Eukaryota
COG5076 LUCA
GeneTreeiENSGT00930000150866
HOGENOMiHOG000231200
HOVERGENiHBG004896
InParanoidiO60885
KOiK11722
OMAiPRPVHMQ
OrthoDBiEOG091G01QC
PhylomeDBiO60885
TreeFamiTF317345

Family and domain databases

Gene3Di1.20.1270.220, 1 hit
1.20.920.10, 2 hits
InterProiView protein in InterPro
IPR031354 BRD4_CDT
IPR001487 Bromodomain
IPR036427 Bromodomain-like_sf
IPR018359 Bromodomain_CS
IPR027353 NET_dom
IPR038336 NET_sf
PfamiView protein in Pfam
PF17035 BET, 1 hit
PF17105 BRD4_CDT, 1 hit
PF00439 Bromodomain, 2 hits
PRINTSiPR00503 BROMODOMAIN
SMARTiView protein in SMART
SM00297 BROMO, 2 hits
SUPFAMiSSF47370 SSF47370, 2 hits
PROSITEiView protein in PROSITE
PS00633 BROMODOMAIN_1, 1 hit
PS50014 BROMODOMAIN_2, 2 hits
PS51525 NET, 1 hit

Sequences (3+)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform A (identifier: O60885-1) [UniParc]FASTAAdd to basket
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.

« Hide
        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
Length:1,362
Mass (Da):152,219
Last modified:January 31, 2002 - v2
Checksum:iD52EFE1CF9960907
GO
Isoform C (identifier: O60885-2) [UniParc]FASTAAdd to basket
Also known as: Brd4S, Short

The sequence of this isoform differs from the canonical sequence as follows:
     720-722: EMA → GPA
     723-1362: Missing.

Show »
Length:722
Mass (Da):80,463
Checksum:iFF040EE016B37F87
GO
Isoform B (identifier: O60885-3) [UniParc]FASTAAdd to basket

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.
Show »
Length:794
Mass (Da):88,289
Checksum:iACB01CC53AA4C431
GO

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
M0QZD9M0QZD9_HUMAN
Bromodomain-containing protein 4
BRD4
572Annotation score:
M0QYW0M0QYW0_HUMAN
Bromodomain containing 4, isoform C...
BRD4 hCG_2000917
146Annotation score:
M0R0H4M0R0H4_HUMAN
Bromodomain-containing protein 4
BRD4
105Annotation score:

Sequence cautioni

The sequence AAC27978 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04191937P → S1 PublicationCorresponds to variant dbSNP:rs35177876Ensembl.1
Natural variantiVAR_041920371A → G1 PublicationCorresponds to variant dbSNP:rs55805532Ensembl.1
Natural variantiVAR_041921563S → N1 PublicationCorresponds to variant dbSNP:rs55970906Ensembl.1
Natural variantiVAR_041922598T → S1 PublicationCorresponds to variant dbSNP:rs34362023Ensembl.1
Natural variantiVAR_041923669R → H1 PublicationCorresponds to variant dbSNP:rs35824241Ensembl.1
Natural variantiVAR_0484271097R → H. Corresponds to variant dbSNP:rs35676845Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_047671720 – 1362EMAPK…EENLF → AFCTSGDFVSPGPSPYHSHV QCGRFREMLRWFLVDVEQTA AGQPHRQSAAGPAITWAPAI AYPSPECARCCVGCS in isoform B. 1 PublicationAdd BLAST643
Alternative sequenceiVSP_010902720 – 722EMA → GPA in isoform C. 1 Publication3
Alternative sequenceiVSP_010903723 – 1362Missing in isoform C. 1 PublicationAdd BLAST640

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links 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.
CCDSiCCDS12328.1 [O60885-1]
CCDS46004.1 [O60885-2]
CCDS82307.1 [O60885-3]
RefSeqiNP_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]
UniGeneiHs.187763

Genome annotation databases

EnsembliENST00000263377; ENSP00000263377; ENSG00000141867 [O60885-1]
ENST00000360016; ENSP00000353112; ENSG00000141867 [O60885-3]
ENST00000371835; ENSP00000360901; ENSG00000141867 [O60885-2]
GeneIDi23476
KEGGihsa:23476
UCSCiuc002nar.4 human [O60885-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Similar proteinsi

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links 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.
CCDSiCCDS12328.1 [O60885-1]
CCDS46004.1 [O60885-2]
CCDS82307.1 [O60885-3]
RefSeqiNP_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]
UniGeneiHs.187763

