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Q9NPI1 (BRD7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bromodomain-containing protein 7
Alternative name(s):
75 kDa bromodomain protein
Protein CELTIX-1
Gene names
Name:BRD7
Synonyms:BP75, CELTIX1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length651 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processCell cycle
Transcription
Transcription regulation
Wnt signaling pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseTumor suppressor
   DomainBromodomain
Coiled coil
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt 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-templated

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-templated

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-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Traceable author statement PubMed 10526152. Source: ProtInc

nucleus

Inferred from direct assay Ref.8Ref.12. Source: UniProtKB

   Molecular_functionhistone acetyl-lysine binding

Inferred from direct assay Ref.8. Source: UniProtKB

histone binding

Inferred from direct assay Ref.2. Source: MGI

p53 binding

Inferred from physical interaction Ref.12. 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

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 651651Bromodomain-containing protein 7
PRO_0000227664

Regions

Domain148 – 21871Bromo
Coiled coil536 – 56732 Potential
Motif65 – 9632Nuclear localization signal Ref.9
Compositional bias3 – 9189Lys-rich

Amino acid modifications

Modified residue2791Phosphoserine Ref.7 Ref.14 Ref.15
Modified residue3281N6-acetyllysine By similarity

Natural variations

Alternative sequence5001E → EQ in isoform 2.
VSP_017564

Experimental info

Sequence conflict661R → G in AAF19526. Ref.1
Sequence conflict831R → T in AAF19526. Ref.1
Sequence conflict961R → Q in AAF19526. Ref.1
Sequence conflict1701M → I in AAH94706. Ref.5
Sequence conflict4851E → G in BAB55031. Ref.6

Secondary structure

................... 651
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 29B7947644C215E7

FASTA65174,139
        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 

« Hide

Isoform 2 [UniParc].

Checksum: AE7A8BB828D0B538
Show »

FASTA65274,267

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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.
RefSeqNP_001167455.1. NM_001173984.2.
NP_037395.2. NM_013263.4.
UniGeneHs.437894.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2I7KNMR-A129-236[»]
ProteinModelPortalQ9NPI1.
SMRQ9NPI1. Positions 129-238, 338-393.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118883. 36 interactions.
DIPDIP-32509N.
IntActQ9NPI1. 26 interactions.
MINTMINT-1383082.
STRING9606.ENSP00000378180.

PTM databases

PhosphoSiteQ9NPI1.

Polymorphism databases

DMDM74734307.

Proteomic databases

PaxDbQ9NPI1.
PRIDEQ9NPI1.

Protocols and materials databases

DNASU29117.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000394688; ENSP00000378180; ENSG00000166164. [Q9NPI1-1]
ENST00000394689; ENSP00000378181; ENSG00000166164. [Q9NPI1-2]
GeneID29117.
KEGGhsa:29117.
UCSCuc002ege.2. human. [Q9NPI1-2]
uc021thx.1. human. [Q9NPI1-1]

Organism-specific databases

CTD29117.
GeneCardsGC16M050352.
HGNCHGNC:14310. BRD7.
HPACAB046458.
neXtProtNX_Q9NPI1.
PharmGKBPA25417.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5076.
HOGENOMHOG000070022.
HOVERGENHBG071934.
KOK11723.
OMAGDIVSTY.
OrthoDBEOG7D2FDM.
PhylomeDBQ9NPI1.
TreeFamTF106439.

Gene expression databases

ArrayExpressQ9NPI1.
BgeeQ9NPI1.
CleanExHS_BRD7.
GenevestigatorQ9NPI1.

Family and domain databases

Gene3D1.20.920.10. 1 hit.
InterProIPR001487. Bromodomain.
IPR021900. DUF3512.
[Graphical view]
PfamPF00439. Bromodomain. 1 hit.
PF12024. DUF3512. 1 hit.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00297. BROMO. 1 hit.
[Graphical view]
SUPFAMSSF47370. SSF47370. 1 hit.
PROSITEPS50014. BROMODOMAIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9NPI1.
GeneWikiBRD7.
GenomeRNAi29117.
NextBio52203.
PROQ9NPI1.

Entry information

Entry nameBRD7_HUMAN
AccessionPrimary (citable) accession number: Q9NPI1
Secondary accession number(s): Q4VC09 expand/collapse secondary AC list , Q8N2L9, Q96KA4, Q9BV48, Q9UH59
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM