Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q15059

- BRD3_HUMAN

UniProt

Q15059 - BRD3_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Bromodomain-containing protein 3

Gene

BRD3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling and interaction with transcription factors. Regulates transcription by promoting the binding of the transcription factor GATA1 to its targets (By similarity). Regulates transcription of the CCND1 gene.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei647 – 6482Breakpoint for translocation to form BDR3-NUT fusion protein

GO - Molecular functioni

  1. chromatin binding Source: UniProtKB
  2. lysine-acetylated histone binding Source: UniProtKB

GO - Biological processi

  1. chromatin modification Source: UniProtKB-KW
  2. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  3. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Bromodomain-containing protein 3
Alternative name(s):
RING3-like protein
Gene namesi
Name:BRD3
Synonyms:KIAA0043, RING3L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:1104. BRD3.

Subcellular locationi

Nucleus Curated
Note: Detected on chromatin.By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving BRD3 is found in a rare, aggressive, and lethal carcinoma arising in midline organs of young people. Translocation t(15;9)(q14;q34) with NUT which produces a BRD3-NUT fusion protein.

Organism-specific databases

PharmGKBiPA25415.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 726725Bromodomain-containing protein 3PRO_0000211181Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei263 – 2631Phosphoserine3 Publications
Modified residuei563 – 5631Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ15059.
PaxDbiQ15059.
PRIDEiQ15059.

PTM databases

PhosphoSiteiQ15059.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ15059.
CleanExiHS_BRD3.
ExpressionAtlasiQ15059. baseline and differential.
GenevestigatoriQ15059.

Organism-specific databases

HPAiHPA051830.

Interactioni

Subunit structurei

Interacts (via bromo domain 1) with GATA1 acetylated at 'Lys-312' and 'Lys-315'. Interacts (via bromo domain 1) with GATA2 acetylated on lysine residues (By similarity). Interacts (via bromo domains) with acetylated lysine residues on the N-terminus of histone H2A, H2B, H3 and H4 (in vitro).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MYCP011063EBI-1383460,EBI-447544

Protein-protein interaction databases

BioGridi113715. 10 interactions.
DIPiDIP-39755N.
IntActiQ15059. 3 interactions.
MINTiMINT-3030809.
STRINGi9606.ENSP00000305918.

Structurei

Secondary structure

1
726
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 313
Helixi37 – 448
Helixi46 – 527
Helixi57 – 593
Turni65 – 695
Helixi73 – 764
Helixi83 – 919
Helixi98 – 11518
Helixi121 – 13717
Helixi310 – 32314
Helixi325 – 3273
Helixi328 – 3314
Helixi332 – 3343
Turni340 – 3445
Helixi348 – 3514
Helixi358 – 3669
Helixi373 – 39018
Helixi396 – 41318

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E7NNMR-A306-415[»]
2NXBX-ray1.40A/B24-144[»]
2OO1X-ray1.70A/B/C/D307-416[»]
2YW5NMR-A25-155[»]
3S91X-ray2.06A24-144[»]
3S92X-ray1.36A306-416[»]
ProteinModelPortaliQ15059.
SMRiQ15059. Positions 25-155, 307-416, 571-644.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15059.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini51 – 12373Bromo 1PROSITE-ProRule annotationAdd
BLAST
Domaini326 – 39873Bromo 2PROSITE-ProRule annotationAdd
BLAST
Domaini562 – 64483NETPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili453 – 52472Sequence AnalysisAdd
BLAST
Coiled coili645 – 68440Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi487 – 55569Lys-richAdd
BLAST
Compositional biasi676 – 72550Ser-richAdd
BLAST

Sequence similaritiesi

Contains 2 bromo domains.PROSITE-ProRule annotation
Contains 1 NET domain.PROSITE-ProRule annotation

Keywords - Domaini

Bromodomain, Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG5076.
GeneTreeiENSGT00760000119206.
HOGENOMiHOG000231200.
HOVERGENiHBG004896.
InParanoidiQ15059.
KOiK11721.
OMAiRHCDSIL.
OrthoDBiEOG7TTQ86.
PhylomeDBiQ15059.
TreeFamiTF317345.

Family and domain databases

Gene3Di1.20.920.10. 2 hits.
InterProiIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR027353. NET_dom.
[Graphical view]
PfamiPF00439. Bromodomain. 2 hits.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 2 hits.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 2 hits.
PROSITEiPS00633. BROMODOMAIN_1. 2 hits.
PS50014. BROMODOMAIN_2. 2 hits.
PS51525. NET. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15059-1) [UniParc]FASTAAdd 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.

