| UniProt ID | BUR1_YEAST | |
|---|---|---|
| UniProt AC | P23293 | |
| Protein Name | Serine/threonine-protein kinase BUR1 | |
| Gene Name | SGV1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 657 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Serine/threonine-protein kinase component of the BUR kinase complex involved in transcription regulation. This complex phosphorylates 'Ser-120' of the UBC2/RAD6 ubiquitin-conjugating enzyme (E2), leading to monoubiquitination of histone H2B, the localization of the PAF1 complex to the chromatin, and the silencing of telomeric-associated genes. Also required for histone H3 'Lys-4' trimethylation. May phosphorylate the 'Ser-5' of the RBP1 carboxy-terminal domain (CTD) repeats. Necessary for the recovery from pheromone-induced growth arrest in the cell cycle G1 phase. The kinase activity of the complex requires the presence of BUR2.. | |
| Protein Sequence | MSDNGSPAVLPKTEFNKYKIGKVKSTPAIQRDAKTNLTYIKLRKRSSEKVYGCTVFQNHYREDEKLGQGTFGEVYKGIHLETQRQVAMKKIIVSVEKDLFPITAQREITILKRLNHKNIIKLIEMVYDHSPDITNAASSNLHKSFYMILPYMVADLSGVLHNPRINLEMCDIKNMMLQILEGLNYIHCAKFMHRDIKTANILIDHNGVLKLADFGLARLYYGCPPNLKYPGGAGSGAKYTSVVVTRWYRAPELVLGDKQYTTAVDIWGVGCVFAEFFEKKPILQGKTDIDQGHVIFKLLGTPTEEDWAVARYLPGAELTTTNYKPTLRERFGKYLSETGLDFLGQLLALDPYKRLTAMSAKHHPWFKEDPLPSEKITLPTEESHEADIKRYKEEMHQSLSQRVPTAPRGHIVEKGESPVVKNLGAIPRGPKKDDASFLPPSKNVLAKPPPSKIRELHQNPRPYHVNSGYAKTAIPPPAAPAGVNRYGPNNSSRNNRFSGNSTAPNNSRNPVNRFHPETNVSSKYNKVPLPLGPQSRYQGNSNESRYKNSPNDSRYHNPRYVNKPETNFNRQPQKYSRQESNAPINKNYNPSNGSRNMAGDHHQGSRPSHPQFPISPSQGQHQLTSKPIEKKNGSFKDERAKPDESKEFQNSDIADLY | |
| 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 | ------MSDNGSPAV ------CCCCCCCCC | 39.52 | 28132839 | |
| 6 | Phosphorylation | --MSDNGSPAVLPKT --CCCCCCCCCCCCC | 18.88 | 28152593 | |
| 25 | Phosphorylation | YKIGKVKSTPAIQRD EECCCCCCCCCCCCC | 42.48 | 28889911 | |
| 127 | Phosphorylation | IKLIEMVYDHSPDIT HHHHHHHHHCCCCCC | 13.46 | 21440633 | |
| 235 | Phosphorylation | KYPGGAGSGAKYTSV CCCCCCCCCCCEEEE | 34.74 | 28889911 | |
| 239 | Phosphorylation | GAGSGAKYTSVVVTR CCCCCCCEEEEEEEE | 12.06 | 22890988 | |
| 240 | Phosphorylation | AGSGAKYTSVVVTRW CCCCCCEEEEEEEEE | 17.84 | 22369663 | |
| 241 | Phosphorylation | GSGAKYTSVVVTRWY CCCCCEEEEEEEEEE | 15.15 | 22890988 | |
| 245 | Phosphorylation | KYTSVVVTRWYRAPE CEEEEEEEEEEECCE | 12.13 | 22890988 | |
| 297 | Ubiquitination | DQGHVIFKLLGTPTE CCCCHHEEECCCCCH | 31.51 | 15699485 | |
| 324 | Ubiquitination | ELTTTNYKPTLRERF CCCCCCCCHHHHHHH | 33.33 | 15699485 | |
| 334 | Phosphorylation | LRERFGKYLSETGLD HHHHHHHHHHHHCCH | 18.81 | 30377154 | |
| 336 | Phosphorylation | ERFGKYLSETGLDFL HHHHHHHHHHCCHHH | 29.98 | 30377154 | |
