UniProt ID | CG12_YEAST | |
---|---|---|
UniProt AC | P20438 | |
Protein Name | G1/S-specific cyclin CLN2 | |
Gene Name | CLN2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 545 | |
Subcellular Localization | ||
Protein Description | Essential for the control of the cell cycle at the G1/S (start) transition. Interacts with the CDC28 protein kinase to form MPF.. | |
Protein Sequence | MASAEPRPRMGLVINAKPDYYPIELSNAELLSHFEMLQEYHQEISTNVIAQSCKFKPNPKLIDQQPEMNPVETRSNIITFLFELSVVTRVTNGIFFHSVRLYDRYCSKRIVLRDQAKLVVATCLWLAAKTWGGCNHIINNVVIPTGGRFYGPNPRARIPRLSELVHYCGDGQVFDESMFLQMERHILDTLNWNIYEPMINDYVLNVDENCLMQYELYENQVTYDKQCSEKRQSQLSQDSDATVDERPYQNEEEEEEDLKLKIKLINLKKFLIDVSAWQYDLLRYELFEVSHGIFSIINQFTNQDHGPFLMTPMTSESKNGEILSTLMNGIVSIPNSLMEVYKTVNGVLPFINQVKEYHLDLQRKLQIASNLNISRKLTISTPSCSFENSNSTSIPSPASSSQSHTPMRNMSSLSDNSVFSRNMEQSSPITPSMYQFGQQQSNSICGSTVSVNSLVNTNNKQRIYEQITGPNSNNATNDYIDLLNLNESNKENQNPATAHYLNGGPPKTSFINHGMFPSPTGTINSGKSSSASSLISFGMGNTQVI | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
60 | Ubiquitination | CKFKPNPKLIDQQPE CCCCCCHHHCCCCCC | 65.79 | 17644757 | |
129 | Ubiquitination | TCLWLAAKTWGGCNH HHHHHHHHHHCCCCH | 38.92 | 17644757 | |
233 | Phosphorylation | QCSEKRQSQLSQDSD HHHHHHHHHHHCCCC | 36.80 | 28889911 | |
236 | Phosphorylation | EKRQSQLSQDSDATV HHHHHHHHCCCCCCC | 25.06 | 19795423 | |
239 | Phosphorylation | QSQLSQDSDATVDER HHHHHCCCCCCCCCC | 22.85 | 19795423 | |
242 | Phosphorylation | LSQDSDATVDERPYQ HHCCCCCCCCCCCCC | 33.22 | 24961812 | |
269 | Ubiquitination | IKLINLKKFLIDVSA HHHHCHHHHHHCHHH | 48.87 | 17644757 | |
311 | Phosphorylation | DHGPFLMTPMTSESK CCCCCEECCCCCCCC | 16.44 | 8756727 | |
342 | Ubiquitination | NSLMEVYKTVNGVLP CHHHHHHHHHHCHHH | 51.69 | 17644757 | |
355 | Ubiquitination | LPFINQVKEYHLDLQ HHHHHHHHHHCCHHH | 42.67 | 17644757 | |
364 | Ubiquitination | YHLDLQRKLQIASNL HCCHHHHHHHHHHHC | 31.61 | 17644757 | |
369 | Phosphorylation | QRKLQIASNLNISRK HHHHHHHHHCCCCCC | 43.40 | 21440633 | |
376 | Ubiquitination | SNLNISRKLTISTPS HHCCCCCCEEEECCC | 43.10 | 17644757 | |
381 | Phosphorylation | SRKLTISTPSCSFEN CCCEEEECCCCCCCC | 18.51 | 8756727 | |
396 | Phosphorylation | SNSTSIPSPASSSQS CCCCCCCCCCCCCCC | 31.28 | 8599119 | |
399 | Phosphorylation | TSIPSPASSSQSHTP CCCCCCCCCCCCCCC | 33.63 | 23749301 | |
400 | Phosphorylation | SIPSPASSSQSHTPM CCCCCCCCCCCCCCC | 34.21 | 23749301 | |
411 | Phosphorylation | HTPMRNMSSLSDNSV CCCCCCHHHCCCCCH | 31.51 | 23749301 | |
417 | Phosphorylation | MSSLSDNSVFSRNME HHHCCCCCHHCCCHH | 29.54 | 28889911 | |
427 | Phosphorylation | SRNMEQSSPITPSMY CCCHHCCCCCCHHHH | 21.73 | 8599119 | |
430 | Phosphorylation | MEQSSPITPSMYQFG HHCCCCCCHHHHCCC | 16.82 | 8756727 | |
464 | Phosphorylation | TNNKQRIYEQITGPN CCCCCCEEEECCCCC | 12.17 | 28889911 | |
468 | Phosphorylation | QRIYEQITGPNSNNA CCEEEECCCCCCCCC | 46.40 | 28889911 | |
472 | Phosphorylation | EQITGPNSNNATNDY EECCCCCCCCCCCCH | 34.30 | 28889911 | |
476 | Phosphorylation | GPNSNNATNDYIDLL CCCCCCCCCCHHHHH | 30.64 | 24961812 | |
479 | Phosphorylation | SNNATNDYIDLLNLN CCCCCCCHHHHHCCC | 9.82 | 21440633 | |
490 | Ubiquitination | LNLNESNKENQNPAT HCCCCCCCCCCCHHH | 68.28 | 17644757 | |
507 | Ubiquitination | YLNGGPPKTSFINHG HHCCCCCCCCCCCCC | 60.99 | 17644757 | |
518 | Phosphorylation | INHGMFPSPTGTINS CCCCCCCCCCCCCCC | 24.67 | 23749301 | |
525 | Phosphorylation | SPTGTINSGKSSSAS CCCCCCCCCCCCCHH | 43.69 | 23749301 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CG12_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 CG12_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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