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Protein

Bromodomain-containing protein 3

Gene

Brd3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 of the CCND1 gene (By similarity). Regulates transcription by promoting the binding of the transcription factor GATA1 to its targets.By similarity

GO - Molecular functioni

GO - Biological processi

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):
Bromodomain-containing FSH-like protein FSRG2
Gene namesi
Name:Brd3
Synonyms:Fsrg2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1914632. Brd3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 726726Bromodomain-containing protein 3PRO_0000211182Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei262 – 2621PhosphoserineCombined sources
Modified residuei280 – 2801PhosphoserineBy similarity
Modified residuei564 – 5641PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8K2F0.
MaxQBiQ8K2F0.
PaxDbiQ8K2F0.
PRIDEiQ8K2F0.

PTM databases

iPTMnetiQ8K2F0.
PhosphoSiteiQ8K2F0.

Expressioni

Gene expression databases

BgeeiQ8K2F0.
CleanExiMM_BRD3.
ExpressionAtlasiQ8K2F0. baseline and differential.
GenevisibleiQ8K2F0. MM.

Interactioni

Subunit structurei

Interacts (via bromo domains) with acetylated lysine residues on the N-terminus of histone H2A, H2B, H3 and H4 (in vitro) (By similarity). 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 similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi212148. 2 interactions.
IntActiQ8K2F0. 1 interaction.
MINTiMINT-4089355.
STRINGi10090.ENSMUSP00000109574.

Structurei

Secondary structure

1
726
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 303Combined sources
Helixi36 – 438Combined sources
Helixi45 – 506Combined sources
Helixi56 – 583Combined sources
Turni65 – 684Combined sources
Helixi72 – 754Combined sources
Beta strandi76 – 783Combined sources
Helixi83 – 908Combined sources
Beta strandi94 – 963Combined sources
Helixi97 – 993Combined sources
Helixi100 – 11415Combined sources
Helixi120 – 13617Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L5ENMR-A24-146[»]
ProteinModelPortaliQ8K2F0.
SMRiQ8K2F0. Positions 24-154, 306-415, 572-645.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8K2F0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini50 – 12273Bromo 1PROSITE-ProRule annotationAdd
BLAST
Domaini325 – 39773Bromo 2PROSITE-ProRule annotationAdd
BLAST
Domaini563 – 64583NETPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili452 – 48231Sequence analysisAdd
BLAST
Coiled coili646 – 68944Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi178 – 23457Pro-richAdd
BLAST
Compositional biasi486 – 55671Lys-richAdd
BLAST
Compositional biasi565 – 5695Poly-Glu
Compositional biasi691 – 72535Ser-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

eggNOGiKOG1474. Eukaryota.
COG5076. LUCA.
GeneTreeiENSGT00760000119206.
HOGENOMiHOG000231200.
HOVERGENiHBG004896.
InParanoidiQ8K2F0.
KOiK11721.
OMAiAGRQPKK.
OrthoDBiEOG7TTQ86.
TreeFamiTF317345.

