UniProt ID | BDF2_YEAST | |
---|---|---|
UniProt AC | Q07442 | |
Protein Name | Bromodomain-containing factor 2 | |
Gene Name | BDF2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 638 | |
Subcellular Localization | Cytoplasm . Nucleus . | |
Protein Description | Transcription factor involved in the expression of a broad class of genes including snRNAs. Required for sporulation and DNA-damage repair. Prevents the spreading of SIR silencing at telomeres and protects histone H4, but not H3, from deacetylation (By similarity).. | |
Protein Sequence | MSRTNMDTRHAHSALLAAPQSATANSRSSNSSSESSSNKNNINVGVGDDSGNVSAVSIDDGPHFRDIFHYGHEENYKLASSGITNLNSSSHAHQTLSPISISNASTPESFPEHPLGLERETEPALEAEMEAEELPPHQSKYLLSSIKATKRLKDARPFLKPVDPIALNIPHYFNYVQTPMDLSLIETKLQGNVYHSVEQVTSDFKTMVDNCLNFNGPESSISSMAKRIQKYFEKKLSAMPPRVLPASALKKTSRNRKKNEDMDSPLVIRRSVSTTNDNIGESGNREGVSGGRPKRTIHPPKSKDLFDIYENSKPKSKTLQKKFRTCLKILKVLMSKKNSDINFPFLQPVDPIALNLPNYFDVVKNPMDLGTISNNLMNWKYKTIDQFVDDLNLVFYNCFQFNPEGNEVHSMGKKLKELFNFHWLENQDILNEIETDSDLEEDNYSSSYSSDDEYDDEDINENDITNPAIQYLEQKLKKMEVELQQLKRQELSKLSKERKRKHLGKTLLRRKAMKHSVDDLKKSITDKINELSDLEMNGMIRIIKNSLPADEILTSNEDEIEIDLDILDEATIARIYERYFEKKNNNNSKRKLSGNYSTAPTNKKKKTLKFLEKDEIINNNNYSDSEEDSSDSSDSDSD | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
50 | Phosphorylation | NVGVGDDSGNVSAVS EEECCCCCCCEEEEE | 36.69 | 19779198 | |
54 | Phosphorylation | GDDSGNVSAVSIDDG CCCCCCEEEEECCCC | 27.27 | 19779198 | |
57 | Phosphorylation | SGNVSAVSIDDGPHF CCCEEEEECCCCCCH | 21.73 | 19779198 | |
141 | Phosphorylation | LPPHQSKYLLSSIKA CCHHHHHHHHHHHHH | 20.37 | 30377154 | |
145 | Phosphorylation | QSKYLLSSIKATKRL HHHHHHHHHHHHHHH | 28.25 | 30377154 | |
264 | Phosphorylation | KKNEDMDSPLVIRRS HCCCCCCCCCEEEEC | 17.31 | 17330950 | |
271 | Phosphorylation | SPLVIRRSVSTTNDN CCCEEEECEECCCCC | 15.57 | 22369663 | |
273 | Phosphorylation | LVIRRSVSTTNDNIG CEEEECEECCCCCCC | 30.66 | 22369663 | |
274 | Phosphorylation | VIRRSVSTTNDNIGE EEEECEECCCCCCCC | 27.71 | 22369663 | |
275 | Phosphorylation | IRRSVSTTNDNIGES EEECEECCCCCCCCC | 32.82 | 21440633 | |
505 | Acetylation | RKRKHLGKTLLRRKA HHHHHHHHHHHHHHH | 42.22 | 25381059 | |
525 | Phosphorylation | DDLKKSITDKINELS HHHHHHHHHHHHHHH | 38.03 | 21440633 | |
532 | Phosphorylation | TDKINELSDLEMNGM HHHHHHHHHHHHHHH | 33.69 | 21440633 | |
544 | Ubiquitination | NGMIRIIKNSLPADE HHHHHHHHCCCCHHH | 37.81 | 17644757 | |
593 | Phosphorylation | NNSKRKLSGNYSTAP CCCCCCCCCCCCCCC | 28.20 | 19823750 | |
596 | Phosphorylation | KRKLSGNYSTAPTNK CCCCCCCCCCCCCCC | 15.78 | 21440633 | |
597 | Phosphorylation | RKLSGNYSTAPTNKK CCCCCCCCCCCCCCC | 23.30 | 27214570 | |
598 | Phosphorylation | KLSGNYSTAPTNKKK CCCCCCCCCCCCCCC | 26.71 | 30377154 |
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 BDF2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BDF2_YEAST !! |
* 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 BDF2_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273 AND SER-593, ANDMASS SPECTROMETRY. | |
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, AND MASSSPECTROMETRY. |