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Q9NPI1

- BRD7_HUMAN

UniProt

Q9NPI1 - BRD7_HUMAN

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Protein
Bromodomain-containing protein 7
Gene
BRD7, BP75, CELTIX1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.5 Publications

GO - Molecular functioni

  1. histone binding Source: MGI
  2. lysine-acetylated histone binding Source: UniProtKB
  3. p53 binding Source: UniProtKB
  4. protein binding Source: UniProtKB
  5. transcription coactivator activity Source: UniProtKB
  6. transcription corepressor activity Source: UniProtKB
  7. transcription factor binding Source: MGI
  8. transcription regulatory region DNA binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. Wnt signaling pathway Source: UniProtKB-KW
  2. cell cycle Source: UniProtKB-KW
  3. negative regulation of G1/S transition of mitotic cell cycle Source: UniProtKB
  4. negative regulation of cell proliferation Source: UniProtKB
  5. negative regulation of transcription, DNA-templated Source: UniProtKB
  6. positive regulation of histone acetylation Source: UniProtKB
  7. positive regulation of transcription, DNA-templated Source: UniProtKB
  8. regulation of transcription from RNA polymerase II promoter Source: MGI
  9. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation, Wnt signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Bromodomain-containing protein 7
Alternative name(s):
75 kDa bromodomain protein
Protein CELTIX-1
Gene namesi
Name:BRD7
Synonyms:BP75, CELTIX1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:14310. BRD7.

Subcellular locationi

Isoform 2 : Nucleus 4 Publications

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA25417.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 651651Bromodomain-containing protein 7
PRO_0000227664Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei279 – 2791Phosphoserine3 Publications
Modified residuei328 – 3281N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9NPI1.
PaxDbiQ9NPI1.
PRIDEiQ9NPI1.

PTM databases

PhosphoSiteiQ9NPI1.

Expressioni

Gene expression databases

ArrayExpressiQ9NPI1.
BgeeiQ9NPI1.
CleanExiHS_BRD7.
GenevestigatoriQ9NPI1.

Organism-specific databases

HPAiCAB046458.

Interactioni

Subunit structurei

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).7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EP300Q094723EBI-711221,EBI-447295
HNRNPUL1Q9BUJ25EBI-711221,EBI-1018153
TP53P046378EBI-711221,EBI-366083

Protein-protein interaction databases

BioGridi118883. 36 interactions.
DIPiDIP-32509N.
IntActiQ9NPI1. 26 interactions.
MINTiMINT-1383082.
STRINGi9606.ENSP00000378180.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi133 – 14816
Helixi152 – 1543
Beta strandi156 – 1583
Turni162 – 1643
Beta strandi165 – 1673
Helixi168 – 1714
Helixi178 – 1858
Turni186 – 1883
Helixi193 – 20917
Beta strandi213 – 2164
Helixi217 – 23519

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I7KNMR-A129-236[»]
ProteinModelPortaliQ9NPI1.
SMRiQ9NPI1. Positions 129-238, 338-393.

Miscellaneous databases

EvolutionaryTraceiQ9NPI1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini148 – 21871Bromo
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili536 – 56732 Reviewed prediction
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi65 – 9632Nuclear localization signal1 Publication
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3 – 9189Lys-rich
Add
BLAST

Sequence similaritiesi

Contains 1 bromo domain.

Keywords - Domaini

Bromodomain, Coiled coil

Phylogenomic databases

eggNOGiCOG5076.
HOGENOMiHOG000070022.
HOVERGENiHBG071934.
KOiK11723.
OMAiGDIVSTY.
OrthoDBiEOG7D2FDM.
PhylomeDBiQ9NPI1.
TreeFamiTF106439.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
InterProiIPR001487. Bromodomain.
IPR021900. DUF3512.
[Graphical view]
PfamiPF00439. Bromodomain. 1 hit.
PF12024. DUF3512. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
PROSITEiPS50014. BROMODOMAIN_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NPI1-1) [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

MGKKHKKHKS DKHLYEEYVE KPLKLVLKVG GNEVTELSTG SSGHDSSLFE    50
DKNDHDKHKD RKRKKRKKGE KQIPGEEKGR KRRRVKEDKK KRDRDRVENE 100
AEKDLQCHAP VRLDLPPEKP LTSSLAKQEE VEQTPLQEAL NQLMRQLQRK 150
DPSAFFSFPV TDFIAPGYSM IIKHPMDFST MKEKIKNNDY QSIEELKDNF 200
KLMCTNAMIY NKPETIYYKA AKKLLHSGMK ILSQERIQSL KQSIDFMADL 250
QKTRKQKDGT DTSQSGEDGG CWQREREDSG DAEAHAFKSP SKENKKKDKD 300
MLEDKFKSNN LEREQEQLDR IVKESGGKLT RRLVNSQCEF ERRKPDGTTT 350
LGLLHPVDPI VGEPGYCPVR LGMTTGRLQS GVNTLQGFKE DKRNKVTPVL 400
YLNYGPYSSY APHYDSTFAN ISKDDSDLIY STYGEDSDLP SDFSIHEFLA 450
TCQDYPYVMA DSLLDVLTKG GHSRTLQEME MSLPEDEGHT RTLDTAKEME 500
ITEVEPPGRL DSSTQDRLIA LKAVTNFGVP VEVFDSEEAE IFQKKLDETT 550
RLLRELQEAQ NERLSTRPPP NMICLLGPSY REMHLAEQVT NNLKELAQQV 600
TPGDIVSTYG VRKAMGISIP SPVMENNFVD LTEDTEEPKK TDVAECGPGG 650
S 651
Length:651
Mass (Da):74,139
Last modified:October 1, 2000 - v1
Checksum:i29B7947644C215E7
GO
Isoform 2 (identifier: Q9NPI1-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:652
Mass (Da):74,267
Checksum:iAE7A8BB828D0B538
GO

