| UniProt ID | SPT2_YEAST | |
|---|---|---|
| UniProt AC | P06843 | |
| Protein Name | Protein SPT2 | |
| Gene Name | SPT2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 333 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Histone chaperone that stabilizes pre-existing histone tetramers and regulates replication-independent histone exchange on chromatin. [PubMed: 26109053 Required for normal chromatin refolding in the coding region of transcribed genes, and for the suppression of spurious transcription] | |
| Protein Sequence | MSFLSKLSQIRKSTTASKAQVQDPLPKKNDEEYSLLPKNYIRDEDPAVKRLKELRRQELLKNGALAKKSGVKRKRGTSSGSEKKKIERNDDDEGGLGIRFKRSIGASHAPLKPVVRKKPEPIKKMSFEELMKQAENNEKQPPKVKSSEPVTKERPHFNKPGFKSSKRPQKKASPGATLRGVSSGGNSIKSSDSPKPVKLNLPTNGFAQPNRRLKEKLESRKQKSRYQDDYDEEDNDMDDFIEDDEDEGYHSKSKHSNGPGYDRDEIWAMFNRGKKRSEYDYDELEDDDMEANEMEILEEEEMARKMARLEDKREEAWLKKHEEEKRRRKKGIR | |
| 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 | ------MSFLSKLSQ ------CCHHHHHHH | 34.59 | 22814378 | |
| 6 | Acetylation | --MSFLSKLSQIRKS --CCHHHHHHHHHHH | 55.06 | 24489116 | |
| 40 | Phosphorylation | YSLLPKNYIRDEDPA HCCCCHHHCCCCCHH | 11.94 | 28889911 | |
| 49 | Acetylation | RDEDPAVKRLKELRR CCCCHHHHHHHHHHH | 54.87 | 25381059 | |
| 103 | Phosphorylation | LGIRFKRSIGASHAP CCCEEEEECCCCCCC | 26.43 | 30377154 | |
| 126 | Phosphorylation | PEPIKKMSFEELMKQ CCCCCCCCHHHHHHH | 38.08 | 22369663 | |
| 146 | Phosphorylation | KQPPKVKSSEPVTKE CCCCCCCCCCCCCCC | 42.81 | 28889911 | |
| 173 | Phosphorylation | KRPQKKASPGATLRG CCCCCCCCCCCEECC | 32.52 | 19823750 | |
| 177 | Phosphorylation | KKASPGATLRGVSSG CCCCCCCEECCCCCC | 23.93 | 21440633 | |
| 182 | Phosphorylation | GATLRGVSSGGNSIK CCEECCCCCCCCCCC | 26.53 | 19823750 | |
| 183 | Phosphorylation | ATLRGVSSGGNSIKS CEECCCCCCCCCCCC | 48.60 | 19823750 | |
| 187 | Phosphorylation | GVSSGGNSIKSSDSP CCCCCCCCCCCCCCC | 34.37 | 19823750 | |
| 190 | Phosphorylation | SGGNSIKSSDSPKPV CCCCCCCCCCCCCCE | 37.39 | 30377154 | |
| 191 | Phosphorylation | GGNSIKSSDSPKPVK CCCCCCCCCCCCCEE | 36.79 | 29136822 | |
| 193 | Phosphorylation | NSIKSSDSPKPVKLN CCCCCCCCCCCEEEC | 36.45 | 29136822 | |
| 216 | Acetylation | PNRRLKEKLESRKQK CCHHHHHHHHHHHHH | 56.84 | 25381059 |
| 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 SPT2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SPT2_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 SPT2_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 TYR-40; SER-126 AND SER-173,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 SER-173, AND MASSSPECTROMETRY. | |
