| UniProt ID | FKBP_YEAST | |
|---|---|---|
| UniProt AC | P20081 | |
| Protein Name | FK506-binding protein 1 | |
| Gene Name | FPR1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 114 | |
| Subcellular Localization | Cytoplasm. | |
| Protein Description | PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.. | |
| Protein Sequence | MSEVIEGNVKIDRISPGDGATFPKTGDLVTIHYTGTLENGQKFDSSVDRGSPFQCNIGVGQVIKGWDVGIPKLSVGEKARLTIPGPYAYGPRGFPGLIPPNSTLVFDVELLKVN | |
| 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 | Acetylation | ------MSEVIEGNV ------CCCEEECCE | 40.34 | 22814378 | |
| 2 | Phosphorylation | ------MSEVIEGNV ------CCCEEECCE | 40.34 | 24909858 | |
| 10 | Succinylation | EVIEGNVKIDRISPG CEEECCEEECEECCC | 42.78 | 23954790 | |
| 15 | Phosphorylation | NVKIDRISPGDGATF CEEECEECCCCCCCC | 24.59 | 21440633 | |
| 24 | Acetylation | GDGATFPKTGDLVTI CCCCCCCCCCCEEEE | 62.03 | 24489116 | |
| 33 | Phosphorylation | GDLVTIHYTGTLENG CCEEEEEEEEEECCC | 11.74 | 22369663 | |
| 34 | Phosphorylation | DLVTIHYTGTLENGQ CEEEEEEEEEECCCC | 14.99 | 22369663 | |
| 36 | Phosphorylation | VTIHYTGTLENGQKF EEEEEEEEECCCCEE | 24.09 | 22369663 | |
| 42 | Ubiquitination | GTLENGQKFDSSVDR EEECCCCEECCCCCC | 53.16 | 23749301 | |
| 45 | Phosphorylation | ENGQKFDSSVDRGSP CCCCEECCCCCCCCC | 35.08 | 22369663 | |
| 46 | Phosphorylation | NGQKFDSSVDRGSPF CCCEECCCCCCCCCE | 29.86 | 20377248 | |
| 51 | Phosphorylation | DSSVDRGSPFQCNIG CCCCCCCCCEECEEC | 24.36 | 22369663 | |
| 64 | Ubiquitination | IGVGQVIKGWDVGIP ECCCCEECCEECCCC | 55.91 | 23749301 | |
| 72 | Acetylation | GWDVGIPKLSVGEKA CEECCCCCCCCCCCE | 52.02 | 24489116 | |
| 78 | 2-Hydroxyisobutyrylation | PKLSVGEKARLTIPG CCCCCCCCEEEECCC | 32.64 | - |
| 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 FKBP_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FKBP_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 FKBP_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-46 AND SER-51, AND MASSSPECTROMETRY. | |
| "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-51, AND MASSSPECTROMETRY. | |
