Q9NPI1 (BRD7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bromodomain-containing protein 7

Alternative name(s):
75 kDa bromodomain protein
Protein CELTIX-1

Gene names

Name:	BRD7
Synonyms:	BP75, CELTIX1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	651 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts both as coactivator and as corepressor. May play a role in chromatin remodeling. Activator of the Wnt signaling pathway in a DVL1-dependent manner by negatively regulating the GSK3B phosphotransferase activity. Induces dephosphorylation of GSK3B at 'Tyr-216'. Down-regulates TRIM24-mediated activation of transcriptional activation by AR By similarity. Transcriptional corepressor that down-regulates the expression of target genes. Binds to target promoters, leading to increased histone H3 acetylation at 'Lys-9' (H3K9ac). Binds to the ESR1 promoter. Recruits BRCA1 and POU2F1 to the ESR1 promoter. Coactivator for TP53-mediated activation of transcription of a set of target genes. Required for TP53-mediated cell-cycle arrest in response to oncogene activation. Promotes acetylation of TP53 at 'Lys-382', and thereby promotes efficient recruitment of TP53 to target promoters. Inhibits cell cycle progression from G1 to S phase. Ref.8 Ref.9 Ref.11 Ref.12 Ref.13
Subunit structure	Interacts with TRIM24, PTPN13 and DVL1. Identified in a complex with SMARCA4/BRG1, SMARCC1/BAF155, SMARCE1/BAF57, DPF2/BAF45D and ARID2, subunits of the SWI/SNF-B (PBAF) chromatin remodeling complex By similarity. Interacts with IRF2 and HNRPUL1. Interacts (via N-terminus) with TP53. Interacts (via C-terminus) with EP300. Interacts with BRCA1. Interacts (via bromo domain) with histone H3 (via N-terminus) acetylated at 'Lys-14' (H3K14ac). Has low affinity for histone H3 acetylated at 'Lys-9' (H3K9ac). Has the highest affinity for histone H3 that is acetylated both at 'Lys-9' (H3K9ac) and at 'Lys-14' (H3K14ac). Has very low affinity for non-acetylated histone H3. Interacts (via bromo domain) with histone H4 (via N-terminus) acetylated at 'Lys-8' (H3K8ac) (in vitro). Ref.1 Ref.2 Ref.8 Ref.11 Ref.12 Ref.13 Ref.16
Subcellular location	Isoform 2: Nucleus Ref.1 Ref.8 Ref.9 Ref.12.
Sequence similarities	Contains 1 bromo domain.
Sequence caution	The sequence AAH01611.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAB55031.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAC11089.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Cell cycle Transcription Transcription regulation Wnt signaling pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Disease	Tumor suppressor
Domain	Bromodomain Coiled coil
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW cell cycle Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of G1/S transition of mitotic cell cycle Inferred from direct assay Ref.8. Source: UniProtKB negative regulation of cell proliferation Inferred from direct assay Ref.12. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from direct assay Ref.8. Source: UniProtKB positive regulation of histone acetylation Inferred from direct assay Ref.12. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.12. Source: UniProtKB regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.2. Source: MGI transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Traceable author statement PubMed 10526152. Source: ProtInc nucleus Inferred from direct assay Ref.8Ref.12. Source: UniProtKB
Molecular_function	histone acetyl-lysine binding Inferred from direct assay Ref.8. Source: UniProtKB transcription coactivator activity Inferred from direct assay Ref.12. Source: UniProtKB transcription corepressor activity Inferred from direct assay Ref.8. Source: UniProtKB transcription factor binding Inferred from direct assay Ref.1. Source: MGI transcription regulatory region DNA binding Inferred from direct assay Ref.12. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EP300	Q09472	3	EBI-711221,EBI-447295
TP53	P04637	8	EBI-711221,EBI-366083

Alternative products

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

Isoform 1 (identifier: Q9NPI1-1)

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: Q9NPI1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     500-500: E → EQ

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 651

651

Bromodomain-containing protein 7

PRO_0000227664

Regions

Domain

148 – 218

71

Bromo

Coiled coil

536 – 567

32

Potential

Motif

65 – 96

32

Nuclear localization signal Ref.9

Compositional bias

3 – 91

89

Lys-rich

Amino acid modifications

Modified residue

279

1

Phosphoserine Ref.7 Ref.14 Ref.15

Natural variations

Alternative sequence

500

1

E → EQ in isoform 2.