Family and domain databases

Gene3Di1.20.920.10. 2 hits.
InterProiIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR027353. NET_dom.
[Graphical view]
PfamiPF17035. BET. 1 hit.
PF00439. 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.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8K2F0-1) [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
MSTTAAAPTG IPAVPGPVNP PPPEVSNPSK PGRKTNQLQY MQNVVVKTLW
60 70 80 90 100
KHQFAWPFYQ PVDAIKLNLP DYHKIIKNPM DMGTIKKRLE NNYYWSASEC
110 120 130 140 150
MQDFNTMFTN CYIYNKPTDD IVLMAQALEK IFLQKVAQMP QEEVELLPPA
160 170 180 190 200
PKGKGRKPAA GAQNAGSQQV AAVSSVSPAT PFQNIPPTVS QTPVIAATPV
210 220 230 240 250
PTITANVTSV PVPPPAAPPP PATPIVPVVP PTPPVVKKKG VKRKADTTTP
260 270 280 290 300
TTSAITASRS ESPPPLSEPK QAKVVARRES GGRPIKPPKK DLEDGEVPQH
310 320 330 340 350
AGKKGKLSEH LRHCDSILRE MLSKKHAAYA WPFYKPVDAE ALELHDYHDI
360 370 380 390 400
IKHPMDLSTV KRKMDSREYP DAQGFAADIR LMFSNCYKYN PPDHEVVAMA
410 420 430 440 450
RKLQDVFEMR FAKMPDEPME APALPAPTAP IVSKGAESSR SSEESSSDSG
460 470 480 490 500
SSDSEEERAT RLAELQEQLK AVHEQLAALS QAPVNKPKKK KEKKEKEKKK
510 520 530 540 550
KDKDKDKEKE KHKAKSEEEK KAKAAPAAKQ AQQKKAPTKK ANSTTTASRQ
560 570 580 590 600
LKKGGKQASA SYDSEEEEEG LPMSYDEKRQ LSLDINRLPG EKLGRVVHII
610 620 630 640 650
QSREPSLRDS NPDEIEIDFE TLKPTTLREL ERYVKSCLQK KQRKPLSTSG
660 670 680 690 700
KKQAAKSKEE LAQEKKKELE KRLQDVSGQL NSKKPTKKEK SGSAPSGGPS
710 720
RLSSSSSSES ASSSSSGSSS DSSDSE
Length:726
Mass (Da):79,762
Last modified:May 10, 2004 - v2
Checksum:iD5B2FC0ACA41D8ED
GO
Isoform 2 (identifier: Q8K2F0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     468-468: Q → QTGCGAFQDQLLNVSSVQ

Note: No experimental confirmation available.
Show »
Length:743
Mass (Da):81,511
Checksum:iEA325174381A3737
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti174 – 1741S → F in BAC36359 (PubMed:16141072).Curated
Sequence conflicti216 – 2161A → T in AAH31536 (PubMed:15489334).Curated
Sequence conflicti477 – 4771A → D in AAF78072 (Ref. 1) Curated
Sequence conflicti659 – 6602EE → VV in AAF78072 (Ref. 1) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei468 – 4681Q → QTGCGAFQDQLLNVSSVQ in isoform 2. 1 PublicationVSP_010249

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF269193 mRNA. Translation: AAF78072.1.
BC031536 mRNA. Translation: AAH31536.1.
AK037435 mRNA. Translation: BAC29806.1.
AK076472 mRNA. Translation: BAC36359.1.
CCDSiCCDS15828.1. [Q8K2F0-1]
CCDS50546.1. [Q8K2F0-2]
RefSeqiNP_001107045.1. NM_001113573.1. [Q8K2F0-1]
NP_001107046.1. NM_001113574.1. [Q8K2F0-2]
NP_075825.3. NM_023336.4. [Q8K2F0-1]
UniGeneiMm.28721.

Genome annotation databases

EnsembliENSMUST00000028282; ENSMUSP00000028282; ENSMUSG00000026918. [Q8K2F0-1]
ENSMUST00000077737; ENSMUSP00000076918; ENSMUSG00000026918. [Q8K2F0-1]
ENSMUST00000113941; ENSMUSP00000109574; ENSMUSG00000026918. [Q8K2F0-2]
ENSMUST00000164296; ENSMUSP00000128812; ENSMUSG00000026918. [Q8K2F0-1]
GeneIDi67382.
KEGGimmu:67382.
UCSCiuc008ixm.2. mouse. [Q8K2F0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF269193 mRNA. Translation: AAF78072.1.
BC031536 mRNA. Translation: AAH31536.1.
AK037435 mRNA. Translation: BAC29806.1.
AK076472 mRNA. Translation: BAC36359.1.
CCDSiCCDS15828.1. [Q8K2F0-1]
CCDS50546.1. [Q8K2F0-2]
RefSeqiNP_001107045.1. NM_001113573.1. [Q8K2F0-1]
NP_001107046.1. NM_001113574.1. [Q8K2F0-2]
NP_075825.3. NM_023336.4. [Q8K2F0-1]
UniGeneiMm.28721.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L5ENMR-A24-146[»]
ProteinModelPortaliQ8K2F0.
SMRiQ8K2F0. Positions 24-154, 306-415, 572-645.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212148. 2 interactions.
IntActiQ8K2F0. 1 interaction.
MINTiMINT-4089355.
STRINGi10090.ENSMUSP00000109574.