« Hide

        10         20         30         40         50
MSTATTVAPA GIPATPGPVN PPPPEVSNPS KPGRKTNQLQ YMQNVVVKTL
60 70 80 90 100
WKHQFAWPFY QPVDAIKLNL PDYHKIIKNP MDMGTIKKRL ENNYYWSASE
110 120 130 140 150
CMQDFNTMFT NCYIYNKPTD DIVLMAQALE KIFLQKVAQM PQEEVELLPP
160 170 180 190 200
APKGKGRKPA AGAQSAGTQQ VAAVSSVSPA TPFQSVPPTV SQTPVIAATP
210 220 230 240 250
VPTITANVTS VPVPPAAAPP PPATPIVPVV PPTPPVVKKK GVKRKADTTT
260 270 280 290 300
PTTSAITASR SESPPPLSDP KQAKVVARRE SGGRPIKPPK KDLEDGEVPQ
310 320 330 340 350
HAGKKGKLSE HLRYCDSILR EMLSKKHAAY AWPFYKPVDA EALELHDYHD
360 370 380 390 400
IIKHPMDLST VKRKMDGREY PDAQGFAADV RLMFSNCYKY NPPDHEVVAM
410 420 430 440 450
ARKLQDVFEM RFAKMPDEPV EAPALPAPAA PMVSKGAESS RSSEESSSDS
460 470 480 490 500
GSSDSEEERA TRLAELQEQL KAVHEQLAAL SQAPVNKPKK KKEKKEKEKK
510 520 530 540 550
KKDKEKEKEK HKVKAEEEKK AKVAPPAKQA QQKKAPAKKA NSTTTAGRQL
560 570 580 590 600
KKGGKQASAS YDSEEEEEGL PMSYDEKRQL SLDINRLPGE KLGRVVHIIQ
610 620 630 640 650
SREPSLRDSN PDEIEIDFET LKPTTLRELE RYVKSCLQKK QRKPFSASGK
660 670 680 690 700
KQAAKSKEEL AQEKKKELEK RLQDVSGQLS SSKKPARKEK PGSAPSGGPS
710 720
RLSSSSSSES GSSSSSGSSS DSSDSE
Length:726
Mass (Da):79,542
Last modified:November 1, 1996 - v1
Checksum:i64F526FC3C1033AA
GO
Isoform 2 (identifier: Q15059-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     549-556: QLKKGGKQ → DHFLTCGV
     557-726: Missing.

Note: No experimental confirmation available.

Show »
Length:556
Mass (Da):60,942
Checksum:i8352F5DF1801A793
GO

Sequence cautioni

The sequence BAA05393.2 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 361T → N in a renal clear cell carcinoma sample; somatic mutation. 1 Publication
VAR_041913
Natural varianti161 – 1611A → T in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041914
Natural varianti172 – 1721A → V.1 Publication
Corresponds to variant rs34609592 [ dbSNP | Ensembl ].
VAR_041915
Natural varianti435 – 4351K → Q.1 Publication
Corresponds to variant rs36093130 [ dbSNP | Ensembl ].
VAR_041916
Natural varianti441 – 4411R → H.1 Publication
Corresponds to variant rs56017928 [ dbSNP | Ensembl ].
VAR_041917
Natural varianti447 – 4471S → P.1 Publication
Corresponds to variant rs55754444 [ dbSNP | Ensembl ].
VAR_041918

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei549 – 5568QLKKGGKQ → DHFLTCGV in isoform 2. 1 PublicationVSP_010247
Alternative sequencei557 – 726170Missing in isoform 2. 1 PublicationVSP_010248Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D26362 mRNA. Translation: BAA05393.2. Different initiation.
AY513270 mRNA. Translation: AAS82952.1.
AL445931 Genomic DNA. Translation: CAI13726.1.
AL445931 Genomic DNA. Translation: CAI13727.1.
CH471090 Genomic DNA. Translation: EAW88113.1.
CH471090 Genomic DNA. Translation: EAW88114.1.
BC032124 mRNA. Translation: AAH32124.1.
Z81330 Genomic DNA. No translation available.
CCDSiCCDS6980.1. [Q15059-1]
RefSeqiNP_031397.1. NM_007371.3. [Q15059-1]
XP_006717354.1. XM_006717291.1. [Q15059-1]
UniGeneiHs.522472.
Hs.654869.

Genome annotation databases

EnsembliENST00000303407; ENSP00000305918; ENSG00000169925. [Q15059-1]
ENST00000371834; ENSP00000360900; ENSG00000169925. [Q15059-2]
GeneIDi8019.
KEGGihsa:8019.
UCSCiuc004cew.3. human. [Q15059-1]
uc004cex.2. human. [Q15059-2]