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2I8NNMR-A352-457[»]
2LSPNMR-B333-460[»]
2MJVNMR-B333-460[»]
2N3KNMR-A600-678[»]
2NCZNMR-A601-683[»]
2ND0NMR-A601-683[»]
2ND1NMR-A601-683[»]
2NNUX-ray1.59B1343-1362[»]
2OSSX-ray1.35A44-168[»]
2OUOX-ray1.89A333-460[»]
2YELX-ray1.65A44-168[»]
2YEMX-ray2.30A/B333-460[»]
3MXFX-ray1.60A42-168[»]
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[»]
4CL9X-ray1.40A44-168[»]
4CLBX-ray1.60A44-168[»]
4DONX-ray1.52A44-166[»]
4E96X-ray1.92A44-168[»]
4F3IX-ray1.40A44-168[»]
4GPJX-ray1.60A44-168[»]
4HBVX-ray1.63A42-168[»]
4HBWX-ray1.69A42-168[»]
4HBXX-ray1.62A42-168[»]
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[»]
4NUCX-ray1.40A44-168[»]
4NUDX-ray1.20A44-168[»]
4NUEX-ray1.30A44-168[»]
4O70X-ray1.55A/B44-168[»]
4O71X-ray1.36A/B44-168[»]
4O72X-ray1.40A44-168[»]
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[»]
4PCEX-ray1.29A44-168[»]
4PCIX-ray1.25A44-168[»]
4PS5X-ray1.40A/B44-168[»]
4QB3X-ray0.94A44-168[»]
4QR3X-ray1.37A44-166[»]
4QR4X-ray1.28A44-166[»]
4QR5X-ray1.41A44-166[»]
4QZSX-ray1.45A44-168[»]
4UIXX-ray1.58A/B/C44-168[»]
4UIYX-ray1.30A44-168[»]
4UIZX-ray1.19A44-168[»]
4UYDX-ray1.37A44-183[»]
4WHWX-ray1.34A44-168[»]
4WIVX-ray1.56A44-168[»]
4X2IX-ray1.20A42-166[»]
4XY9X-ray1.83A42-168[»]
4XYAX-ray2.05A42-168[»]
4YH3X-ray1.60A44-170[»]
4YH4X-ray1.33A44-170[»]
4Z1QX-ray1.40A/B42-167[»]
4Z1SX-ray1.06A/B42-166[»]
4Z93X-ray1.27A349-460[»]
4ZC9X-ray0.99A44-168[»]
4ZW1X-ray1.75A44-168[»]
5A5SX-ray1.36A44-168[»]
5A85X-ray1.72A44-168[»]
5ACYX-ray2.01A/B44-168[»]
5AD2X-ray2.01A/B44-168[»]
5AD3X-ray1.49A/B44-168[»]
5BT4X-ray1.50A/B/C44-168[»]
5CFWX-ray1.15A44-168[»]
5COIX-ray1.62A44-168[»]
5CP5X-ray1.79A44-168[»]
5CPEX-ray1.62A44-168[»]
5CQTX-ray1.60A44-168[»]
5CRMX-ray1.99A44-168[»]
5CRZX-ray2.12A44-168[»]
5CS8X-ray1.62A44-168[»]
5CTLX-ray2.51A44-168[»]
5CY9X-ray1.55A44-168[»]
5D0CX-ray1.49A44-168[»]
5D24X-ray1.65A43-168[»]
5D25X-ray1.70A43-168[»]
5D26X-ray1.82A42-168[»]
5D3HX-ray1.70A44-168[»]
5D3JX-ray1.70A43-168[»]
5D3LX-ray1.50A42-168[»]
5D3NX-ray2.15A43-168[»]
5D3PX-ray1.95A42-168[»]
5D3RX-ray2.20A42-168[»]
5D3SX-ray1.75A44-168[»]
5D3TX-ray1.93A42-168[»]
5DLXX-ray1.90A44-168[»]
5DLZX-ray1.70A44-168[»]
5DW2X-ray1.12A44-170[»]
5DX4X-ray2.30A44-168[»]
5E0RX-ray1.35A44-168[»]
5EGUX-ray2.21A/B/C/D44-168[»]
5EI4X-ray1.05A44-168[»]
5EISX-ray1.60A44-168[»]
5F5ZX-ray1.76A44-168[»]
5F60X-ray1.35A44-168[»]
5F61X-ray1.45A/B44-168[»]
5F62X-ray1.35A44-168[»]
5F63X-ray1.45A44-168[»]
5FBXX-ray1.85A44-168[»]
5H21X-ray1.59A44-167[»]
5HCLX-ray1.50A44-168[»]
5HLSX-ray2.18A42-168[»]
5HM0X-ray1.40A42-168[»]
5HQ5X-ray1.60A44-168[»]
5HQ6X-ray1.95A44-166[»]
5HQ7X-ray1.90A44-167[»]
5I80X-ray1.45A42-167[»]
5I88X-ray1.40A42-167[»]
