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Protein

Bromodomain-containing protein 2

Gene

BRD2

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

Functioni

May play a role in spermatogenesis or folliculogenesis (By similarity). Binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling. Regulates transcription of the CCND1 gene. Plays a role in nucleosome assembly.By similarity1 Publication

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • lysine-acetylated histone binding Source: UniProtKB

GO - Biological processi

  • chromatin modification Source: UniProtKB-KW
  • nucleosome assembly Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • spermatogenesis Source: ProtInc
  • 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 2
Alternative name(s):
O27.1.1
Really interesting new gene 3 protein
Gene namesi
Name:BRD2
Synonyms:KIAA9001, RING3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:1103. BRD2.

Subcellular locationi

  • Nucleus Curated

  • Note: Detected on chromatin and nucleosomes.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi78 – 781Q → A: Loss of homodimerization. 1 Publication
Mutagenesisi142 – 1432MQ → AA: Loss of homodimerization. 1 Publication
Mutagenesisi153 – 1531Y → K: Loss of homodimerization. 1 Publication
Mutagenesisi154 – 1541I → A: Partial loss of homodimerization; when associated with A-182. 1 Publication
Mutagenesisi170 – 1701E → A: Loss of homodimerization. 1 Publication
Mutagenesisi174 – 1741L → E: Loss of homodimerization. 1 Publication
Mutagenesisi177 – 1771V → E: Loss of homodimerization. 1 Publication
Mutagenesisi182 – 1821Q → A: Partial loss of homodimerization; when associated with A-154. 1 Publication

Organism-specific databases

PharmGKBiPA25414.

Chemistry

ChEMBLiCHEMBL1293289.
GuidetoPHARMACOLOGYi1944.

Polymorphism and mutation databases

BioMutaiBRD2.
DMDMi12230989.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 801801Bromodomain-containing protein 2PRO_0000211180Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei6 – 61PhosphothreonineCombined sources
Modified residuei37 – 371PhosphoserineCombined sources
Modified residuei298 – 2981PhosphoserineCombined sources
Modified residuei301 – 3011PhosphoserineCombined sources
Modified residuei305 – 3051PhosphoserineCombined sources
Modified residuei633 – 6331PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP25440.
MaxQBiP25440.
PaxDbiP25440.
PRIDEiP25440.

PTM databases

iPTMnetiP25440.
PhosphoSiteiP25440.

Expressioni

Gene expression databases

BgeeiP25440.
CleanExiHS_BRD2.
ExpressionAtlasiP25440. baseline and differential.
GenevisibleiP25440. HS.

Organism-specific databases

HPAiHPA042816.
HPA054746.

Interactioni

Subunit structurei

Homodimer. Interacts with E2F1 and with histone H4 acetylated at 'Lys-13'.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HIST1H4KP628055EBI-2874802,EBI-302023
RUNX3Q137618EBI-2874802,EBI-925990

GO - Molecular functioni

  • lysine-acetylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111973. 36 interactions.
DIPiDIP-60835N.
IntActiP25440. 19 interactions.
MINTiMINT-4530155.
STRINGi9606.ENSP00000378702.

