P25440 (BRD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bromodomain-containing protein 2

Alternative name(s):
O27.1.1
Really interesting new gene 3 protein

Gene names

Name:	BRD2
Synonyms:	KIAA9001, RING3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	801 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role in spermatogenesis or folliculogenesis By similarity.
Subunit structure	Homodimer. Interacts with E2F1 and with histone H4 acetylated at 'Lys-13'. Ref.15
Subcellular location	Nucleus By similarity.
Domain	One bromodomain is sufficient for a partial interaction with histone H4 acetylated at 'Lys-13'.
Sequence similarities	Contains 2 bromo domains. Contains 1 ET domain.
Sequence caution	The sequence AAA68890.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Bromodomain Repeat
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	spermatogenesis Traceable author statement. Source: ProtInc
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein serine/threonine kinase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P25440-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P25440-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 801

801

Bromodomain-containing protein 2

PRO_0000211180

Regions

Domain

91 – 163

73

Bromo 1

Domain

364 – 436

73

Bromo 2

Domain

638 – 801

164

ET

Motif

555 – 559

5

Nuclear localization signal Potential

Compositional bias

61 – 64

4

Poly-Pro

Compositional bias

476 – 515

40

Glu/Ser-rich

Compositional bias

492 – 506

15

Poly-Glu

Compositional bias

544 – 566

23

Arg/Lys-rich (highly basic)

Compositional bias

551 – 559

9

Poly-Lys

Compositional bias

634 – 638

5

Poly-Glu

Compositional bias

775 – 801

27

Ser-rich

Compositional bias

775 – 793

19

Poly-Ser

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.12

Modified residue

37

1

Phosphoserine Ref.13

Modified residue

298

1

Phosphoserine Ref.8 Ref.11 Ref.12 Ref.13

Modified residue

301

1

Phosphoserine Ref.8 Ref.11 Ref.12 Ref.13

Modified residue

305

1

Phosphoserine Ref.11

Modified residue

320

1

Phosphoserine Ref.10

Modified residue

633

1

Phosphoserine Ref.11

Modified residue

724

1

Phosphothreonine Ref.9

Natural variations

Alternative sequence

615

1

L → LQAGVQWRDLGLLQPPLLGF KRFSCLSLPSSQDYRL in isoform 2.

VSP_022600

Natural variant

30

1

G → E in a glioblastoma multiforme sample; somatic mutation. Ref.17

VAR_041904

Natural variant

49

1

A → G. Ref.17

VAR_041905

Natural variant

49

1

A → S. Ref.17
Corresponds to variant rs55669504 [ dbSNP | Ensembl ].

VAR_041906

Natural variant

212

1

A → P. Ref.17
Corresponds to variant rs35952031 [ dbSNP | Ensembl ].

VAR_041907

Natural variant

238

1

L → F. Ref.5 Ref.17
Corresponds to variant rs176250 [ dbSNP | Ensembl ].

VAR_022132

Natural variant

260

1

P → Q. Ref.17
Corresponds to variant rs35294809 [ dbSNP | Ensembl ].

VAR_041908

Natural variant

474

1

A → V. Ref.17
Corresponds to variant rs3918143 [ dbSNP | Ensembl ].

VAR_029300

Natural variant

547

1

R → K.
Corresponds to variant rs1049369 [ dbSNP | Ensembl ].

VAR_029301

Natural variant

558

1

R → G in a gastric adenocarcinoma sample; somatic mutation. Ref.17

VAR_041909

Natural variant

569

1

A → T. Ref.17
Corresponds to variant rs34530779 [ dbSNP | Ensembl ].

VAR_041910

Natural variant

599

1

A → P. Ref.17
Corresponds to variant rs55952113 [ dbSNP | Ensembl ].

VAR_041911

Natural variant

714

1

P → L in a glioblastoma multiforme sample; somatic mutation. Ref.17

VAR_041912

Experimental info

Mutagenesis

78

1

Q → A: Loss of homodimerization. Ref.15

Mutagenesis

142 – 143

2

MQ → AA: Loss of homodimerization.

