| UniProt ID | WHI5_YEAST | |
|---|---|---|
| UniProt AC | Q12416 | |
| Protein Name | G1-specific transcriptional repressor WHI5 | |
| Gene Name | WHI5 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 295 | |
| Subcellular Localization | Cytoplasm . Nucleus . Shuttles in a cell cycle-regulated manner. Localizes to the nucleus, where it is associated with SBF-dependent promoters. In late G1 phase, phosphorylation by G1-specific cyclin-CDK causes its export to the cytoplasm. Eliminatio | |
| Protein Description | Transcriptional repressor that negatively regulates G1-specific, SBF- and MBF-dependent transcription. Binds via SBF to promoters of G1-specific genes to repress transcription in early G1. During G1, phosphorylated by cyclin-CDK CLN3-CDC28 and progressively hyperphosphorylated by CDK associated with other G1-cyclins, which leads to dissociation of WHI5 from SBF, activating SBF-dependent transcription in late G1. Elimination of CDK activity at the end of mitosis by the mitotic exit network (MEN) allows WHI5 to reassociate with SBF to again repress G1/S transcription.. | |
| Protein Sequence | MSLRTPKRSRTSDEQEQEQEQEQVQNPDTHVNNEHQQRPGPTTLLSTPVRLKNGFGTPSPPSPPGITKSITKSRRRPSTTSLQGIFMSPVNKRRVGITAHGRVYDHNDDGHESESEDDENEEENENQKKYDGHVSMPLLPPTTPKSRRSEVFLSPSPRLRSPPTAARRSTGERPIREISHTLRTRLNYALVKLQNGWTDKTLPELETELAPAVQTPPRRYHNRFPDSADAGTSAHTAFLQALGGHPPREEATAVETLMLLSSPTKKQQHRPVPATSAGEPTDETEPESDTEVETS | |
| 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 | ------MSLRTPKRS ------CCCCCCCCC | 26.93 | 19823750 | |
| 5 | Phosphorylation | ---MSLRTPKRSRTS ---CCCCCCCCCCCC | 38.15 | 19172996 | |
| 7 | Acetylation | -MSLRTPKRSRTSDE -CCCCCCCCCCCCHH | 63.49 | 25381059 | |
| 42 | Phosphorylation | HQQRPGPTTLLSTPV CCCCCCCCCEECCCE | 35.67 | 28132839 | |
| 46 | Phosphorylation | PGPTTLLSTPVRLKN CCCCCEECCCEECCC | 33.50 | 21440633 | |
| 47 | Phosphorylation | GPTTLLSTPVRLKNG CCCCEECCCEECCCC | 26.27 | 15210110 | |
| 57 | Phosphorylation | RLKNGFGTPSPPSPP ECCCCCCCCCCCCCC | 20.52 | ||
| 59 | Phosphorylation | KNGFGTPSPPSPPGI CCCCCCCCCCCCCCC | 49.64 | 22369663 | |
| 62 | Phosphorylation | FGTPSPPSPPGITKS CCCCCCCCCCCCCCC | 47.30 | 22369663 | |
| 67 | Phosphorylation | PPSPPGITKSITKSR CCCCCCCCCCCCCCC | 25.34 | 29136822 | |
| 71 | Phosphorylation | PGITKSITKSRRRPS CCCCCCCCCCCCCCC | 30.02 | 28889911 | |
| 73 | Phosphorylation | ITKSITKSRRRPSTT CCCCCCCCCCCCCCC | 23.52 | 24961812 | |
| 78 | Phosphorylation | TKSRRRPSTTSLQGI CCCCCCCCCCCCCEE | 42.37 | 22369663 | |
| 79 | Phosphorylation | KSRRRPSTTSLQGIF CCCCCCCCCCCCEEE | 24.08 | 22369663 | |
| 80 | Phosphorylation | SRRRPSTTSLQGIFM CCCCCCCCCCCEEEE | 31.60 | 22369663 | |
| 81 | Phosphorylation | RRRPSTTSLQGIFMS CCCCCCCCCCEEEEC | 20.84 | 22369663 | |
| 88 | Phosphorylation | SLQGIFMSPVNKRRV CCCEEEECCCCCCCE | 18.23 | 22369663 | |