Structurei

Secondary structure

1
801
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi77 – 848Combined sources
Helixi86 – 916Combined sources
Helixi97 – 993Combined sources
Helixi105 – 1084Combined sources
Helixi113 – 1164Combined sources
Helixi123 – 1319Combined sources
Helixi138 – 15518Combined sources
Helixi161 – 17717Combined sources
Helixi344 – 36118Combined sources
Helixi363 – 3653Combined sources
Helixi366 – 3694Combined sources
Helixi370 – 3723Combined sources
Helixi378 – 3814Combined sources
Helixi386 – 3894Combined sources
Helixi396 – 4049Combined sources
Turni406 – 4083Combined sources
Helixi411 – 42818Combined sources
Helixi434 – 45118Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X0JX-ray1.80A/B/C73-194[»]
2DVQX-ray2.04A/B/C73-194[»]
2DVRX-ray2.30A/B/C73-194[»]
2DVSX-ray2.04A/B/C73-194[»]
2DVVX-ray1.80A348-455[»]
2E3KX-ray2.30A/B/C/D348-455[»]
2G4ANMR-A348-455[»]
2YDWX-ray1.90A/B/C67-200[»]
2YEKX-ray1.98A/B/C67-200[»]
3AQAX-ray2.30A/B/C73-194[»]
3ONIX-ray1.61A344-455[»]
4A9EX-ray1.91A/B/C67-200[»]
4A9FX-ray1.73A/B/C67-200[»]
4A9HX-ray2.05A/B/C67-200[»]
4A9IX-ray2.25A/B/C67-200[»]
4A9JX-ray1.90A/B/C67-200[»]
4A9MX-ray2.06A/B/C67-200[»]
4A9NX-ray1.85A/B/C67-200[»]
4A9OX-ray1.78A/B/C67-200[»]
4AKNX-ray1.82A/B/C67-200[»]
4ALGX-ray1.60A67-200[»]
4ALHX-ray1.78A/B/C67-200[»]
4J1PX-ray1.08A344-455[»]
4MR5X-ray1.63A344-455[»]
4MR6X-ray1.67A344-455[»]
4QEUX-ray1.50A344-455[»]
4QEVX-ray1.80A344-455[»]
4QEWX-ray1.70A344-455[»]
4UYFX-ray1.60A/B/C67-200[»]
4UYGX-ray2.50A/B/C/D/E/F338-473[»]
4UYHX-ray1.73A/B/C67-200[»]
5BT5X-ray1.40A344-455[»]
5DFBX-ray1.40A344-455[»]
5DFCX-ray1.50A344-455[»]
5DFDX-ray1.50A344-455[»]
5HELX-ray1.45A71-194[»]
5HEMX-ray1.65A/B71-194[»]
5HENX-ray1.79A/B/C71-194[»]
5HFQX-ray1.40A344-455[»]
ProteinModelPortaliP25440.
SMRiP25440. Positions 72-189, 344-455, 637-714.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25440.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini91 – 16373Bromo 1PROSITE-ProRule annotationAdd
BLAST
Domaini364 – 43673Bromo 2PROSITE-ProRule annotationAdd
BLAST
Domaini632 – 71483NETPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi555 – 5595Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi61 – 644Poly-Pro
Compositional biasi476 – 51540Glu/Ser-richAdd
BLAST
Compositional biasi492 – 50615Poly-GluAdd
BLAST
Compositional biasi544 – 56623Arg/Lys-rich (highly basic)Add
BLAST
Compositional biasi551 – 5599Poly-Lys
Compositional biasi634 – 6385Poly-Glu
Compositional biasi775 – 80127Ser-richAdd
BLAST
Compositional biasi775 – 79319Poly-SerAdd
BLAST

Domaini

One bromodomain is sufficient for a partial interaction with histone H4 acetylated at 'Lys-13'.

Sequence similaritiesi

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

Keywords - Domaini

Bromodomain, Repeat

Phylogenomic databases

eggNOGiKOG1474. Eukaryota.
COG5076. LUCA.
GeneTreeiENSGT00760000119206.
HOGENOMiHOG000231200.
HOVERGENiHBG004896.
InParanoidiP25440.
KOiK08871.
OMAiTESSVAQ.
PhylomeDBiP25440.
TreeFamiTF317345.