VSP_017564

Experimental info

Sequence conflict

66

1

R → G in AAF19526. Ref.1

Sequence conflict

83

1

R → T in AAF19526. Ref.1

Sequence conflict

96

1

R → Q in AAF19526. Ref.1

Sequence conflict

170

1

M → I in AAH94706. Ref.5

Sequence conflict

485

1

E → G in BAB55031. Ref.6

Secondary structure

1

.

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.

.

.

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.

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.

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651

Helix Strand Turn

Details...

Helix

133 – 148

16

Helix

152 – 154

3

Beta strand

156 – 158

3

Turn

162 – 164

3

Beta strand

165 – 167

3

Helix

168 – 171

4

Helix

178 – 185

8

Turn

186 – 188

3

Helix

193 – 209

17

Beta strand

213 – 216

4

Helix

217 – 235

19

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 29B7947644C215E7	FASTA	651	74,139
	10 20 30 40 50 60 MGKKHKKHKS DKHLYEEYVE KPLKLVLKVG GNEVTELSTG SSGHDSSLFE DKNDHDKHKD 70 80 90 100 110 120 RKRKKRKKGE KQIPGEEKGR KRRRVKEDKK KRDRDRVENE AEKDLQCHAP VRLDLPPEKP 130 140 150 160 170 180 LTSSLAKQEE VEQTPLQEAL NQLMRQLQRK DPSAFFSFPV TDFIAPGYSM IIKHPMDFST 190 200 210 220 230 240 MKEKIKNNDY QSIEELKDNF KLMCTNAMIY NKPETIYYKA AKKLLHSGMK ILSQERIQSL 250 260 270 280 290 300 KQSIDFMADL QKTRKQKDGT DTSQSGEDGG CWQREREDSG DAEAHAFKSP SKENKKKDKD 310 320 330 340 350 360 MLEDKFKSNN LEREQEQLDR IVKESGGKLT RRLVNSQCEF ERRKPDGTTT LGLLHPVDPI 370 380 390 400 410 420 VGEPGYCPVR LGMTTGRLQS GVNTLQGFKE DKRNKVTPVL YLNYGPYSSY APHYDSTFAN 430 440 450 460 470 480 ISKDDSDLIY STYGEDSDLP SDFSIHEFLA TCQDYPYVMA DSLLDVLTKG GHSRTLQEME 490 500 510 520 530 540 MSLPEDEGHT RTLDTAKEME ITEVEPPGRL DSSTQDRLIA LKAVTNFGVP VEVFDSEEAE 550 560 570 580 590 600 IFQKKLDETT RLLRELQEAQ NERLSTRPPP NMICLLGPSY REMHLAEQVT NNLKELAQQV 610 620 630 640 650 TPGDIVSTYG VRKAMGISIP SPVMENNFVD LTEDTEEPKK TDVAECGPGG S
	Isoform 2 [UniParc]. Checksum: AE7A8BB828D0B538	FASTA	652	74,267
	10 20 30 40 50 60 MGKKHKKHKS DKHLYEEYVE KPLKLVLKVG GNEVTELSTG SSGHDSSLFE DKNDHDKHKD 70 80 90 100 110 120 RKRKKRKKGE KQIPGEEKGR KRRRVKEDKK KRDRDRVENE AEKDLQCHAP VRLDLPPEKP 130 140 150 160 170 180 LTSSLAKQEE VEQTPLQEAL NQLMRQLQRK DPSAFFSFPV TDFIAPGYSM IIKHPMDFST 190 200 210 220 230 240 MKEKIKNNDY QSIEELKDNF KLMCTNAMIY NKPETIYYKA AKKLLHSGMK ILSQERIQSL 250 260 270 280 290 300 KQSIDFMADL QKTRKQKDGT DTSQSGEDGG CWQREREDSG DAEAHAFKSP SKENKKKDKD 310 320 330 340 350 360 MLEDKFKSNN LEREQEQLDR IVKESGGKLT RRLVNSQCEF ERRKPDGTTT LGLLHPVDPI 370 380 390 400 410 420 VGEPGYCPVR LGMTTGRLQS GVNTLQGFKE DKRNKVTPVL YLNYGPYSSY APHYDSTFAN 430 440 450 460 470 480 ISKDDSDLIY STYGEDSDLP SDFSIHEFLA TCQDYPYVMA DSLLDVLTKG GHSRTLQEME 490 500 510 520 530 540 MSLPEDEGHT RTLDTAKEME QITEVEPPGR LDSSTQDRLI ALKAVTNFGV PVEVFDSEEA 550 560 570 580 590 600 EIFQKKLDET TRLLRELQEA QNERLSTRPP PNMICLLGPS YREMHLAEQV TNNLKELAQQ 610 620 630 640 650 VTPGDIVSTY GVRKAMGISI PSPVMENNFV DLTEDTEEPK KTDVAECGPG GS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of celtix-1, a bromodomain protein interacting with the transcription factor interferon regulatory factor 2." Staal A., Enserink J.M., Stein J.L., Stein G.S., van Wijnen A.J. J. Cell. Physiol. 185:269-279(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH IRF2, SUBCELLULAR LOCATION. Tissue: Cervix carcinoma.