| 338 | Phosphorylation | FGKYLSETGLDFLGQ HHHHHHHHCCHHHHH | 39.40 | 30377154 | |
| 352 | Phosphorylation | QLLALDPYKRLTAMS HHHCCCHHHHHHHHH | 14.38 | 30377154 | |
| 389 | Acetylation | ESHEADIKRYKEEMH HHHHHHHHHHHHHHH | 50.66 | 24489116 | |
| 391 | Phosphorylation | HEADIKRYKEEMHQS HHHHHHHHHHHHHHH | 20.11 | 28889911 | |
| 398 | Phosphorylation | YKEEMHQSLSQRVPT HHHHHHHHHHHCCCC | 18.47 | 25005228 | |
| 400 | Phosphorylation | EEMHQSLSQRVPTAP HHHHHHHHHCCCCCC | 22.61 | 19823750 | |
| 405 | Phosphorylation | SLSQRVPTAPRGHIV HHHHCCCCCCCCCEE | 46.57 | 19823750 | |
| 414 | Acetylation | PRGHIVEKGESPVVK CCCCEECCCCCCCEE | 58.02 | 22865919 | |
| 417 | Phosphorylation | HIVEKGESPVVKNLG CEECCCCCCCEECCC | 31.50 | 25521595 | |
| 421 | Acetylation | KGESPVVKNLGAIPR CCCCCCEECCCCCCC | 46.84 | 22865919 | |
| 467 | Phosphorylation | PRPYHVNSGYAKTAI CCCCCCCCCCCCCCC | 31.90 | 30377154 | |
| 486 | Phosphorylation | APAGVNRYGPNNSSR CCCCCCCCCCCCCCC | 31.56 | 19779198 | |
| 502 | Phosphorylation | NRFSGNSTAPNNSRN CCCCCCCCCCCCCCC | 50.57 | 28889911 | |
| 523 | Acetylation | PETNVSSKYNKVPLP CCCCCCCCCCCCCCC | 45.39 | 24489116 | |
| 563 | Acetylation | HNPRYVNKPETNFNR CCCCCCCCCCCCCCC | 33.90 | 24489116 | |
| 574 | Acetylation | NFNRQPQKYSRQESN CCCCCCCCCCCCCCC | 52.45 | 25381059 | |
| 580 | Phosphorylation | QKYSRQESNAPINKN CCCCCCCCCCCCCCC | 29.92 | 21551504 | |
| 586 | Acetylation | ESNAPINKNYNPSNG CCCCCCCCCCCCCCC | 62.62 | 25381059 | |
| 615 | Phosphorylation | SHPQFPISPSQGQHQ CCCCCCCCCCCCCCC | 20.80 | 25704821 | |
| 634 | Phosphorylation | PIEKKNGSFKDERAK CHHHCCCCCCCCCCC | 38.22 | 28889911 | |
| 636 | Acetylation | EKKNGSFKDERAKPD HHCCCCCCCCCCCCC | 61.45 | 25381059 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 240 | T | Phosphorylation | Kinase | CDK7 | - | GPS |
| 240 | T | Phosphorylation | Kinase | CAK | - | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BUR1_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 BUR1_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 THR-240; SER-417 ANDSER-634, 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-417, AND MASSSPECTROMETRY. | |
| "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-400 AND THR-405, 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-417, AND MASSSPECTROMETRY. | |
| "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-241, AND MASSSPECTROMETRY. | |
| "Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-240, AND MASSSPECTROMETRY. | |
| "Activation of the Bur1-Bur2 cyclin-dependent kinase complex byCak1."; Yao S., Prelich G.; Mol. Cell. Biol. 22:6750-6758(2002). Cited for: PHOSPHORYLATION AT THR-240, MUTAGENESIS OF THR-240, AND FUNCTION. | |
