UniProt ID | CG23_YEAST | |
---|---|---|
UniProt AC | P24870 | |
Protein Name | G2/mitotic-specific cyclin-3 | |
Gene Name | CLB3 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 427 | |
Subcellular Localization | ||
Protein Description | Essential for the control of the cell cycle at the G2/M (mitosis) transition. Interacts with the CDC2 protein kinase to form MPF. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed at mitosis.. | |
Protein Sequence | MHHNSQSLSSGHIRSPEDENVAPIGNLKHRTGSLSHISSAHPRVALSDVTNIVATNSSNNSISKPKVAPIKERLDSAAIIEEERLDANSVAQRKEADHNDLLTDREQEEPVEDDGESEEDEEEDQEPLLLQHYASDTLVWEHAFRTYYRTTLDPNDDDVYDVVMVAELSNEIFEYMRKLEDLYKPNPYYMDKQPELRWSFRSTLIDWIVQVHEKFQLLPETLYLCINIIDRYLCKEVVPVNKFQLVGAASLFIAAKYEEINCPTIKDFVYMSENCYSRNDLLDAERTILNGLEFELGWPGPMSFLRRISKADDYEHDTRTLAKYLLESTIMDHRLVSAQPSWLAAGAYFLSKIILGQNQWSLAHVYYSNYTQEQILPLATIILENCRYASKRHNAIWRKYSSRRYLHSSQIVAKWIALAEHRVERSN | |
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 |
---|---|---|---|---|---|
5 | Phosphorylation | ---MHHNSQSLSSGH ---CCCCCCCCCCCC | 19.45 | 30377154 | |
7 | Phosphorylation | -MHHNSQSLSSGHIR -CCCCCCCCCCCCCC | 30.00 | 28889911 | |
10 | Phosphorylation | HNSQSLSSGHIRSPE CCCCCCCCCCCCCCC | 39.42 | 24961812 | |
15 | Phosphorylation | LSSGHIRSPEDENVA CCCCCCCCCCCCCCC | 31.85 | 28889911 | |
31 | Phosphorylation | IGNLKHRTGSLSHIS CCCCCCCCCCHHHHH | 30.73 | 28889911 | |
33 | Phosphorylation | NLKHRTGSLSHISSA CCCCCCCCHHHHHCC | 26.53 | 21082442 | |
50 | Phosphorylation | RVALSDVTNIVATNS CEEHHHCCEEEEECC | 24.99 | 30377154 | |
57 | Phosphorylation | TNIVATNSSNNSISK CEEEEECCCCCCCCC | 30.04 | 28889911 | |
58 | Phosphorylation | NIVATNSSNNSISKP EEEEECCCCCCCCCC | 41.94 | 28889911 | |
61 | Phosphorylation | ATNSSNNSISKPKVA EECCCCCCCCCCCCC | 32.27 | 21082442 | |
63 | Phosphorylation | NSSNNSISKPKVAPI CCCCCCCCCCCCCCH | 42.60 | 21082442 | |
89 | Phosphorylation | EERLDANSVAQRKEA HHHCCHHHHHHHHHC | 22.13 | 28889911 | |
103 | Phosphorylation | ADHNDLLTDREQEEP CCCCCCCCHHHCCCC | 40.06 | 25704821 | |
323 | Acetylation | HDTRTLAKYLLESTI CCHHHHHHHHHHHCC | 39.27 | 24489116 | |
352 | Ubiquitination | AGAYFLSKIILGQNQ HHHHHHHHHHHCCCC | 35.59 | 17644757 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CG23_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 CG23_YEAST !! |
Kegg Drug | ||||||
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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-33, AND MASSSPECTROMETRY. |