Mutagenesis

153

1

Y → K: Loss of homodimerization. Ref.15

Mutagenesis

154

1

I → A: Partial loss of homodimerization; when associated with A-182. Ref.15

Mutagenesis

170

1

E → A: Loss of homodimerization. Ref.15

Mutagenesis

174

1

L → E: Loss of homodimerization. Ref.15

Mutagenesis

177

1

V → E: Loss of homodimerization. Ref.15

Mutagenesis

182

1

Q → A: Partial loss of homodimerization; when associated with A-154. Ref.15

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

801

Helix Strand Turn

Details...

Helix

77 – 84

8

Helix

86 – 92

7

Helix

97 – 99

3

Helix

105 – 108

4

Helix

113 – 116

4

Helix

123 – 131

9

Helix

138 – 155

18

Helix

161 – 177

17

Helix

349 – 362

14

Helix

366 – 373

8

Helix

378 – 382

5

Helix

384 – 389

6

Helix

396 – 405

10

Turn

406 – 408

3

Helix

411 – 428

18

Helix

434 – 452

19

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 11, 2001. Version 2. Checksum: 9A075EEB13507D8E	FASTA	801	88,061
	10 20 30 40 50 60 MLQNVTPHNK LPGEGNAGLL GLGPEAAAPG KRIRKPSLLY EGFESPTMAS VPALQLTPAN 70 80 90 100 110 120 PPPPEVSNPK KPGRVTNQLQ YLHKVVMKAL WKHQFAWPFR QPVDAVKLGL PDYHKIIKQP 130 140 150 160 170 180 MDMGTIKRRL ENNYYWAASE CMQDFNTMFT NCYIYNKPTD DIVLMAQTLE KIFLQKVASM 190 200 210 220 230 240 PQEEQELVVT IPKNSHKKGA KLAALQGSVT SAHQVPAVSS VSHTALYTPP PEIPTTVLNI 250 260 270 280 290 300 PHPSVISSPL LKSLHSAGPP LLAVTAAPPA QPLAKKKGVK RKADTTTPTP TAILAPGSPA 310 320 330 340 350 360 SPPGSLEPKA ARLPPMRRES GRPIKPPRKD LPDSQQQHQS SKKGKLSEQL KHCNGILKEL 370 380 390 400 410 420 LSKKHAAYAW PFYKPVDASA LGLHDYHDII KHPMDLSTVK RKMENRDYRD AQEFAADVRL 430 440 450 460 470 480 MFSNCYKYNP PDHDVVAMAR KLQDVFEFRY AKMPDEPLEP GPLPVSTAMP PGLAKSSSES 490 500 510 520 530 540 SSEESSSESS SEEEEEEDEE DEEEEESESS DSEEERAHRL AELQEQLRAV HEQLAALSQG 550 560 570 580 590 600 PISKPKRKRE KKEKKKKRKA EKHRGRAGAD EDDKGPRAPR PPQPKKSKKA SGSGGGSAAL 610 620 630 640 650 660 GPSGFGPSGG SGTKLPKKAT KTAPPALPTG YDSEEEEESR PMSYDEKRQL SLDINKLPGE 670 680 690 700 710 720 KLGRVVHIIQ AREPSLRDSN PEEIEIDFET LKPSTLRELE RYVLSCLRKK PRKPYTIKKP 730 740 750 760 770 780 VGKTKEELAL EKKRELEKRL QDVSGQLNST KKPPKKANEK TESSSAQQVA VSRLSASSSS 790 800 SDSSSSSSSS SSSDTSDSDS G
	Isoform 2 [UniParc]. Checksum: 9064FEB42F773B84	FASTA	836	92,033
	10 20 30 40 50 60 MLQNVTPHNK LPGEGNAGLL GLGPEAAAPG KRIRKPSLLY EGFESPTMAS VPALQLTPAN 70 80 90 100 110 120 PPPPEVSNPK KPGRVTNQLQ YLHKVVMKAL WKHQFAWPFR QPVDAVKLGL PDYHKIIKQP 130 140 150 160 170 180 MDMGTIKRRL ENNYYWAASE CMQDFNTMFT NCYIYNKPTD DIVLMAQTLE KIFLQKVASM 190 200 210 220 230 240 PQEEQELVVT IPKNSHKKGA KLAALQGSVT SAHQVPAVSS VSHTALYTPP PEIPTTVLNI 250 260 270 280 290 300 PHPSVISSPL LKSLHSAGPP LLAVTAAPPA QPLAKKKGVK RKADTTTPTP TAILAPGSPA 310 320 330 340 350 360 SPPGSLEPKA ARLPPMRRES GRPIKPPRKD LPDSQQQHQS SKKGKLSEQL KHCNGILKEL 370 380 390 400 410 420 LSKKHAAYAW PFYKPVDASA LGLHDYHDII KHPMDLSTVK RKMENRDYRD AQEFAADVRL 430 440 450 460 470 480 MFSNCYKYNP PDHDVVAMAR KLQDVFEFRY AKMPDEPLEP GPLPVSTAMP PGLAKSSSES 490 500 510 