| 104 | Phosphorylation | ITAHGRVYDHNDDGH EEEECEEECCCCCCC | 15.32 | 23749301 | |
| 113 | Phosphorylation | HNDDGHESESEDDEN CCCCCCCCCCCCCCC | 40.52 | 25533186 | |
| 115 | Phosphorylation | DDGHESESEDDENEE CCCCCCCCCCCCCHH | 56.45 | 25533186 | |
| 142 | Phosphorylation | SMPLLPPTTPKSRRS CCCCCCCCCCCCCCC | 54.51 | 21440633 | |
| 143 | Phosphorylation | MPLLPPTTPKSRRSE CCCCCCCCCCCCCCC | 34.20 | 21440633 | |
| 146 | Phosphorylation | LPPTTPKSRRSEVFL CCCCCCCCCCCCEEC | 33.84 | 28889911 | |
| 149 | Phosphorylation | TTPKSRRSEVFLSPS CCCCCCCCCEECCCC | 36.68 | 22890988 | |
| 154 | Phosphorylation | RRSEVFLSPSPRLRS CCCCEECCCCCCCCC | 16.33 | 22369663 | |
| 156 | Phosphorylation | SEVFLSPSPRLRSPP CCEECCCCCCCCCCC | 21.19 | 22369663 | |
| 161 | Phosphorylation | SPSPRLRSPPTAARR CCCCCCCCCCCHHHC | 39.56 | 25533186 | |
| 164 | Phosphorylation | PRLRSPPTAARRSTG CCCCCCCCHHHCCCC | 36.01 | 29136822 | |
| 169 | Phosphorylation | PPTAARRSTGERPIR CCCHHHCCCCCCCHH | 34.90 | 28889911 | |
| 201 | Phosphorylation | QNGWTDKTLPELETE HCCCCCCCHHHHHHH | 50.81 | 28132839 | |
| 207 | Phosphorylation | KTLPELETELAPAVQ CCHHHHHHHCCCCCC | 49.26 | 28132839 | |
| 215 | Phosphorylation | ELAPAVQTPPRRYHN HCCCCCCCCCCCCCC | 28.76 | 22369663 | |
| 252 | Phosphorylation | HPPREEATAVETLML CCCHHHHHHHHHHHH | 34.22 | 25704821 | |
| 262 | Phosphorylation | ETLMLLSSPTKKQQH HHHHHHCCCCCCCCC | 36.24 | 15210110 | |
| 275 | Phosphorylation | QHRPVPATSAGEPTD CCCCCCCCCCCCCCC | 17.03 | 19823750 | |
| 276 | Phosphorylation | HRPVPATSAGEPTDE CCCCCCCCCCCCCCC | 36.06 | 29136822 | |
| 281 | Phosphorylation | ATSAGEPTDETEPES CCCCCCCCCCCCCCC | 42.01 | 29136822 | |
| 284 | Phosphorylation | AGEPTDETEPESDTE CCCCCCCCCCCCCCC | 60.70 | 29136822 | |
| 288 | Phosphorylation | TDETEPESDTEVETS CCCCCCCCCCCCCCC | 61.62 | 25521595 | |
| 290 | Phosphorylation | ETEPESDTEVETS-- CCCCCCCCCCCCC-- | 51.73 | 19823750 | |
| 294 | Phosphorylation | ESDTEVETS------ CCCCCCCCC------ | 44.93 | 29136822 | |
| 295 | Phosphorylation | SDTEVETS------- CCCCCCCC------- | 25.39 | 29136822 |
| 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 WHI5_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of WHI5_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 WHI5_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-62; THR-67; SER-113;SER-115; SER-154; SER-156 AND SER-161, 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-59; SER-62; SER-113;SER-115; SER-161 AND SER-288, AND MASS 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-62, AND MASSSPECTROMETRY. | |
| "Cln3 activates G1-specific transcription via phosphorylation of theSBF bound repressor Whi5."; de Bruin R.A.M., McDonald W.H., Kalashnikova T.I., Yates J. III,Wittenberg C.; Cell 117:887-898(2004). Cited for: FUNCTION, PHOSPHORYLATION AT THR-47; SER-59; SER-62; SER-161 ANDSER-262, INTERACTION WITH SBF, AND MASS SPECTROMETRY. | |
