| UniProt ID | YL345_YEAST | |
|---|---|---|
| UniProt AC | Q06137 | |
| Protein Name | Putative 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase YLR345W | |
| Gene Name | YLR345W | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 509 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Synthesis and degradation of fructose 2,6-bisphosphate.. | |
| Protein Sequence | MPNVLSDDEELLNGLGSEIMKPSRQGNHMARTVKRWVNKERATTADLKNVNIDGVHGPVNTESYISPGQLYSTDSGNLFHAGRILVVLVGLPATSKTLLSVAITRYTRWLGVRTKSFHFSEYKESAKNIPSDYFCVVPTSKEGVAFVEKLRMQMLNDILAFFNDLSGQLAIYDALNIRKIDRKNLETTFSEIGVKVLFIESIVSDQEIMNRNIALALESNDYKGLSTDEAIDEYMRRLSVNEPYYEMMTHDEELSYIKYINLGKQIIVKDNIHGYLVNKIVFFLMNLRQKKGCVYFARCGTSDKDNYIHDEELNEEGIHYSQVLKDFVLQRIKQKRQAKKNSDSLVEVIDGSHDEDLKTSLIVWTGPRKRTHDTALFFSKEGIKVQQRSELRQLNPGSIADLTDQQIMDKFPSEYKESLKDPYHFRFPRAESYHDLAVRMEPLLLEMEHTSKDILIIAHESTLRVLYGYLMACTCVELPNLNFTRDKLVEISFSPFCNTVELLNIPLTS | |
| 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 |
|---|---|---|---|---|---|
| 6 | Phosphorylation | --MPNVLSDDEELLN --CCCCCCCHHHHHH | 38.44 | 22369663 | |
| 17 | Phosphorylation | ELLNGLGSEIMKPSR HHHHHCCCCCCCCCC | 29.06 | 22369663 | |
| 21 | Acetylation | GLGSEIMKPSRQGNH HCCCCCCCCCCCCCH | 45.57 | 25381059 | |
| 23 | Phosphorylation | GSEIMKPSRQGNHMA CCCCCCCCCCCCHHH | 31.55 | 22369663 | |
| 72 | Phosphorylation | ISPGQLYSTDSGNLF CCCCCEEECCCCCCE | 34.04 | 30377154 | |
| 75 | Phosphorylation | GQLYSTDSGNLFHAG CCEEECCCCCCEECC | 29.66 | 28889911 | |
| 104 | Phosphorylation | TLLSVAITRYTRWLG HHHHHHHHHHHHHHC | 14.11 | 17563356 | |
| 149 | Acetylation | EGVAFVEKLRMQMLN HHHHHHHHHHHHHHH | 35.77 | 24489116 | |
| 190 | Phosphorylation | KNLETTFSEIGVKVL CCCCCCHHHHCCEEE | 26.64 | 28889911 | |
| 219 | Phosphorylation | NIALALESNDYKGLS HHHHHHHCCCCCCCC | 35.53 | 28889911 | |
| 344 | Phosphorylation | QAKKNSDSLVEVIDG HHHHCCCCCEEECCC | 33.85 | 28889911 | |
| 432 | Phosphorylation | FRFPRAESYHDLAVR CCCCCCCCHHHHHHH | 27.12 | 27214570 |
| 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 YL345_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of YL345_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 YL345_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-6; SER-75 AND SER-432,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 THR-104, AND MASSSPECTROMETRY. | |