520 530 540 SSEESSSESS SEEEEEEDEE DEEEEESESS DSEEERAHRL AELQEQLRAV HEQLAALSQG 550 560 570 580 590 600 PISKPKRKRE KKEKKKKRKA EKHRGRAGAD EDDKGPRAPR PPQPKKSKKA SGSGGGSAAL 610 620 630 640 650 660 GPSGFGPSGG SGTKLQAGVQ WRDLGLLQPP LLGFKRFSCL SLPSSQDYRL PKKATKTAPP 670 680 690 700 710 720 ALPTGYDSEE EEESRPMSYD EKRQLSLDIN KLPGEKLGRV VHIIQAREPS LRDSNPEEIE 730 740 750 760 770 780 IDFETLKPST LRELERYVLS CLRKKPRKPY TIKKPVGKTK EELALEKKRE LEKRLQDVSG 790 800 810 820 830 QLNSTKKPPK KANEKTESSS AQQVAVSRLS ASSSSSDSSS SSSSSSSSDT SDSDSG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 1352711] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: T-cell.
[2]	"Phylogeny and structure of the RING3 gene." Thorpe K.L., Abdulla S., Kaufman J., Trowsdale J., Beck S. Immunogenetics 44:391-396(1996) [PubMed: 8781126] [Abstract] 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]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: 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: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PHE-238.
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: PNS.
[8]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-301, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-724, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; SER-301; SER-305 AND SER-633, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-301, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-298 AND SER-301, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"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: 17148447] [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.
[16]	"Selective inhibition of BET bromodomains." Filippakopoulos P., Qi J., Picaud S., Shen Y., Smith W.B., Fedorov O., Morse E.M., Keates T., Hickman T.T., Felletar I., Philpott M., Munro S., McKeown M.R., Wang Y., Christie A.L., West N., Cameron M.J., Schwartz B. , Heightman T.D., La Thangue N., French C.A., Wiest O., Kung A.L., Knapp S., Bradner J.E. Nature 468:1067-1073(2010) [PubMed: 20871596] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) OF 344-452.
[17]	"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: 17344846] [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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X62083 mRNA. Translation: CAA43996.1.
M80613 mRNA. Translation: AAA68890.1. Different initiation.
X96670 Genomic DNA. Translation: CAA65450.1.
D42040 mRNA. Translation: BAA07641.1.
BX648109 mRNA. Translation: CAH56171.1.
AL645941 Genomic DNA. Translation: CAI18110.1.
AL662845 Genomic DNA. Translation: CAI17492.1.
AL805913, AL935042 Genomic DNA. Translation: CAI18548.1.
AL935042, AL805913 Genomic DNA. Translation: CAI18689.1.
BX005422 Genomic DNA. Translation: CAM26115.1.
BX908719, CR936909 Genomic DNA. Translation: CAQ09037.1.
CR936909, BX908719 Genomic DNA. Translation: CAQ07147.1.
Z96104 Genomic DNA. Translation: CAC69989.1.
CH471081 Genomic DNA. Translation: EAX03663.1.
BC063840 mRNA. Translation: AAH63840.1.

