| UniProt ID | BDF1_YEAST | |
|---|---|---|
| UniProt AC | P35817 | |
| Protein Name | Bromodomain-containing factor 1 | |
| Gene Name | BDF1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 686 | |
| Subcellular Localization | 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.. | |
| Protein Sequence | MTDITPVQNDVDVNGNNVNDDVSSNLKRPIDQGDPSNGLAEEENPANNQLHLKKARLDGDALTSSPAGLAENGIEGATLAANGENGYNATGSGAEDEQQGLKKEEGGQGTKQEDLDENSKQELPMEVPKEPAPAPPPEPDMNNLPQNPIPKHQQKHALLAIKAVKRLKDARPFLQPVDPVKLDIPFYFNYIKRPMDLSTIERKLNVGAYEVPEQITEDFNLMVNNSIKFNGPNAGISQMARNIQASFEKHMLNMPAKDAPPVIAKGRRSSAQEDAPIVIRRAQTHNGRPKRTIHPPKSKDIYPYESKKPKSKRLQQAMKFCQSVLKELMAKKHASYNYPFLEPVDPVSMNLPTYFDYVKEPMDLGTIAKKLNDWQYQTMEDFERDVRLVFKNCYTFNPDGTIVNMMGHRLEEVFNSKWADRPNLDDYDSDEDSRTQGDYDDYESEYSESDIDETIITNPAIQYLEEQLARMKVELQQLKKQELEKIRKERRLARGSKKRGKRSKGRSGSKNASSKGRRDKKNKLKTVVTYDMKRIITERINDLPTSKLERAIDIIKKSMPNISEDDEVELDLDTLDNHTILTLYNTFFRQYESSSGASNGLDGTSGVTRDASSLSPTSAGSRKRRSKALSQEEQSRQIEKIKNKLAILDSASPLSQNGSPGQIQSAAHNGFSSSSDDDVSSESEEE | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MTDITPVQN ------CCCCCCCCC | 35.79 | 28132839 | |
| 5 | Phosphorylation | ---MTDITPVQNDVD ---CCCCCCCCCCCC | 21.88 | 22369663 | |
| 36 | Phosphorylation | PIDQGDPSNGLAEEE CCCCCCCCCCCCCCC | 48.55 | 21551504 | |
| 53 | Acetylation | ANNQLHLKKARLDGD CCCCEEEEECCCCCC | 33.37 | 24489116 | |
| 63 | Phosphorylation | RLDGDALTSSPAGLA CCCCCHHCCCCCHHH | 28.95 | 21440633 | |
| 64 | Phosphorylation | LDGDALTSSPAGLAE CCCCHHCCCCCHHHH | 34.86 | 20377248 | |
| 65 | Phosphorylation | DGDALTSSPAGLAEN CCCHHCCCCCHHHHC | 17.34 | 20377248 | |
| 78 | Phosphorylation | ENGIEGATLAANGEN HCCCCCCEEEECCCC | 27.99 | 20377248 | |
| 87 | Phosphorylation | AANGENGYNATGSGA EECCCCCCCCCCCCH | 17.13 | 20377248 | |
| 90 | Phosphorylation | GENGYNATGSGAEDE CCCCCCCCCCCHHHH | 28.39 | 21440633 | |
| 92 | Phosphorylation | NGYNATGSGAEDEQQ CCCCCCCCCHHHHHH | 30.40 | 20377248 | |
| 119 | Phosphorylation | QEDLDENSKQELPME HHHCCCCCCCCCCCC | 33.40 | 28889911 | |
| 237 | Phosphorylation | NGPNAGISQMARNIQ CCCCHHHHHHHHHHH | 17.00 | 25704821 | |
| 246 | Phosphorylation | MARNIQASFEKHMLN HHHHHHHHHHHHHHC | 19.98 | 30377154 | |
| 269 | Phosphorylation | VIAKGRRSSAQEDAP EEECCCCCCCCCCCC | 28.76 | 22369663 | |
| 270 | Phosphorylation | IAKGRRSSAQEDAPI EECCCCCCCCCCCCE | 31.96 | 22369663 | |
| 299 | Acetylation | TIHPPKSKDIYPYES CCCCCCCCCCCCCCC | 55.03 | 24489116 | |
| 307 | Acetylation | DIYPYESKKPKSKRL CCCCCCCCCCCCHHH | 62.24 | 24489116 | |
| 336 | Phosphorylation | MAKKHASYNYPFLEP HHHHCCCCCCCCCCC | 21.35 | 27017623 | |
| 338 | Phosphorylation | KKHASYNYPFLEPVD HHCCCCCCCCCCCCC | 6.27 | 27017623 | |