[2]	"Regulation of transcription by the heterogeneous nuclear ribonucleoprotein E1B-AP5 is mediated by complex formation with the novel bromodomain-containing protein BRD7." Kzhyshkowska J.G., Rusch A., Wolf H., Dobner T. Biochem. J. 371:385-393(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH HNRPUL1, ASSOCIATION WITH HISTONES AND HNRPUL1. Tissue: Fetal brain.
[3]	Yu Y., Li G.Y. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] 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 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 198-651 (ISOFORM 2). Tissue: Brain and Skin.
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 236-651 (ISOFORM 1). Tissue: Embryo.
[7]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"The transcriptional regulation role of BRD7 by binding to acetylated histone through bromodomain." Peng C., Zhou J., Liu H.Y., Zhou M., Wang L.L., Zhang Q.H., Yang Y.X., Xiong W., Shen S.R., Li X.L., Li G.Y. J. Cell. Biochem. 97:882-892(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ACETYLATED HISTONE H3.
[9]	"Identification of nuclear localization signal that governs nuclear import of BRD7 and its essential roles in inhibiting cell cycle progression." Zhou M., Liu H., Xu X., Zhou H., Li X., Peng C., Shen S., Xiong W., Ma J., Zeng Z., Fang S., Nie X., Yang Y., Zhou J., Xiang J., Cao L., Peng S., Li S., Li G. J. Cell. Biochem. 98:920-930(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION.
[10]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: T-cell.
[11]	"BRD7, a subunit of SWI/SNF complexes, binds directly to BRCA1 and regulates BRCA1-dependent transcription." Harte M.T., O'Brien G.J., Ryan N.M., Gorski J.J., Savage K.I., Crawford N.T., Mullan P.B., Harkin D.P. Cancer Res. 70:2538-2547(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PROMOTER BINDING, INTERACTION WITH BRCA1.
[12]	"BRD7 is a candidate tumour suppressor gene required for p53 function." Drost J., Mantovani F., Tocco F., Elkon R., Comel A., Holstege H., Kerkhoven R., Jonkers J., Voorhoeve P.M., Agami R., Del Sal G. Nat. Cell Biol. 12:380-389(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TP53 AND EP300.
[13]	"Polybromo-associated BRG1-associated factor components BRD7 and BAF180 are critical regulators of p53 required for induction of replicative senescence." Burrows A.E., Smogorzewska A., Elledge S.J. Proc. Natl. Acad. Sci. U.S.A. 107:14280-14285(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TP53.
[14]	"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-279, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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-279, MASS SPECTROMETRY.
[16]	"Solution structure of BRD7 bromodomain and its interaction with acetylated peptides from histone H3 and H4." Sun H., Liu J., Zhang J., Shen W., Huang H., Xu C., Dai H., Wu J., Shi Y. Biochem. Biophys. Res. Commun. 358:435-441(2007) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 129-236, INTERACTION WITH ACETYLATED HISTONE PEPTIDES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF213969 mRNA. Translation: AAF19526.1.
AJ271881 mRNA. Translation: CAB72445.1.
AF152604 mRNA. Translation: AAF75126.1.
BC001611 mRNA. Translation: AAH01611.1. Different initiation.
AC007493 Genomic DNA. No translation available.
AC007597 Genomic DNA. No translation available.
AC023826 Genomic DNA. No translation available.
BC050728 mRNA. Translation: AAH50728.1.
BC094706 mRNA. Translation: AAH94706.1.
AK027308 mRNA. Translation: BAB55031.1. Different initiation.
AK074613 mRNA. Translation: BAC11089.1. Different initiation.