5IGKX-ray1.70A44-168[»]
5JWMX-ray1.71A/B333-460[»]
5KDHX-ray1.50A44-168[»]
5KHMX-ray1.48A/B44-168[»]
5KJ0X-ray1.51A44-168[»]
5KU3X-ray1.14A42-167[»]
5LJ1X-ray1.90A42-168[»]
5LJ2X-ray1.19A42-168[»]
5LRQX-ray1.70A42-163[»]
5LUUX-ray1.61A44-168[»]
5M39X-ray1.38A/B42-168[»]
5M3AX-ray1.65A44-168[»]
5MKZX-ray1.62A44-168[»]
5MLIX-ray1.63A42-168[»]
5N2MX-ray1.54A44-168[»]
5NNCX-ray2.22A/B44-168[»]
5NNDX-ray1.82A/B44-168[»]
5NNEX-ray1.15A44-168[»]
5NNFX-ray1.15A44-168[»]
5NNGX-ray1.20A44-168[»]
5O97X-ray1.30A44-168[»]
5T35X-ray2.70A/E333-460[»]
5TI2X-ray1.65A44-168[»]
5TI3X-ray1.70A44-168[»]
5TI4X-ray1.62A44-168[»]
5TI5X-ray1.83A44-168[»]
5TI6X-ray1.70A44-168[»]
5TI7X-ray1.65A44-168[»]
5U28X-ray1.80A44-180[»]
5U2CX-ray3.30A/B342-460[»]
5U2EX-ray1.99A/B42-180[»]
5U2FX-ray2.52A/B42-180[»]
5UEOX-ray1.85A/B352-457[»]
5UEPX-ray1.77A352-457[»]
5UEQX-ray1.70A352-457[»]
5UERX-ray1.87A352-457[»]
5UESX-ray1.62A352-457[»]
5UETX-ray2.29A352-457[»]
5UEUX-ray2.26A/B352-457[»]
5UEVX-ray1.94A352-457[»]
5UEXX-ray2.29A352-457[»]
5UEYX-ray2.41A352-457[»]
5UEZX-ray1.51A352-457[»]
5UF0X-ray1.35A352-457[»]
5ULAX-ray1.50A/B44-168[»]
5UOOX-ray1.69A333-460[»]
5UVSX-ray2.15A352-457[»]
5UVTX-ray1.67A352-457[»]
5UVUX-ray1.66A352-457[»]
5UVVX-ray1.99A/B352-457[»]
5UVWX-ray2.14A/B/C57-165[»]
5UVXX-ray1.53A/B352-457[»]
5UVYX-ray2.25A352-457[»]
5UVZX-ray1.63A352-457[»]
5V67X-ray1.78A44-168[»]
5VBOX-ray1.30A44-168[»]
5VBPX-ray1.83A/B44-168[»]
5VOMX-ray1.67A/B44-168[»]
5VZSX-ray1.71A/B42-168[»]
5W55X-ray1.35A42-168[»]
5WA5X-ray1.17A42-168[»]
5WMAX-ray1.40A44-168[»]
5WMDX-ray1.27A44-168[»]
5WMGX-ray1.19A44-168[»]
5WUUX-ray1.72A44-167[»]
5XHYX-ray1.98A44-166[»]
5XI2X-ray1.91A44-166[»]
5XI3X-ray1.67A44-166[»]
5XI4X-ray1.49A44-166[»]
5Y1YX-ray1.91A44-167[»]
5Y8CX-ray1.42A44-166[»]
5Y8WX-ray1.76A44-168[»]
5Y8YX-ray1.87A44-168[»]
5Y8ZX-ray1.84A44-168[»]
5Y93X-ray1.62A44-168[»]
5Y94X-ray2.00A44-168[»]
5Z9CNMR-A53-168[»]
6BN7X-ray3.50C42-168[»]
6BN8X-ray3.99C42-168[»]
6BN9X-ray4.38C42-168[»]
6BNBX-ray6.34C42-168[»]
6BNHNMR-A601-683[»]
6BOYX-ray3.33C42-168[»]
6C7QX-ray1.51A333-460[»]
6C7RX-ray1.50A44-165[»]
6CD4X-ray1.23A42-168[»]
6CISX-ray1.51A44-166[»]
6CIYX-ray1.68A44-168[»]
6CJ1X-ray1.53A44-166[»]
6CKRX-ray1.62A/B44-168[»]
6CKSX-ray1.72A44-168[»]
6CZUX-ray1.47A42-170[»]
6CZVX-ray1.88A42-170[»]
6DJCX-ray1.46A/B44-173[»]
6DNEX-ray2.96A/B44-477[»]
6E4AX-ray1.26A/B44-170[»]
6FNXX-ray1.19A44-168[»]
6FO5X-ray0.95A44-168[»]
6FSYX-ray1.34A42-168[»]
6FT3X-ray1.28A42-168[»]
6FT4X-ray1.34A42-168[»]
6HDQX-ray1.70A44-168[»]
ProteinModelPortaliO60885
SMRiO60885
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117036, 98 interactors
CORUMiO60885
DIPiDIP-39776N
IntActiO60885, 45 interactors
MINTiO60885
STRINGi9606.ENSP00000263377