Polymorphism databases

DMDMi12643726.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D26362 mRNA. Translation: BAA05393.2 . Different initiation.
AY513270 mRNA. Translation: AAS82952.1 .
AL445931 Genomic DNA. Translation: CAI13726.1 .
AL445931 Genomic DNA. Translation: CAI13727.1 .
CH471090 Genomic DNA. Translation: EAW88113.1 .
CH471090 Genomic DNA. Translation: EAW88114.1 .
BC032124 mRNA. Translation: AAH32124.1 .
Z81330 Genomic DNA. No translation available.
CCDSi CCDS6980.1. [Q15059-1 ]
RefSeqi NP_031397.1. NM_007371.3. [Q15059-1 ]
XP_006717354.1. XM_006717291.1. [Q15059-1 ]
UniGenei Hs.522472.
Hs.654869.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2E7N NMR - A 306-415 [» ]
2NXB X-ray 1.40 A/B 24-144 [» ]
2OO1 X-ray 1.70 A/B/C/D 307-416 [» ]
2YW5 NMR - A 25-155 [» ]
3S91 X-ray 2.06 A 24-144 [» ]
3S92 X-ray 1.36 A 306-416 [» ]
ProteinModelPortali Q15059.
SMRi Q15059. Positions 25-155, 307-416, 571-644.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113715. 10 interactions.
DIPi DIP-39755N.
IntActi Q15059. 3 interactions.
MINTi MINT-3030809.
STRINGi 9606.ENSP00000305918.

Chemistry

BindingDBi Q15059.
ChEMBLi CHEMBL1795186.
GuidetoPHARMACOLOGYi 2725.

PTM databases

PhosphoSitei Q15059.

Polymorphism databases

DMDMi 12643726.

Proteomic databases

MaxQBi Q15059.
PaxDbi Q15059.
PRIDEi Q15059.

Protocols and materials databases

DNASUi 8019.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000303407 ; ENSP00000305918 ; ENSG00000169925 . [Q15059-1 ]
ENST00000371834 ; ENSP00000360900 ; ENSG00000169925 . [Q15059-2 ]
GeneIDi 8019.
KEGGi hsa:8019.
UCSCi uc004cew.3. human. [Q15059-1 ]
uc004cex.2. human. [Q15059-2 ]

Organism-specific databases

CTDi 8019.
GeneCardsi GC09M136897.
HGNCi HGNC:1104. BRD3.
HPAi HPA051830.
MIMi 601541. gene.
neXtProti NX_Q15059.
PharmGKBi PA25415.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5076.
GeneTreei ENSGT00760000119206.
HOGENOMi HOG000231200.
HOVERGENi HBG004896.
InParanoidi Q15059.
KOi K11721.
OMAi RHCDSIL.
OrthoDBi EOG7TTQ86.
PhylomeDBi Q15059.
TreeFami TF317345.

Miscellaneous databases

EvolutionaryTracei Q15059.
GeneWikii BRD3.
GenomeRNAii 8019.
NextBioi 30578.
PROi Q15059.
SOURCEi Search...

Gene expression databases

Bgeei Q15059.
CleanExi HS_BRD3.
ExpressionAtlasi Q15059. baseline and differential.
Genevestigatori Q15059.

Family and domain databases

Gene3Di 1.20.920.10. 2 hits.
InterProi IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR027353. NET_dom.
[Graphical view ]
Pfami PF00439. Bromodomain. 2 hits.
[Graphical view ]
PRINTSi PR00503. BROMODOMAIN.
SMARTi SM00297. BROMO. 2 hits.
[Graphical view ]
SUPFAMi SSF47370. SSF47370. 2 hits.
PROSITEi PS00633. BROMODOMAIN_1. 2 hits.
PS50014. BROMODOMAIN_2. 2 hits.
PS51525. NET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
    Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
    DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  2. "Differentially expressed genes in endothelial differentiation."
    Ishii H., Mimori K., Mori M., Vecchione A.
    DNA Cell Biol. 24:432-437(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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 2).
    Tissue: Colon.
  6. "Chromosomal localization, gene structure and transcription pattern of the ORFX gene, a homologue of the MHC-linked RING3 gene."
    Thorpe K.L., Gorman P., Thomas C., Sheer D., Trowsdale J., Beck S.
    Gene 200:177-183(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 363-726.
  7. "The double bromodomain proteins Brd2 and Brd3 couple histone acetylation to transcription."
    LeRoy G., Rickards B., Flint S.J.
    Mol. Cell 30:51-60(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ACETYLATED CHROMATIN.
  8. "BRD-NUT oncoproteins: a family of closely related nuclear proteins that block epithelial differentiation and maintain the growth of carcinoma cells."
    French C.A., Ramirez C.L., Kolmakova J., Hickman T.T., Cameron M.J., Thyne M.E., Kutok J.L., Toretsky J.A., Tadavarthy A.K., Kees U.R., Fletcher J.A., Aster J.C.
    Oncogene 27:2237-2242(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION WITH NUT.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND SER-563, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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-263 AND SER-563, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Solution structure of the first and second bromodomain from human bromodomain containing protein 3."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 25-415.
  15. Cited for: X-RAY CRYSTALLOGRAPHY (1.36 ANGSTROMS) OF 24-416, SUBUNIT, DOMAIN.
  16. "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.
    , 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] ASN-36; THR-161; VAL-172; GLN-435; HIS-441 AND PRO-447.

Entry informationi

Entry nameiBRD3_HUMAN
AccessioniPrimary (citable) accession number: Q15059
Secondary accession number(s): B1APD9
, Q4G5Y3, Q5T1R7, Q8N5M3, Q92645
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 138 of the entry and version 1 of the sequence. [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 chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3