| UniProt ID | TBB_YEAST | |
|---|---|---|
| UniProt AC | P02557 | |
| Protein Name | Tubulin beta chain | |
| Gene Name | TUB2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 457 | |
| Subcellular Localization | Cytoplasm, cytoskeleton . Colocalizes with kinesin KIP3 at the plus ends of growing microtubules and along the microtubule lattice. | |
| Protein Description | Tubulin is the major constituent of microtubules. [PubMed: 28013290 It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.] | |
| Protein Sequence | MREIIHISTGQCGNQIGAAFWETICGEHGLDFNGTYHGHDDIQKERLNVYFNEASSGKWVPRSINVDLEPGTIDAVRNSAIGNLFRPDNYIFGQSSAGNVWAKGHYTEGAELVDSVMDVIRREAEGCDSLQGFQITHSLGGGTGSGMGTLLISKIREEFPDRMMATFSVLPSPKTSDTVVEPYNATLSVHQLVEHSDETFCIDNEALYDICQRTLKLNQPSYGDLNNLVSSVMSGVTTSLRYPGQLNSDLRKLAVNLVPFPRLHFFMVGYAPLTAIGSQSFRSLTVPELTQQMFDAKNMMAAADPRNGRYLTVAAFFRGKVSVKEVEDEMHKVQSKNSDYFVEWIPNNVQTAVCSVAPQGLDMAATFIANSTSIQELFKRVGDQFSAMFKRKAFLHWYTSEGMDELEFSEAESNMNDLVSEYQQYQEATVEDDEEVDENGDFGAPQNQDEPITENFE | |
| 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 |
|---|---|---|---|---|---|
| 58 | Acetylation | FNEASSGKWVPRSIN EECCCCCCCCCCEEE | 47.14 | 24489116 | |
| 103 | Ubiquitination | SAGNVWAKGHYTEGA CCCCEEECCCCCCCH | 30.43 | 17644757 | |
| 115 | Phosphorylation | EGAELVDSVMDVIRR CCHHHHHHHHHHHHH | 16.32 | 28889911 | |
| 252 | Ubiquitination | QLNSDLRKLAVNLVP CCCHHHHHHHHHHCC | 48.36 | 17644757 | |
| 270 | Phosphorylation | LHFFMVGYAPLTAIG CEEEEEEECCCEECC | 8.14 | 22369663 | |
| 274 | Phosphorylation | MVGYAPLTAIGSQSF EEEECCCEECCCCCH | 18.37 | 22369663 | |
| 278 | Phosphorylation | APLTAIGSQSFRSLT CCCEECCCCCHHCCC | 19.28 | 22369663 | |
| 280 | Phosphorylation | LTAIGSQSFRSLTVP CEECCCCCHHCCCHH | 25.07 | 22369663 | |
| 297 | Acetylation | TQQMFDAKNMMAAAD HHHHHHHHHHHHHCC | 47.42 | 24489116 | |
| 324 | Acetylation | FRGKVSVKEVEDEMH ECCCCEEHHHHHHHH | 48.84 | 24489116 | |
| 332 | Acetylation | EVEDEMHKVQSKNSD HHHHHHHHHHHCCCC | 40.43 | 24489116 | |
| 390 | Acetylation | DQFSAMFKRKAFLHW HHHHHHHHHHHHHHH | 39.65 | 24489116 |
| 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 TBB_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TBB_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 TBB_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-278 AND SER-280, ANDMASS SPECTROMETRY. | |
