| UniProt ID | CBF1_YEAST | |
|---|---|---|
| UniProt AC | P17106 | |
| Protein Name | Centromere-binding protein 1 | |
| Gene Name | CBF1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 351 | |
| Subcellular Localization | Nucleus . Mitochondrion . Chromosome, centromere . | |
| Protein Description | Required for chromosome stability and methionine prototrophy. It is involved in chromosomal segregation. Binds to a highly conserved DNA sequence (5'-RTCACRTG-3'), called CDEI, found in centromeres and in several promoters. DNA-binding activity is enhanced by MET28. Required as an auxiliary factor for transcriptional activation of sulfur metabolism together with MET4 and MET28.. | |
| Protein Sequence | MNSLANNNKLSTEDEEIHSARKRGYNEEQNYSEARKKQRDQGLLSQESNDGNIDSALLSEGATLKGTQSQYESGLTSNKDEKGSDDEDASVAEAAVAATVNYTDLIQGQEDSSDAHTSNQTNANGEHKDSLNGERAITPSNEGVKPNTSLEGMTSSPMESTQQSKNDMLIPLAEHDRGPEHQQDDEDNDDADIDLKKDISMQPGRRGRKPTTLATTDEWKKQRKDSHKEVERRRRENINTAINVLSDLLPVRESSKAAILACAAEYIQKLKETDEANIEKWTLQKLLSEQNASQLASANEKLQEELGNAYKEIEYMKRVLRKEGIEYEDMHTHKKQENERKSTRSDNPHEA | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MNSLANNN -------CCCCCCCC | 7.49 | 22814378 | |
| 9 | Acetylation | NSLANNNKLSTEDEE CCCCCCCCCCCCHHH | 46.03 | 24489116 | |
| 11 | Phosphorylation | LANNNKLSTEDEEIH CCCCCCCCCCHHHHH | 31.21 | 30377154 | |
| 12 | Phosphorylation | ANNNKLSTEDEEIHS CCCCCCCCCHHHHHH | 58.87 | 30377154 | |
| 19 | Phosphorylation | TEDEEIHSARKRGYN CCHHHHHHHHHHCCC | 35.12 | 23749301 | |
| 32 | Phosphorylation | YNEEQNYSEARKKQR CCHHCCHHHHHHHHH | 32.12 | 30377154 | |
| 45 | Phosphorylation | QRDQGLLSQESNDGN HHHHCHHCCCCCCCC | 36.62 | 22369663 | |
| 48 | Phosphorylation | QGLLSQESNDGNIDS HCHHCCCCCCCCCCH | 32.36 | 22369663 | |
| 55 | Phosphorylation | SNDGNIDSALLSEGA CCCCCCCHHHHHCCC | 19.61 | 22369663 | |
| 59 | Phosphorylation | NIDSALLSEGATLKG CCCHHHHHCCCCCCC | 34.53 | 22369663 | |
| 63 | Phosphorylation | ALLSEGATLKGTQSQ HHHHCCCCCCCCHHH | 39.60 | 22369663 | |
| 67 | Phosphorylation | EGATLKGTQSQYESG CCCCCCCCHHHHHCC | 24.37 | 22369663 | |
| 69 | Phosphorylation | ATLKGTQSQYESGLT CCCCCCHHHHHCCCC | 34.27 | 22369663 | |
| 73 | Phosphorylation | GTQSQYESGLTSNKD CCHHHHHCCCCCCCC | 33.88 | 22369663 | |
| 76 | Phosphorylation | SQYESGLTSNKDEKG HHHHCCCCCCCCCCC | 33.50 | 22369663 | |
| 77 | Phosphorylation | QYESGLTSNKDEKGS HHHCCCCCCCCCCCC | 47.10 | 22369663 | |
| 84 | Phosphorylation | SNKDEKGSDDEDASV CCCCCCCCCCHHHHH | 53.62 | 27214570 | |
| 130 | Phosphorylation | ANGEHKDSLNGERAI CCCCCCCCCCCCCCC | 28.65 | 20377248 | |
| 138 | Phosphorylation | LNGERAITPSNEGVK CCCCCCCCCCCCCCC | 21.49 | 22369663 | |
| 140 | Phosphorylation | GERAITPSNEGVKPN CCCCCCCCCCCCCCC | 38.57 | 22369663 | |
| 148 | Phosphorylation | NEGVKPNTSLEGMTS CCCCCCCCCCCCCCC | 43.12 | 22369663 | |
| 149 | Phosphorylation | EGVKPNTSLEGMTSS CCCCCCCCCCCCCCC | 30.94 | 22369663 | |
| 154 | Phosphorylation | NTSLEGMTSSPMEST CCCCCCCCCCCCCCC | 36.59 | 22369663 | |
| 155 | Phosphorylation | TSLEGMTSSPMESTQ CCCCCCCCCCCCCCC | 24.45 | 22369663 | |
| 156 | Phosphorylation | SLEGMTSSPMESTQQ CCCCCCCCCCCCCCC | 21.06 | 22369663 | |
| 160 | Phosphorylation | MTSSPMESTQQSKND CCCCCCCCCCCCCCC | 25.84 | 22890988 | |
| 161 | Phosphorylation | TSSPMESTQQSKNDM CCCCCCCCCCCCCCC | 19.81 | 22890988 | |
| 164 | Phosphorylation | PMESTQQSKNDMLIP CCCCCCCCCCCCEEC | 24.49 | 22890988 | |
| 200 | Phosphorylation | IDLKKDISMQPGRRG CCHHHHHCCCCCCCC | 22.84 | 30377154 | |
| 211 | Phosphorylation | GRRGRKPTTLATTDE CCCCCCCCCCCCHHH | 37.16 | 28889911 | |
| 226 | Phosphorylation | WKKQRKDSHKEVERR HHHHHHHHHHHHHHH | 39.22 | 30377154 | |
| 228 | Acetylation | KQRKDSHKEVERRRR HHHHHHHHHHHHHHH | 68.36 | 25381059 | |
| 254 | Phosphorylation | DLLPVRESSKAAILA HHCCCCCHHHHHHHH | 26.95 | 30377154 | |
| 269 | Ubiquitination | CAAEYIQKLKETDEA HHHHHHHHHHHCCHH | 52.55 | 22817900 | |
| 271 | Ubiquitination | AEYIQKLKETDEANI HHHHHHHHHCCHHHH | 66.65 | 23749301 | |
| 280 | Acetylation | TDEANIEKWTLQKLL CCHHHHHHHHHHHHH | 41.50 | 24489116 | |
| 297 | Phosphorylation | QNASQLASANEKLQE CCHHHHHHHHHHHHH | 39.97 | 30377154 | |
| 311 | Acetylation | EELGNAYKEIEYMKR HHHHHHHHHHHHHHH | 50.21 | 22865919 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CBF1_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 CBF1_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-45; SER-48; SER-84;THR-138; SER-140; SER-149; THR-154 AND SER-156, 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-45; SER-48; THR-148;SER-155 AND SER-156, AND MASS 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 THR-138, AND MASSSPECTROMETRY. | |