| 353 | Phosphorylation | PVSMNLPTYFDYVKE CCCCCCCCHHHHCCC | 39.73 | 27017623 | |
| 357 | Phosphorylation | NLPTYFDYVKEPMDL CCCCHHHHCCCCCCH | 11.97 | 27017623 | |
| 427 | Phosphorylation | DRPNLDDYDSDEDSR CCCCCCCCCCCCCCC | 19.60 | 22890988 | |
| 429 | Phosphorylation | PNLDDYDSDEDSRTQ CCCCCCCCCCCCCCC | 36.35 | 22369663 | |
| 433 | Phosphorylation | DYDSDEDSRTQGDYD CCCCCCCCCCCCCCC | 34.87 | 22890988 | |
| 547 | Acetylation | INDLPTSKLERAIDI HHHCCHHHHHHHHHH | 57.77 | 24489116 | |
| 598 | Phosphorylation | YESSSGASNGLDGTS HHCCCCCCCCCCCCC | 34.65 | 30377154 | |
| 604 | Phosphorylation | ASNGLDGTSGVTRDA CCCCCCCCCCCCCCH | 23.21 | 23749301 | |
| 605 | Phosphorylation | SNGLDGTSGVTRDAS CCCCCCCCCCCCCHH | 36.47 | 23749301 | |
| 608 | Phosphorylation | LDGTSGVTRDASSLS CCCCCCCCCCHHHCC | 26.76 | 27017623 | |
| 612 | Phosphorylation | SGVTRDASSLSPTSA CCCCCCHHHCCCCCH | 35.78 | 22369663 | |
| 613 | Phosphorylation | GVTRDASSLSPTSAG CCCCCHHHCCCCCHH | 34.29 | 22369663 | |
| 615 | Phosphorylation | TRDASSLSPTSAGSR CCCHHHCCCCCHHHH | 28.25 | 22369663 | |
| 617 | Phosphorylation | DASSLSPTSAGSRKR CHHHCCCCCHHHHHH | 28.03 | 22369663 | |
| 618 | Phosphorylation | ASSLSPTSAGSRKRR HHHCCCCCHHHHHHH | 33.73 | 22369663 | |
| 621 | Phosphorylation | LSPTSAGSRKRRSKA CCCCCHHHHHHHHHH | 34.05 | 22890988 | |
| 626 | Phosphorylation | AGSRKRRSKALSQEE HHHHHHHHHHCCHHH | 26.72 | 23749301 | |
| 627 | Ubiquitination | GSRKRRSKALSQEEQ HHHHHHHHHCCHHHH | 52.08 | 23749301 | |
| 627 | Acetylation | GSRKRRSKALSQEEQ HHHHHHHHHCCHHHH | 52.08 | 25381059 | |
| 630 | Phosphorylation | KRRSKALSQEEQSRQ HHHHHHCCHHHHHHH | 40.17 | 29136822 | |
| 635 | Phosphorylation | ALSQEEQSRQIEKIK HCCHHHHHHHHHHHH | 29.45 | 23749301 | |
| 652 | Phosphorylation | LAILDSASPLSQNGS HHHHHCCCCCCCCCC | 30.26 | 28889911 | |
| 659 | Phosphorylation | SPLSQNGSPGQIQSA CCCCCCCCCHHHCCH | 33.15 | 28889911 |
| 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 BDF1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BDF1_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 BDF1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| 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-65; THR-90; SER-92;SER-269; SER-270; SER-612; SER-613; SER-615; THR-617; SER-652 ANDSER-659, AND MASS SPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269 AND SER-270, ANDMASS SPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, AND MASSSPECTROMETRY. | |
| "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-270 AND SER-429, ANDMASS SPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, AND MASSSPECTROMETRY. | |