IPI

IPI00014414.
IPI00440502.

PIR

A56619.

RefSeq

NP_001106653.1. NM_001113182.2.
NP_001186384.1. NM_001199455.1.
NP_001186385.1. NM_001199456.1.
NP_005095.1. NM_005104.3.

UniGene

Hs.75243.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X0J	X-ray	1.80	A/B/C	73-194	[»]
2DVQ	X-ray	2.04	A/B/C	73-194	[»]
2DVR	X-ray	2.30	A/B/C	73-194	[»]
2DVS	X-ray	2.04	A/B/C	73-194	[»]
2DVV	X-ray	1.80	A	348-455	[»]
2E3K	X-ray	2.30	A/B/C/D	348-455	[»]
2G4A	NMR	-	A	348-455	[»]
2YDW	X-ray	1.90	A/B/C	67-192	[»]
2YEK	X-ray	1.98	A/B/C	67-192	[»]
3AQA	X-ray	2.30	A/B/C	73-194	[»]
3ONI	X-ray	1.61	A	344-452	[»]

ProteinModelPortal

P25440.

SMR

P25440. Positions 73-186, 346-455, 637-714.

ModBase

Search...

Protein-protein interaction databases

IntAct

P25440. 1 interaction.

STRING

P25440.

PTM databases

PhosphoSite

P25440.

Polymorphism databases

DMDM

12230989.

Proteomic databases

PRIDE

P25440.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000374825; ENSP00000363958; ENSG00000204256.
ENST00000374831; ENSP00000363964; ENSG00000204256.
ENST00000383108; ENSP00000372588; ENSG00000234507.
ENST00000399528; ENSP00000382444; ENSG00000215077.
ENST00000399529; ENSP00000382445; ENSG00000215077.
ENST00000422217; ENSP00000411714; ENSG00000235307.
ENST00000438194; ENSP00000401791; ENSG00000234507.

GeneID

6046.

KEGG

hsa:6046.

UCSC

uc003ocn.2. human.
uc010juh.1. human.

Organism-specific databases

CTD

6046.

GeneCards

GC06P032983.

HGNC

HGNC:1103. BRD2.

HPA

HPA042816.

MIM

601540. gene.

neXtProt

NX_P25440.

PharmGKB

PA25414.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

HBG004896.

OMA

RPSQPKK.

OrthoDB

EOG4NZTT4.

PhylomeDB

P25440.

Gene expression databases

Bgee

P25440.

CleanEx

HS_BRD2.

Genevestigator

P25440.

GermOnline

ENSG00000204256. Homo sapiens.

Family and domain databases

InterPro

IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
[Graphical view]

Gene3D

G3DSA:1.20.920.10. Bromodomain. 2 hits.

KO

K08871.

Pfam

PF00439. Bromodomain. 2 hits.
[Graphical view]

PRINTS

PR00503. BROMODOMAIN.

SMART

SM00297. BROMO. 2 hits.
[Graphical view]

SUPFAM

SSF47370. Bromodomain. 2 hits.

PROSITE

PS00633. BROMODOMAIN_1. 2 hits.
PS50014. BROMODOMAIN_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

23557.

SOURCE

Search...

Entry information

Entry name

BRD2_HUMAN

Accession

Primary (citable) accession number: P25440
Secondary accession number(s): B0S7P0 , B1AZT1, O00699, O00700, Q15310, Q5STC9, Q6P3U2, Q969U4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	January 11, 2001
Last modified:	January 25, 2012
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.