| UniProt ID | BUD32_YEAST | |
|---|---|---|
| UniProt AC | P53323 | |
| Protein Name | EKC/KEOPS complex subunit BUD32 | |
| Gene Name | BUD32 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 261 | |
| Subcellular Localization | Cytoplasm . Nucleus . Chromosome, telomere . | |
| Protein Description | Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators. Important for bud site selection.. | |
| Protein Sequence | MTQEFIDKVSSYLTPDVDIAPISQGAEAIVFTTTTHPYLPRAKDSHQKYIIKYRPPKRYRHPQIDQALTKHRTLNESRLLAKLYLIPGLCVPQLIACDPYNGFIWLEFLGEDLPGGHGFSNLKNFLWMHDQDPYSDLVATTLRKVGRQIGLLHWNDYCHGDLTSSNIVLVRDGARWTPHLIDFGLGSVSNLVEDKGVDLYVLERAILSTHSKHAEKYNAWIMEGFEEVYREQGAKGAKKLKEVTKRFEEVRLRGRKRSMLG | |
| 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 |
|---|---|---|---|---|---|
| 187 | Phosphorylation | LIDFGLGSVSNLVED HHHCCCCCHHHHHHC | 27.67 | 28889911 | |
| 189 | Phosphorylation | DFGLGSVSNLVEDKG HCCCCCHHHHHHCCC | 26.58 | 28889911 | |
| 258 | Phosphorylation | RLRGRKRSMLG---- HHHHHHHHHCC---- | 22.76 | 28889911 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BUD32_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 BUD32_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Structure-function analysis of yeast piD261/Bud32, an atypicalprotein kinase essential for normal cell life."; Facchin S., Lopreiato R., Stocchetto S., Arrigoni G., Cesaro L.,Marin O., Carignani G., Pinna L.A.; Biochem. J. 364:457-463(2002). Cited for: PHOSPHORYLATION AT SER-187 AND SER-189, AND MUTAGENESIS OF SER-187 ANDSER-189. | |