Chemistry databases

BindingDBiO60885
ChEMBLiCHEMBL1163125
GuidetoPHARMACOLOGYi1945

PTM databases

iPTMnetiO60885
PhosphoSitePlusiO60885

Polymorphism and mutation databases

BioMutaiBRD4

Proteomic databases

EPDiO60885
MaxQBiO60885
PaxDbiO60885
PeptideAtlasiO60885
PRIDEiO60885
ProteomicsDBi49651
49652 [O60885-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263377; ENSP00000263377; ENSG00000141867 [O60885-1]
ENST00000360016; ENSP00000353112; ENSG00000141867 [O60885-3]
ENST00000371835; ENSP00000360901; ENSG00000141867 [O60885-2]
GeneIDi23476
KEGGihsa:23476
UCSCiuc002nar.4 human [O60885-1]

Organism-specific databases

CTDi23476
DisGeNETi23476
EuPathDBiHostDB:ENSG00000141867.17
GeneCardsiBRD4
HGNCiHGNC:13575 BRD4
HPAiCAB068177
CAB068178
HPA015055
HPA061646
MalaCardsiBRD4
MIMi608749 gene
neXtProtiNX_O60885
OpenTargetsiENSG00000141867
Orphaneti443167 NUT midline carcinoma
PharmGKBiPA25416
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1474 Eukaryota
COG5076 LUCA
GeneTreeiENSGT00930000150866
HOGENOMiHOG000231200
HOVERGENiHBG004896
InParanoidiO60885
KOiK11722
OMAiPRPVHMQ
OrthoDBiEOG091G01QC
PhylomeDBiO60885
TreeFamiTF317345

Enzyme and pathway databases

SIGNORiO60885

Miscellaneous databases

ChiTaRSiBRD4 human
EvolutionaryTraceiO60885
GeneWikiiBRD4
GenomeRNAii23476
PMAP-CutDBiO60885
PROiPR:O60885
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000141867 Expressed in 239 organ(s), highest expression level in amniotic fluid
CleanExiHS_BRD4
ExpressionAtlasiO60885 baseline and differential
GenevisibleiO60885 HS

Family and domain databases

Gene3Di1.20.1270.220, 1 hit
1.20.920.10, 2 hits
InterProiView protein in InterPro
IPR031354 BRD4_CDT
IPR001487 Bromodomain
IPR036427 Bromodomain-like_sf
IPR018359 Bromodomain_CS
IPR027353 NET_dom
IPR038336 NET_sf
PfamiView protein in Pfam
PF17035 BET, 1 hit
PF17105 BRD4_CDT, 1 hit
PF00439 Bromodomain, 2 hits
PRINTSiPR00503 BROMODOMAIN
SMARTiView protein in SMART
SM00297 BROMO, 2 hits
SUPFAMiSSF47370 SSF47370, 2 hits
PROSITEiView protein in PROSITE
PS00633 BROMODOMAIN_1, 1 hit
PS50014 BROMODOMAIN_2, 2 hits
PS51525 NET, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiBRD4_HUMAN
AccessioniPrimary (citable) accession number: O60885
Secondary accession number(s): O60433
, Q4G0X8, Q86YS8, Q96PD3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 31, 2002
Last modified: November 7, 2018
This is version 178 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  2. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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