PTM databases

iPTMnetiQ8K2F0.
PhosphoSiteiQ8K2F0.

Proteomic databases

EPDiQ8K2F0.
MaxQBiQ8K2F0.
PaxDbiQ8K2F0.
PRIDEiQ8K2F0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028282; ENSMUSP00000028282; ENSMUSG00000026918. [Q8K2F0-1]
ENSMUST00000077737; ENSMUSP00000076918; ENSMUSG00000026918. [Q8K2F0-1]
ENSMUST00000113941; ENSMUSP00000109574; ENSMUSG00000026918. [Q8K2F0-2]
ENSMUST00000164296; ENSMUSP00000128812; ENSMUSG00000026918. [Q8K2F0-1]
GeneIDi67382.
KEGGimmu:67382.
UCSCiuc008ixm.2. mouse. [Q8K2F0-1]

Organism-specific databases

CTDi8019.
MGIiMGI:1914632. Brd3.

Phylogenomic databases

eggNOGiKOG1474. Eukaryota.
COG5076. LUCA.
GeneTreeiENSGT00760000119206.
HOGENOMiHOG000231200.
HOVERGENiHBG004896.
InParanoidiQ8K2F0.
KOiK11721.
OMAiAGRQPKK.
OrthoDBiEOG7TTQ86.
TreeFamiTF317345.

Miscellaneous databases

ChiTaRSiBrd3. mouse.
EvolutionaryTraceiQ8K2F0.
NextBioi324408.
PROiQ8K2F0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K2F0.
CleanExiMM_BRD3.
ExpressionAtlasiQ8K2F0. baseline and differential.
GenevisibleiQ8K2F0. MM.

Family and domain databases

Gene3Di1.20.920.10. 2 hits.
InterProiIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR027353. NET_dom.
[Graphical view]
PfamiPF17035. BET. 1 hit.
PF00439. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression pattern of Fsrg2, a putative murine bromodomain-containing homolog of the Drosophila gene female sterile homeotic."
    Shang E., Wolgemuth D.J.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  2. "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 1).
    Tissue: Mammary tumor.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-494 (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Head and Thymus.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Kidney and Testis.
  6. "Bromodomain protein Brd3 associates with acetylated GATA1 to promote its chromatin occupancy at erythroid target genes."
    Lamonica J.M., Deng W., Kadauke S., Campbell A.E., Gamsjaeger R., Wang H., Cheng Y., Billin A.N., Hardison R.C., Mackay J.P., Blobel G.A.
    Proc. Natl. Acad. Sci. U.S.A. 108:E159-E168(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ACETYLATED GATA1 AND ACETYLATED HISTONE H4, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Structural basis and specificity of acetylated transcription factor GATA1 recognition by BET family bromodomain protein Brd3."
    Gamsjaeger R., Webb S.R., Lamonica J.M., Billin A., Blobel G.A., Mackay J.P.
    Mol. Cell. Biol. 31:2632-2640(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 24-146 IN COMPLEX WITH ACETYLATED GATA1, INTERACTION WITH ACETYLATED GATA1.

Entry informationi

Entry nameiBRD3_MOUSE
AccessioniPrimary (citable) accession number: Q8K2F0
Secondary accession number(s): Q8C665, Q8CAX7, Q9JI25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: March 16, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.