| UniProt ID | TRI1_YEAST | |
|---|---|---|
| UniProt AC | Q05024 | |
| Protein Name | Protein TRI1 | |
| Gene Name | TRI1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 226 | |
| Subcellular Localization | Cytoplasm . Nucleus . Nucleus, nucleolus . | |
| Protein Description | May be involved in transcription regulation.. | |
| Protein Sequence | MADINKYIPMVDAILSVSNPDEISPKRVRKALQILYSVNLDSQRKLINELILERFGDIQENPRVLIPKNDLISRDQELSLRLQKEEERPLRSTRKRKGKSESKSKRKKKKNDSPDSNSISVRKVLLSAPLQKFLGSEELPRTQVVKMIWQYIKEHDLQNPKDRREILCDEKMEPIFGKKMTMFSMNKLLTKHLFNPDEIVKHEEEQKQTPEKEIKLENESLPNLSG | |
| 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 |
|---|---|---|---|---|---|
| 24 | Phosphorylation | VSNPDEISPKRVRKA CCCCCCCCHHHHHHH | 23.48 | 21440633 | |
| 68 | Acetylation | NPRVLIPKNDLISRD CCCEEEECCCCCCCC | 56.98 | 24489116 | |
| 79 | Phosphorylation | ISRDQELSLRLQKEE CCCCHHHHHHHHHHH | 15.64 | 27214570 | |
| 100 | Phosphorylation | TRKRKGKSESKSKRK HHHHCCCCCCHHHHH | 56.63 | 28889911 | |
| 113 | Phosphorylation | RKKKKNDSPDSNSIS HHCCCCCCCCCCCHH | 39.75 | 22369663 | |
| 116 | Phosphorylation | KKNDSPDSNSISVRK CCCCCCCCCCHHHHH | 35.54 | 22369663 | |
| 178 | Acetylation | KMEPIFGKKMTMFSM CCCCCCCCCCCHHHH | 28.73 | 25381059 | |
| 179 | Acetylation | MEPIFGKKMTMFSMN CCCCCCCCCCHHHHH | 39.73 | 25381059 | |
| 201 | Sumoylation | FNPDEIVKHEEEQKQ CCHHHHHCCHHHHCC | 51.46 | - | |
| 201 | Sumoylation | FNPDEIVKHEEEQKQ CCHHHHHCCHHHHCC | 51.46 | - | |
| 209 | Phosphorylation | HEEEQKQTPEKEIKL CHHHHCCCCHHHHHC | 40.21 | 24961812 | |
| 215 | Sumoylation | QTPEKEIKLENESLP CCCHHHHHCCCCCCC | 51.33 | - | |
| 215 | Sumoylation | QTPEKEIKLENESLP CCCHHHHHCCCCCCC | 51.33 | - | |
| 220 | Phosphorylation | EIKLENESLPNLSG- HHHCCCCCCCCCCC- | 61.79 | 22369663 | |
| 225 | Phosphorylation | NESLPNLSG------ CCCCCCCCC------ | 49.44 | 22369663 |
| 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 TRI1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TRI1_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 TRI1_YEAST !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| SMT3_YEAST | SMT3 | physical | 18719252 | |
| LRP1_YEAST | LRP1 | genetic | 20093466 | |
| MRT4_YEAST | MRT4 | genetic | 20093466 | |
| SYT1_YEAST | SYT1 | genetic | 20093466 | |
| MRT4_YEAST | MRT4 | genetic | 27708008 | |
| NNK1_YEAST | NNK1 | genetic | 27708008 |
| 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-113 AND SER-225, ANDMASS SPECTROMETRY. | |
| Sumoylation | |
| Reference | PubMed |
| "Topoisomerase I-dependent viability loss in saccharomyces cerevisiaemutants defective in both SUMO conjugation and DNA repair."; Chen X.L., Silver H.R., Xiong L., Belichenko I., Adegite C.,Johnson E.S.; Genetics 177:17-30(2007). Cited for: SUMOYLATION AT LYS-201 AND LYS-215, AND MUTAGENESIS OF LYS-201 ANDLYS-215. | |