Family and domain databases

Gene3Di1.20.920.10. 3 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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P25440-1) [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
MLQNVTPHNK LPGEGNAGLL GLGPEAAAPG KRIRKPSLLY EGFESPTMAS
60 70 80 90 100
VPALQLTPAN PPPPEVSNPK KPGRVTNQLQ YLHKVVMKAL WKHQFAWPFR
110 120 130 140 150
QPVDAVKLGL PDYHKIIKQP MDMGTIKRRL ENNYYWAASE CMQDFNTMFT
160 170 180 190 200
NCYIYNKPTD DIVLMAQTLE KIFLQKVASM PQEEQELVVT IPKNSHKKGA
210 220 230 240 250
KLAALQGSVT SAHQVPAVSS VSHTALYTPP PEIPTTVLNI PHPSVISSPL
260 270 280 290 300
LKSLHSAGPP LLAVTAAPPA QPLAKKKGVK RKADTTTPTP TAILAPGSPA
310 320 330 340 350
SPPGSLEPKA ARLPPMRRES GRPIKPPRKD LPDSQQQHQS SKKGKLSEQL
360 370 380 390 400
KHCNGILKEL LSKKHAAYAW PFYKPVDASA LGLHDYHDII KHPMDLSTVK
410 420 430 440 450
RKMENRDYRD AQEFAADVRL MFSNCYKYNP PDHDVVAMAR KLQDVFEFRY
460 470 480 490 500
AKMPDEPLEP GPLPVSTAMP PGLAKSSSES SSEESSSESS SEEEEEEDEE
510 520 530 540 550
DEEEEESESS DSEEERAHRL AELQEQLRAV HEQLAALSQG PISKPKRKRE
560 570 580 590 600
KKEKKKKRKA EKHRGRAGAD EDDKGPRAPR PPQPKKSKKA SGSGGGSAAL
610 620 630 640 650
GPSGFGPSGG SGTKLPKKAT KTAPPALPTG YDSEEEEESR PMSYDEKRQL
660 670 680 690 700
SLDINKLPGE KLGRVVHIIQ AREPSLRDSN PEEIEIDFET LKPSTLRELE
710 720 730 740 750
RYVLSCLRKK PRKPYTIKKP VGKTKEELAL EKKRELEKRL QDVSGQLNST
760 770 780 790 800
KKPPKKANEK TESSSAQQVA VSRLSASSSS SDSSSSSSSS SSSDTSDSDS

G
Length:801
Mass (Da):88,061
Last modified:January 11, 2001 - v2
Checksum:i9A075EEB13507D8E
GO
Isoform 2 (identifier: P25440-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     615-615: L → LQAGVQWRDLGLLQPPLLGFKRFSCLSLPSSQDYRL

Note: No experimental confirmation available.
Show »
Length:836
Mass (Da):92,033
Checksum:i9064FEB42F773B84
GO
Isoform 3 (identifier: P25440-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-47: Missing.

Show »
Length:754
Mass (Da):83,151
Checksum:i2DC450BD2727B979
GO
Isoform 4 (identifier: P25440-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-120: Missing.

Show »
Length:681
Mass (Da):74,881
Checksum:i22CE98AEC0994F92
GO

Sequence cautioni

The sequence AAA68890.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti490 – 4901S → F in CAH56179 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti30 – 301G → E in a glioblastoma multiforme sample; somatic mutation. 1 Publication
VAR_041904
Natural varianti49 – 491A → G.1 Publication
Corresponds to variant rs115232156 [ dbSNP | Ensembl ].
VAR_041905
Natural varianti49 – 491A → S.1 Publication
Corresponds to variant rs55669504 [ dbSNP | Ensembl ].
VAR_041906
Natural varianti212 – 2121A → P.1 Publication
Corresponds to variant rs35952031 [ dbSNP | Ensembl ].
VAR_041907
Natural varianti238 – 2381L → F.2 Publications
Corresponds to variant rs176250 [ dbSNP | Ensembl ].
VAR_022132
Natural varianti260 – 2601P → Q.1 Publication
Corresponds to variant rs35294809 [ dbSNP | Ensembl ].
VAR_041908
Natural varianti474 – 4741A → V.1 Publication
Corresponds to variant rs3918143 [ dbSNP | Ensembl ].
VAR_029300
Natural varianti547 – 5471R → K.
Corresponds to variant rs1049369 [ dbSNP | Ensembl ].
VAR_029301
Natural varianti558 – 5581R → G in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041909
Natural varianti569 – 5691A → T.1 Publication
Corresponds to variant rs34530779 [ dbSNP | Ensembl ].
VAR_041910
Natural varianti599 – 5991A → P.1 Publication
Corresponds to variant rs55952113 [ dbSNP | Ensembl ].
VAR_041911
Natural varianti714 – 7141P → L in a glioblastoma multiforme sample; somatic mutation. 1 Publication
VAR_041912

