UniProt ID | BRD7_MOUSE | |
---|---|---|
UniProt AC | O88665 | |
Protein Name | Bromodomain-containing protein 7 | |
Gene Name | Brd7 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 651 | |
Subcellular Localization | Nucleus . | |
Protein Description | Acts both as coactivator and as corepressor. May play a role in chromatin remodeling. 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 (By similarity). 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.. | |
Protein Sequence | MGKKHKKHKSDRHFYEEYVEKPLKLVLKVGGSEVTELSTGSSGHDSSLFEDRSDHDKHKDRKRKKRKKGEKQAPGEEKGRKRRRVKEDKKKRDRDRAENEVDRDLQCHVPIRLDLPPEKPLTSSLAKQEEVEQTPLQEALNQLMRQLQRKDPSAFFSFPVTDFIAPGYSMIIKHPMDFSTMKEKIKNNDYQSIEELKDNFKLMCTNAMIYNKPETIYYKAAKKLLHSGMKILSQERIQSLKQSIDFMSDLQKTRKQKERTDACQSGEDSGCWQREREDSGDAETQAFRSPAKDNKRKDKDVLEDKWRSSNSEREHEQIERVVQESGGKLTRRLANSQCEFERRKPDGTTTLGLLHPVDPIVGEPGYCPVRLGMTTGRLQSGVNTLQGFKEDKRNRVTPVLYLNYGPYSSYAPHYDSTFANISKDDSDLIYSTYGEDSDLPNNFSISEFLATCQDYPYVMADSLLDVLTKGGHSRSLQDLDMSSPEDEGQTRALDTAKEAEITQIEPTGRLESSSQDRLTALQAVTTFGAPAEVFDSEEAEVFQRKLDETTRLLRELQEAQNERLSTRPPPNMICLLGPSYREMYLAEQVTNNLKELTQQVTPGDVVSIHGVRKAMGISVPSPIVGNSFVDLTGECEEPKETSTAECGPDAS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
18 | Phosphorylation | DRHFYEEYVEKPLKL CCCHHHHHHHCCEEE | 11.28 | 25159016 | |
32 | Phosphorylation | LVLKVGGSEVTELST EEEEECCCEEEEECC | 23.98 | 25293948 | |
35 | Phosphorylation | KVGGSEVTELSTGSS EECCCEEEEECCCCC | 27.45 | 25293948 | |
38 | Phosphorylation | GSEVTELSTGSSGHD CCEEEEECCCCCCCC | 25.21 | 19060867 | |
39 | Phosphorylation | SEVTELSTGSSGHDS CEEEEECCCCCCCCC | 54.42 | 19060867 | |
41 | Phosphorylation | VTELSTGSSGHDSSL EEEECCCCCCCCCCC | 32.98 | 21183079 | |
42 | Phosphorylation | TELSTGSSGHDSSLF EEECCCCCCCCCCCC | 41.30 | 22817900 | |
46 | Phosphorylation | TGSSGHDSSLFEDRS CCCCCCCCCCCCCCC | 24.22 | 25293948 | |
47 | Phosphorylation | GSSGHDSSLFEDRSD CCCCCCCCCCCCCCC | 43.04 | 25293948 | |
53 | Phosphorylation | SSLFEDRSDHDKHKD CCCCCCCCCCCHHHH | 52.17 | 25338131 | |
197 | Ubiquitination | YQSIEELKDNFKLMC CCCHHHHHHHHEEEE | 54.64 | 22790023 | |
265 | Phosphorylation | ERTDACQSGEDSGCW HHCHHHHCCCCCCCC | 43.99 | 26643407 | |
279 | Phosphorylation | WQREREDSGDAETQA CCCCCCCCCCHHHHH | 33.54 | 25521595 | |
284 | Phosphorylation | EDSGDAETQAFRSPA CCCCCHHHHHHCCCC | 27.24 | 25619855 | |
289 | Phosphorylation | AETQAFRSPAKDNKR HHHHHHCCCCCCCCC | 23.82 | 26824392 | |
311 | Phosphorylation | DKWRSSNSEREHEQI HHHHCCCHHHHHHHH | 39.72 | 27841257 | |
328 | Acetylation | VVQESGGKLTRRLAN HHHHHCCHHHHHHHH | 50.65 | 23806337 | |
380 | Phosphorylation | MTTGRLQSGVNTLQG CCCCCCCCCCCCHHC | 49.66 | - | |
475 | Phosphorylation | TKGGHSRSLQDLDMS HCCCCCCCHHHCCCC | 33.14 | 25159016 | |
482 | Phosphorylation | SLQDLDMSSPEDEGQ CHHHCCCCCCCCHHH | 42.27 | 21082442 | |
483 | Phosphorylation | LQDLDMSSPEDEGQT HHHCCCCCCCCHHHC | 26.18 | 22942356 | |
490 | Phosphorylation | SPEDEGQTRALDTAK CCCCHHHCHHHHHHH | 28.85 | 21743459 | |
618 | Phosphorylation | VRKAMGISVPSPIVG HHHHHCCCCCCCCCC | 23.42 | 26643407 | |
621 | Phosphorylation | AMGISVPSPIVGNSF HHCCCCCCCCCCCCE | 25.71 | 26643407 | |
627 | Phosphorylation | PSPIVGNSFVDLTGE CCCCCCCCEECCCCC | 22.25 | 26643407 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of BRD7_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BRD7_MOUSE !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of BRD7_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of BRD7_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, AND MASSSPECTROMETRY. |