Sequence cautioni

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei500 – 5001E → EQ in isoform 2.
VSP_017564

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661R → G in AAF19526. 1 Publication
Sequence conflicti83 – 831R → T in AAF19526. 1 Publication
Sequence conflicti96 – 961R → Q in AAF19526. 1 Publication
Sequence conflicti170 – 1701M → I in AAH94706. 1 Publication
Sequence conflicti485 – 4851E → G in BAB55031. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS10742.1. [Q9NPI1-1]
CCDS54007.1. [Q9NPI1-2]
RefSeqiNP_001167455.1. NM_001173984.2. [Q9NPI1-2]
NP_037395.2. NM_013263.4. [Q9NPI1-1]
UniGeneiHs.437894.

Genome annotation databases

EnsembliENST00000394688; ENSP00000378180; ENSG00000166164. [Q9NPI1-1]
ENST00000394689; ENSP00000378181; ENSG00000166164. [Q9NPI1-2]
GeneIDi29117.
KEGGihsa:29117.
UCSCiuc002ege.2. human. [Q9NPI1-2]
uc021thx.1. human. [Q9NPI1-1]

Polymorphism databases

DMDMi74734307.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS10742.1. [Q9NPI1-1 ]
CCDS54007.1. [Q9NPI1-2 ]
RefSeqi NP_001167455.1. NM_001173984.2. [Q9NPI1-2 ]
NP_037395.2. NM_013263.4. [Q9NPI1-1 ]
UniGenei Hs.437894.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2I7K NMR - A 129-236 [» ]
ProteinModelPortali Q9NPI1.
SMRi Q9NPI1. Positions 129-238, 338-393.
ModBasei Search...

Protein-protein interaction databases

BioGridi 118883. 36 interactions.
DIPi DIP-32509N.
IntActi Q9NPI1. 26 interactions.
MINTi MINT-1383082.
STRINGi 9606.ENSP00000378180.

PTM databases

PhosphoSitei Q9NPI1.

Polymorphism databases

DMDMi 74734307.

Proteomic databases

MaxQBi Q9NPI1.
PaxDbi Q9NPI1.
PRIDEi Q9NPI1.

Protocols and materials databases

DNASUi 29117.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000394688 ; ENSP00000378180 ; ENSG00000166164 . [Q9NPI1-1 ]
ENST00000394689 ; ENSP00000378181 ; ENSG00000166164 . [Q9NPI1-2 ]
GeneIDi 29117.
KEGGi hsa:29117.
UCSCi uc002ege.2. human. [Q9NPI1-2 ]
uc021thx.1. human. [Q9NPI1-1 ]

Organism-specific databases

CTDi 29117.
GeneCardsi GC16M050352.
HGNCi HGNC:14310. BRD7.
HPAi CAB046458.
neXtProti NX_Q9NPI1.
PharmGKBi PA25417.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5076.
HOGENOMi HOG000070022.
HOVERGENi HBG071934.
KOi K11723.
OMAi GDIVSTY.
OrthoDBi EOG7D2FDM.
PhylomeDBi Q9NPI1.
TreeFami TF106439.

Miscellaneous databases

EvolutionaryTracei Q9NPI1.
GeneWikii BRD7.
GenomeRNAii 29117.
NextBioi 52203.
PROi Q9NPI1.

Gene expression databases

ArrayExpressi Q9NPI1.
Bgeei Q9NPI1.
CleanExi HS_BRD7.
Genevestigatori Q9NPI1.

Family and domain databases

Gene3Di 1.20.920.10. 1 hit.
InterProi IPR001487. Bromodomain.
IPR021900. DUF3512.
[Graphical view ]
Pfami PF00439. Bromodomain. 1 hit.
PF12024. DUF3512. 1 hit.
[Graphical view ]
PRINTSi PR00503. BROMODOMAIN.
SMARTi SM00297. BROMO. 1 hit.
[Graphical view ]
SUPFAMi SSF47370. SSF47370. 1 hit.
PROSITEi PS50014. BROMODOMAIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, 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. 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.

Entry informationi

Entry nameiBRD7_HUMAN
AccessioniPrimary (citable) accession number: Q9NPI1
Secondary accession number(s): Q4VC09
, Q8N2L9, Q96KA4, Q9BV48, Q9UH59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 112 of the entry and version 1 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 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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