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 120120Missing in isoform 4. 1 PublicationVSP_055028Add
BLAST
Alternative sequencei1 – 4747Missing in isoform 3. 1 PublicationVSP_055029Add
BLAST
Alternative sequencei615 – 6151L → LQAGVQWRDLGLLQPPLLGF KRFSCLSLPSSQDYRL in isoform 2. 1 PublicationVSP_022600

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62083 mRNA. Translation: CAA43996.1.
M80613 mRNA. Translation: AAA68890.1. Different initiation.
X96670 Genomic DNA. Translation: CAA65450.1.
Z96104 Genomic DNA. Translation: CAC69989.1.
D42040 mRNA. Translation: BAA07641.1.
BX647233 mRNA. Translation: CAH56179.1.
BX648109 mRNA. Translation: CAH56171.1.
AL832722 mRNA. Translation: CAH56208.1.
AL645941 Genomic DNA. No translation available.
AL662845 Genomic DNA. No translation available.
AL805913 Genomic DNA. No translation available.
BX005422 Genomic DNA. No translation available.
BX908719 Genomic DNA. No translation available.
CR936909 Genomic DNA. No translation available.
AL935042 Genomic DNA. No translation available.
CH471081 Genomic DNA. Translation: EAX03662.1.
CH471081 Genomic DNA. Translation: EAX03663.1.
BC063840 mRNA. Translation: AAH63840.1.
CCDSiCCDS4762.1. [P25440-1]
CCDS56420.1. [P25440-2]
CCDS56421.1. [P25440-3]
PIRiA56619.
RefSeqiNP_001106653.1. NM_001113182.2. [P25440-1]
NP_001186384.1. NM_001199455.1. [P25440-2]
NP_001186385.1. NM_001199456.1. [P25440-3]
NP_001278915.1. NM_001291986.1. [P25440-4]
NP_005095.1. NM_005104.3. [P25440-1]
UniGeneiHs.75243.

Genome annotation databases

EnsembliENST00000374825; ENSP00000363958; ENSG00000204256. [P25440-1]
ENST00000374831; ENSP00000363964; ENSG00000204256. [P25440-1]
ENST00000383108; ENSP00000372588; ENSG00000234507. [P25440-1]
ENST00000395287; ENSP00000378702; ENSG00000204256. [P25440-2]
ENST00000399527; ENSP00000382443; ENSG00000215077. [P25440-2]
ENST00000399528; ENSP00000382444; ENSG00000215077. [P25440-1]
ENST00000399529; ENSP00000382445; ENSG00000215077. [P25440-1]
ENST00000414731; ENSP00000391246; ENSG00000234704.
ENST00000436979; ENSP00000405634; ENSG00000235307. [P25440-3]
ENST00000438194; ENSP00000401791; ENSG00000234507. [P25440-1]
ENST00000442863; ENSP00000410994; ENSG00000234507. [P25440-2]
ENST00000448067; ENSP00000412885; ENSG00000235307. [P25440-2]
ENST00000449085; ENSP00000409145; ENSG00000204256. [P25440-3]
ENST00000449118; ENSP00000399009; ENSG00000234704.
ENST00000549126; ENSP00000449380; ENSG00000235307. [P25440-1]
ENST00000552587; ENSP00000449609; ENSG00000235307. [P25440-1]
GeneIDi6046.
KEGGihsa:6046.
UCSCiuc003ocn.4. human. [P25440-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62083 mRNA. Translation: CAA43996.1.
M80613 mRNA. Translation: AAA68890.1. Different initiation.
X96670 Genomic DNA. Translation: CAA65450.1.
Z96104 Genomic DNA. Translation: CAC69989.1.
D42040 mRNA. Translation: BAA07641.1.
BX647233 mRNA. Translation: CAH56179.1.
BX648109 mRNA. Translation: CAH56171.1.
AL832722 mRNA. Translation: CAH56208.1.
AL645941 Genomic DNA. No translation available.
AL662845 Genomic DNA. No translation available.
AL805913 Genomic DNA. No translation available.
BX005422 Genomic DNA. No translation available.
BX908719 Genomic DNA. No translation available.
CR936909 Genomic DNA. No translation available.
AL935042 Genomic DNA. No translation available.
CH471081 Genomic DNA. Translation: EAX03662.1.
CH471081 Genomic DNA. Translation: EAX03663.1.
BC063840 mRNA. Translation: AAH63840.1.
CCDSiCCDS4762.1. [P25440-1]
CCDS56420.1. [P25440-2]
CCDS56421.1. [P25440-3]
PIRiA56619.
RefSeqiNP_001106653.1. NM_001113182.2. [P25440-1]
NP_001186384.1. NM_001199455.1. [P25440-2]
NP_001186385.1. NM_001199456.1. [P25440-3]
NP_001278915.1. NM_001291986.1. [P25440-4]
NP_005095.1. NM_005104.3. [P25440-1]
UniGeneiHs.75243.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X0JX-ray1.80A/B/C73-194[»]
2DVQX-ray2.04A/B/C73-194[»]
2DVRX-ray2.30A/B/C73-194[»]
2DVSX-ray2.04A/B/C73-194[»]
2DVVX-ray1.80A348-455[»]
2E3KX-ray2.30A/B/C/D348-455[»]
2G4ANMR-A348-455[»]
2YDWX-ray1.90A/B/C67-200[»]
2YEKX-ray1.98A/B/C67-200[»]
3AQAX-ray2.30A/B/C73-194[»]
3ONIX-ray1.61A344-455[»]
4A9EX-ray1.91A/B/C67-200[»]
4A9FX-ray1.73A/B/C67-200[»]
4A9HX-ray2.05A/B/C67-200[»]
4A9IX-ray2.25A/B/C67-200[»]
4A9JX-ray1.90A/B/C67-200[»]
4A9MX-ray2.06A/B/C67-200[»]
4A9NX-ray1.85A/B/C67-200[»]
4A9OX-ray1.78A/B/C67-200[»]
4AKNX-ray1.82A/B/C67-200[»]
4ALGX-ray1.60A67-200[»]
4ALHX-ray1.78A/B/C67-200[»]
4J1PX-ray1.08A344-455[»]
4MR5X-ray1.63A344-455[»]
4MR6X-ray1.67A344-455[»]
4QEUX-ray1.50A344-455[»]
4QEVX-ray1.80A344-455[»]
4QEWX-ray1.70A344-455[»]
4UYFX-ray1.60A/B/C67-200[»]
4UYGX-ray2.50A/B/C/D/E/F338-473[»]
4UYHX-ray1.73A/B/C67-200[»]
5BT5X-ray1.40A344-455[»]
5DFBX-ray1.40A344-455[»]
5DFCX-ray1.50A344-455[»]
5DFDX-ray1.50A344-455[»]
5HELX-ray1.45A71-194[»]
5HEMX-ray1.65A/B71-194[»]
5HENX-ray1.79A/B/C71-194[»]
5HFQX-ray1.40A344-455[»]
ProteinModelPortaliP25440.
SMRiP25440. Positions 72-189, 344-455, 637-714.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111973. 36 interactions.
DIPiDIP-60835N.
IntActiP25440. 19 interactions.
MINTiMINT-4530155.
STRINGi9606.ENSP00000378702.

Chemistry

ChEMBLiCHEMBL1293289.
GuidetoPHARMACOLOGYi1944.

PTM databases

iPTMnetiP25440.
PhosphoSiteiP25440.

Polymorphism and mutation databases

BioMutaiBRD2.
DMDMi12230989.

Proteomic databases

EPDiP25440.
MaxQBiP25440.
PaxDbiP25440.
PRIDEiP25440.

