UniProt ID | DOT1_YEAST | |
---|---|---|
UniProt AC | Q04089 | |
Protein Name | Histone-lysine N-methyltransferase, H3 lysine-79 specific | |
Gene Name | DOT1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 582 | |
Subcellular Localization | Nucleus . | |
Protein Description | Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones. Can bind to DNA (in vitro).. | |
Protein Sequence | MGGQESISNNNSDSFIMSSPNLDSQESSISPIDEKKGTDMQTKSLSSYSKGTLLSKQVQNLLEEANKYDPIYGSSLPRGFLRDRNTKGKDNGLVPLVEKVIPPIHKKTNNRNTRKKSSTTTKKDVKKPKAAKVKGKNGRTNHKHTPISKQEIDTAREKKPLKKGRANKKNDRDSPSSTFVDWNGPCLRLQYPLFDIEYLRSHEIYSGTPIQSISLRTNSPQPTSLTSDNDTSSVTTAKLQSILFSNYMEEYKVDFKRSTAIYNPMSEIGKLIEYSCLVFLPSPYAEQLKETILPDLNASFDNSDTKGFVNAINLYNKMIREIPRQRIIDHLETIDKIPRSFIHDFLHIVYTRSIHPQANKLKHYKAFSNYVYGELLPNFLSDVYQQCQLKKGDTFMDLGSGVGNCVVQAALECGCALSFGCEIMDDASDLTILQYEELKKRCKLYGMRLNNVEFSLKKSFVDNNRVAELIPQCDVILVNNFLFDEDLNKKVEKILQTAKVGCKIISLKSLRSLTYQINFYNVENIFNRLKVQRYDLKEDSVSWTHSGGEYYISTVMEDVDESLFSPAARGRRNRGTPVKYTR | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
43 | Ubiquitination | KGTDMQTKSLSSYSK CCCCCCHHHCCHHCH | 32.29 | 23749301 | |
50 | Ubiquitination | KSLSSYSKGTLLSKQ HHCCHHCHHHHHHHH | 47.91 | 23749301 | |
99 | Acetylation | GLVPLVEKVIPPIHK CCHHHHHHHCCCCCC | 37.68 | 24489116 | |
217 | Phosphorylation | IQSISLRTNSPQPTS CEEEEECCCCCCCCC | 45.39 | 30377154 | |
219 | Phosphorylation | SISLRTNSPQPTSLT EEEECCCCCCCCCCC | 25.05 | 25752575 | |
223 | Phosphorylation | RTNSPQPTSLTSDND CCCCCCCCCCCCCCC | 30.99 | 23749301 | |
224 | Phosphorylation | TNSPQPTSLTSDNDT CCCCCCCCCCCCCCC | 36.01 | 19779198 | |
226 | Phosphorylation | SPQPTSLTSDNDTSS CCCCCCCCCCCCCCC | 33.53 | 30377154 | |
231 | Phosphorylation | SLTSDNDTSSVTTAK CCCCCCCCCCCHHHH | 29.20 | 30377154 | |
232 | Phosphorylation | LTSDNDTSSVTTAKL CCCCCCCCCCHHHHH | 26.19 | 30377154 | |
238 | Ubiquitination | TSSVTTAKLQSILFS CCCCHHHHHHHHHHC | 44.99 | 17644757 | |
336 | Acetylation | DHLETIDKIPRSFIH HHHHHHHHCCHHHHH | 51.24 | 24489116 | |
576 | Phosphorylation | RGRRNRGTPVKYTR- CCCCCCCCCCCCCC- | 22.98 | 19684113 | |
579 | Acetylation | RNRGTPVKYTR---- CCCCCCCCCCC---- | 41.95 | 25381059 | |
580 | Phosphorylation | NRGTPVKYTR----- CCCCCCCCCC----- | 14.16 | 19684113 |
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 DOT1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DOT1_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 DOT1_YEAST !! |
Kegg Drug | ||||||
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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-219, AND MASSSPECTROMETRY. |