| UniProt ID | BOP2_YEAST | |
|---|---|---|
| UniProt AC | Q06150 | |
| Protein Name | Protein BOP2 | |
| Gene Name | BOP2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 570 | |
| Subcellular Localization | ||
| Protein Description | ||
| Protein Sequence | MVAALTYLPTELIQRIFEFTVVETDSQYWLYNLVALIDFSVSSRGGGSITEDFLTNYVRKNLMVLDLTCEATQDSILRAEYGFLKRLLPYIDMDAQYIRVVDLETNADKAQNLKAEKLIVIFDEFSDLKLIETFFPLANSNSNIIEFVFCVRNIKSSFYSPLEKLHIANIVADIDINTLYLDFVDSNIYSDQNFFGIFDPDIFQLINKNYRNFFSKTNEKGKKRPPICKKICFPFVETLNLDYMALDSFFNSILHKLTTKIKTFERNNEFDVDKNLNLNSTTTVAALIIKSILQQFFNNFHISFPNLVTLNFIKMSTYPNNNEITQCCNFIDLSSYVLNKCLSENISINFLFQLHSLKNWSMPKIKEFTGHKFKYDETTFSGSPERYIKSLRGNIKILQEMAINETNDGTCYFRVKLIPEGVEKTQIINWIPFTSSFSDDTFKQRHHLKRPMICLKNNSLRSLTVKIIRIEKCSSIRIQGFYLPNLQELFINNTLCDTTQHQKQASNDMSCIEFTSWNELPQCKKLGFAQLEDDSNYVLNISNLQDHLPNLDLRESFPTFFDIRQKFVVV | |
| 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 |
|---|---|---|---|---|---|
| 85 | Acetylation | RAEYGFLKRLLPYID HHHHHHHHHHHHHCC | 38.44 | 22865919 | |
| 155 | Acetylation | VFCVRNIKSSFYSPL EEEHHCCCCCCCCHH | 43.53 | 22865919 | |
| 343 | Phosphorylation | YVLNKCLSENISINF HHHHHHHCCCCCEEH | 37.76 | 25521595 | |
| 356 | Phosphorylation | NFLFQLHSLKNWSMP EHHHHHHHCCCCCCC | 50.02 | 25521595 | |
| 378 | Phosphorylation | HKFKYDETTFSGSPE CCCCCCCCCCCCCHH | 30.18 | 24961812 | |
| 379 | Phosphorylation | KFKYDETTFSGSPER CCCCCCCCCCCCHHH | 17.47 | 28889911 | |
| 381 | Phosphorylation | KYDETTFSGSPERYI CCCCCCCCCCHHHHH | 35.95 | 29136822 | |
| 383 | Phosphorylation | DETTFSGSPERYIKS CCCCCCCCHHHHHHH | 23.53 | 24961812 |
| 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 BOP2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BOP2_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 BOP2_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 THR-379 AND SER-383, ANDMASS 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-383, AND MASSSPECTROMETRY. | |