Protocols and materials databases

DNASUi6046.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374825; ENSP00000363958; ENSG00000204256. [P25440-1]
ENST00000374831; ENSP00000363964; ENSG00000204256. [P25440-1]
ENST00000383108; ENSP00000372588; ENSG00000234507. [P25440-1]
ENST00000395287; ENSP00000378702; ENSG00000204256. [P25440-2]
ENST00000399527; ENSP00000382443; ENSG00000215077. [P25440-2]
ENST00000399528; ENSP00000382444; ENSG00000215077. [P25440-1]
ENST00000399529; ENSP00000382445; ENSG00000215077. [P25440-1]
ENST00000414731; ENSP00000391246; ENSG00000234704.
ENST00000436979; ENSP00000405634; ENSG00000235307. [P25440-3]
ENST00000438194; ENSP00000401791; ENSG00000234507. [P25440-1]
ENST00000442863; ENSP00000410994; ENSG00000234507. [P25440-2]
ENST00000448067; ENSP00000412885; ENSG00000235307. [P25440-2]
ENST00000449085; ENSP00000409145; ENSG00000204256. [P25440-3]
ENST00000449118; ENSP00000399009; ENSG00000234704.
ENST00000549126; ENSP00000449380; ENSG00000235307. [P25440-1]
ENST00000552587; ENSP00000449609; ENSG00000235307. [P25440-1]
GeneIDi6046.
KEGGihsa:6046.
UCSCiuc003ocn.4. human. [P25440-1]

Organism-specific databases

CTDi6046.
GeneCardsiBRD2.
HGNCiHGNC:1103. BRD2.
HPAiHPA042816.
HPA054746.
MIMi601540. gene.
neXtProtiNX_P25440.
PharmGKBiPA25414.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1474. Eukaryota.
COG5076. LUCA.
GeneTreeiENSGT00760000119206.
HOGENOMiHOG000231200.
HOVERGENiHBG004896.
InParanoidiP25440.
KOiK08871.
OMAiTESSVAQ.
PhylomeDBiP25440.
TreeFamiTF317345.

Miscellaneous databases

ChiTaRSiBRD2. human.
EvolutionaryTraceiP25440.
GeneWikiiBRD2.
GenomeRNAii6046.
NextBioi23557.
PROiP25440.
SOURCEiSearch...

Gene expression databases

BgeeiP25440.
CleanExiHS_BRD2.
ExpressionAtlasiP25440. baseline and differential.
GenevisibleiP25440. HS.

Family and domain databases

Gene3Di1.20.920.10. 3 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. "A homologue of the Drosophila female sterile homeotic (fsh) gene in the class II region of the human MHC."
    Beck S., Hanson I., Kelly A., Pappin D.J.C., Trowsdale J.
    DNA Seq. 2:203-210(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: T-cell.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION TO N-TERMINUS.
  3. Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki T., Ishikawa K., Tabata S.
    Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
    Tissue: Bone marrow and Testis.
  5. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PHE-238.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: PNS.
  8. "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.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; SER-301; SER-305 AND SER-633, 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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-298 AND SER-301, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6; SER-298 AND SER-301, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; SER-301 AND SER-305, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "Crystal structure of the human BRD2 bromodomain: insights into dimerization and recognition of acetylated histone h4."
    Nakamura Y., Umehara T., Nakano K., Jang M.K., Shirouzu M., Morita S., Uda-Tochio H., Hamana H., Terada T., Adachi N., Matsumoto T., Tanaka A., Horikoshi M., Ozato K., Padmanabhan B., Yokoyama S.
    J. Biol. Chem. 282:4193-4201(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 73-194, HOMODIMERIZATION, INTERACTION WITH E2F1 AND HISTONE H4, MUTAGENESIS OF GLN-78; 142-MET-GLN-143; TYR-153; ILE-154; GLU-170; LEU-174; VAL-177 AND GLN-182.
  17. Cited for: X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) OF 344-452.
  18. "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] GLU-30; GLY-49; SER-49; PRO-212; PHE-238; GLN-260; VAL-474; GLY-558; THR-569; PRO-599 AND LEU-714.

Entry informationi

Entry nameiBRD2_HUMAN
AccessioniPrimary (citable) accession number: P25440
Secondary accession number(s): A2AAU0
, B0S7P0, B1AZT1, O00699, O00700, Q15310, Q5STC9, Q63HQ9, Q658Y7, Q6P3U2, Q969U4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 11, 2001
Last modified: May 11, 2016
This is version 162 of the entry and version 2 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 6
    Human chromosome 6: 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

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.