IPI

IPI00001707.
IPI00647008.

RefSeq

NP_001167455.1. NM_001173984.2.
NP_037395.2. NM_013263.4.

UniGene

Hs.437894.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2I7K	NMR	-	A	129-236	[»]

ProteinModelPortal

Q9NPI1.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-32509N.

IntAct

Q9NPI1. 19 interactions.

MINT

MINT-1383082.

STRING

9606.ENSP00000378180.

PTM databases

PhosphoSite

Q9NPI1.

Polymorphism databases

DMDM

74734307.

Proteomic databases

PaxDb

Q9NPI1.

PRIDE

Q9NPI1.

Protocols and materials databases

DNASU

29117.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000394688; ENSP00000378180; ENSG00000166164.
ENST00000394689; ENSP00000378181; ENSG00000166164.

GeneID

29117.

KEGG

hsa:29117.

UCSC

uc002ege.2. human.
uc021thx.1. human.

Organism-specific databases

CTD

29117.

GeneCards

GC16M050352.

HGNC

HGNC:14310. BRD7.

HPA

CAB046458.

neXtProt

NX_Q9NPI1.

PharmGKB

PA25417.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5076.

HOGENOM

HOG000070022.

HOVERGEN

HBG071934.

KO

K11723.

OMA

EDKFKSN.

OrthoDB

EOG4D26PG.

PhylomeDB

Q9NPI1.

Gene expression databases

ArrayExpress

Q9NPI1.

Bgee

Q9NPI1.

CleanEx

HS_BRD7.

Genevestigator

Q9NPI1.

GermOnline

ENSG00000166164. Homo sapiens.

Family and domain databases

Gene3D

1.20.920.10. 1 hit.

InterPro

IPR001487. Bromodomain.
IPR021900. DUF3512.
[Graphical view]

Pfam

PF00439. Bromodomain. 1 hit.
PF12024. DUF3512. 1 hit.
[Graphical view]

PRINTS

PR00503. BROMODOMAIN.

SMART

SM00297. BROMO. 1 hit.
[Graphical view]

SUPFAM

SSF47370. Bromodomain. 1 hit.

PROSITE

PS00633. BROMODOMAIN_1. False negative.
PS50014. BROMODOMAIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9NPI1.

GenomeRNAi

29117.

NextBio

52203.

Entry information

Entry name

BRD7_HUMAN

Accession

Primary (citable) accession number: Q9NPI1
Secondary accession number(s): Q4VC09 , Q8N2L9, Q96KA4, Q9BV48, Q9UH59

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 101 of the entry and version 1 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.