Q9NPI1 · BRD7_HUMAN
- ProteinBromodomain-containing protein 7
- GeneBRD7
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids651 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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
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
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBromodomain-containing protein 7
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9NPI1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 798 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, cross-link, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000227664 | 1-651 | UniProt | Bromodomain-containing protein 7 | |||
Sequence: MGKKHKKHKSDKHLYEEYVEKPLKLVLKVGGNEVTELSTGSSGHDSSLFEDKNDHDKHKDRKRKKRKKGEKQIPGEEKGRKRRRVKEDKKKRDRDRVENEAEKDLQCHAPVRLDLPPEKPLTSSLAKQEEVEQTPLQEALNQLMRQLQRKDPSAFFSFPVTDFIAPGYSMIIKHPMDFSTMKEKIKNNDYQSIEELKDNFKLMCTNAMIYNKPETIYYKAAKKLLHSGMKILSQERIQSLKQSIDFMADLQKTRKQKDGTDTSQSGEDGGCWQREREDSGDAEAHAFKSPSKENKKKDKDMLEDKFKSNNLEREQEQLDRIVKESGGKLTRRLVNSQCEFERRKPDGTTTLGLLHPVDPIVGEPGYCPVRLGMTTGRLQSGVNTLQGFKEDKRNKVTPVLYLNYGPYSSYAPHYDSTFANISKDDSDLIYSTYGEDSDLPSDFSIHEFLATCQDYPYVMADSLLDVLTKGGHSRTLQEMEMSLPEDEGHTRTLDTAKEMEITEVEPPGRLDSSTQDRLIALKAVTNFGVPVEVFDSEEAEIFQKKLDETTRLLRELQEAQNERLSTRPPPNMICLLGPSYREMHLAEQVTNNLKELAQQVTPGDIVSTYGVRKAMGISIPSPVMENNFVDLTEDTEEPKKTDVAECGPGGS | |||||||
Cross-link | 21 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 41 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 42 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 46 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 47 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 52 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 127 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 186 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 197 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 201 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 212 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 241 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 263 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 265 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 279 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 279 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 289 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 289 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 291 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 305 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 307 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 328 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Cross-link | 344 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 380 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 380 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 389 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 482 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 514 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 621 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 621 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 651 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
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)
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)
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9NPI1 | EP300 Q09472 | 3 | EBI-711221, EBI-447295 | |
BINARY | Q9NPI1 | HNRNPUL1 Q9BUJ2 | 5 | EBI-711221, EBI-1018153 | |
BINARY | Q9NPI1 | PLEKHF2 Q9H8W4 | 3 | EBI-711221, EBI-742388 | |
BINARY | Q9NPI1 | TP53 P04637 | 9 | EBI-711221, EBI-366083 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, motif, compositional bias, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 35-132 | Disordered | ||||
Sequence: TELSTGSSGHDSSLFEDKNDHDKHKDRKRKKRKKGEKQIPGEEKGRKRRRVKEDKKKRDRDRVENEAEKDLQCHAPVRLDLPPEKPLTSSLAKQEEVE | ||||||
Motif | 65-96 | Nuclear localization signal | ||||
Sequence: KRKKGEKQIPGEEKGRKRRRVKEDKKKRDRDR | ||||||
Compositional bias | 90-109 | Basic and acidic residues | ||||
Sequence: KKRDRDRVENEAEKDLQCHA | ||||||
Domain | 148-218 | Bromo | ||||
Sequence: QRKDPSAFFSFPVTDFIAPGYSMIIKHPMDFSTMKEKIKNNDYQSIEELKDNFKLMCTNAMIYNKPETIYY | ||||||
Region | 253-301 | Disordered | ||||
Sequence: TRKQKDGTDTSQSGEDGGCWQREREDSGDAEAHAFKSPSKENKKKDKDM | ||||||
Compositional bias | 270-301 | Basic and acidic residues | ||||
Sequence: GCWQREREDSGDAEAHAFKSPSKENKKKDKDM | ||||||
Coiled coil | 536-567 | |||||
Sequence: SEEAEIFQKKLDETTRLLRELQEAQNERLSTR |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
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.
- Name1
- Length651
- Mass (Da)74,139
- Last updated2000-10-01 v1
- Checksum29B7947644C215E7
Q9NPI1-2
- Name2
- Differences from canonical
- 500-500: E → EQ
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0AA34QW01 | A0AA34QW01_HUMAN | BRD7 | 692 | ||
A0AA34QVS2 | A0AA34QVS2_HUMAN | BRD7 | 668 | ||
I3L4V5 | I3L4V5_HUMAN | BRD7 | 109 | ||
I3L0Y7 | I3L0Y7_HUMAN | BRD7 | 32 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 66 | in Ref. 1; AAF19526 | ||||
Sequence: R → G | ||||||
Sequence conflict | 83 | in Ref. 1; AAF19526 | ||||
Sequence: R → T | ||||||
Compositional bias | 90-109 | Basic and acidic residues | ||||
Sequence: KKRDRDRVENEAEKDLQCHA | ||||||
Sequence conflict | 96 | in Ref. 1; AAF19526 | ||||
Sequence: R → Q | ||||||
Sequence conflict | 170 | in Ref. 5; AAH94706 | ||||
Sequence: M → I | ||||||
Compositional bias | 270-301 | Basic and acidic residues | ||||
Sequence: GCWQREREDSGDAEAHAFKSPSKENKKKDKDM | ||||||
Sequence conflict | 485 | in Ref. 6; BAB55031 | ||||
Sequence: E → G | ||||||
Alternative sequence | VSP_017564 | 500 | in isoform 2 | |||
Sequence: E → EQ |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF213969 EMBL· GenBank· DDBJ | AAF19526.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ271881 EMBL· GenBank· DDBJ | CAB72445.1 EMBL· GenBank· DDBJ | mRNA | ||
AF152604 EMBL· GenBank· DDBJ | AAF75126.1 EMBL· GenBank· DDBJ | mRNA | ||
BC001611 EMBL· GenBank· DDBJ | AAH01611.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC007493 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC007597 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC023826 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC050728 EMBL· GenBank· DDBJ | AAH50728.1 EMBL· GenBank· DDBJ | mRNA | ||
BC094706 EMBL· GenBank· DDBJ | AAH94706.1 EMBL· GenBank· DDBJ | mRNA | ||
AK027308 EMBL· GenBank· DDBJ | BAB55031.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK074613 EMBL· GenBank· DDBJ | BAC11089.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |