| UniProt ID | MSC1_YEAST | |
|---|---|---|
| UniProt AC | Q03104 | |
| Protein Name | Meiotic sister chromatid recombination protein 1 | |
| Gene Name | MSC1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 513 | |
| Subcellular Localization | ||
| Protein Description | ||
| Protein Sequence | MKQFKLVNAVSASFVLIGLVLANSDSVFDKWTQEDLADYLRDNKKSLEKYATDSIEDLKTEASQVWDKHAQPKPWWQVWSSDSSSVSNSNPGWFGYTGSSDHPVSDWLFDTWSTDSLRNFLKKNGVDVDDAKASKDSLVKTAKENFNKISKSLKSSGYYPSSSYFDSWSTKDLQNWLNDNGIDYDKAVQSKDELVQKVKENIYRTSEKAEQQRLGLLESLDLAHQQILDTSGQIKDTVFDKWSSDQLTNWLESHKVNIDKNMAKKHDYLVRMAKENSANLKDDIYWYLDYMKRESSPFLTKTPEYVGSVWDSSKNFLTNLYSKFRGKTDNVINDTFLVGLDSWPKDKLKMFLDARGIKYSMLSTEHQLRELVKKSRNEKLKILPKDYQKYFDNSNWSLDDIKGWFADKKDDFQDSQTYSTIMQDFDKVSKNTNDAKDQIAKTWSNTFQSWSQEDLLQYLKSFGVPVKQTSTKDDLINLAKQNTQWLFGTVKEPAYKRYLHNVKNWSKSILGFN | |
| 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 |
|---|---|---|---|---|---|
| 49 | Ubiquitination | DNKKSLEKYATDSIE HCHHHHHHHCCCCHH | 45.54 | 17644757 | |
| 52 | Phosphorylation | KSLEKYATDSIEDLK HHHHHHCCCCHHHHH | 27.47 | 30377154 | |
| 54 | Phosphorylation | LEKYATDSIEDLKTE HHHHCCCCHHHHHHH | 24.43 | 30377154 | |
| 59 | Ubiquitination | TDSIEDLKTEASQVW CCCHHHHHHHHHHHH | 57.55 | 17644757 | |
| 68 | Ubiquitination | EASQVWDKHAQPKPW HHHHHHHHCCCCCCC | 25.73 | 17644757 | |
| 68 | Acetylation | EASQVWDKHAQPKPW HHHHHHHHCCCCCCC | 25.73 | 22865919 | |
| 132 | Acetylation | GVDVDDAKASKDSLV CCCHHHHHHCHHHHH | 61.25 | 24489116 | |
| 134 | Phosphorylation | DVDDAKASKDSLVKT CHHHHHHCHHHHHHH | 35.97 | 19823750 | |
| 135 | 2-Hydroxyisobutyrylation | VDDAKASKDSLVKTA HHHHHHCHHHHHHHH | 57.08 | - | |
| 137 | Phosphorylation | DAKASKDSLVKTAKE HHHHCHHHHHHHHHH | 38.51 | 19823750 | |
| 154 | Ubiquitination | NKISKSLKSSGYYPS HHHHHHHHHCCCCCC | 50.06 | 17644757 | |
| 171 | Ubiquitination | YFDSWSTKDLQNWLN HHCCCCHHHHHHHHH | 51.42 | 17644757 | |
| 186 | Ubiquitination | DNGIDYDKAVQSKDE HCCCCHHHHHCCHHH | 44.20 | 17644757 | |
| 186 | Acetylation | DNGIDYDKAVQSKDE HCCCCHHHHHCCHHH | 44.20 | 24489116 | |
| 191 | 2-Hydroxyisobutyrylation | YDKAVQSKDELVQKV HHHHHCCHHHHHHHH | 37.82 | - | |
| 197 | 2-Hydroxyisobutyrylation | SKDELVQKVKENIYR CHHHHHHHHHHHHHH | 48.04 | - | |
| 199 | 2-Hydroxyisobutyrylation | DELVQKVKENIYRTS HHHHHHHHHHHHHCC | 52.67 | - | |
| 208 | 2-Hydroxyisobutyrylation | NIYRTSEKAEQQRLG HHHHCCHHHHHHHHH | 57.92 | - | |
| 237 | Phosphorylation | TSGQIKDTVFDKWSS CCCCCCCHHHHHCCH | 20.33 | 28889911 | |
| 243 | Phosphorylation | DTVFDKWSSDQLTNW CHHHHHCCHHHHHHH | 29.76 | 28889911 | |
| 265 | 2-Hydroxyisobutyrylation | IDKNMAKKHDYLVRM CCHHHHHHHHHHHHH | 31.97 | - | |
| 318 | Phosphorylation | DSSKNFLTNLYSKFR CCCCHHHHHHHHHHC | 21.02 | 26447709 | |
| 321 | Phosphorylation | KNFLTNLYSKFRGKT CHHHHHHHHHHCCCC | 16.34 | 26447709 | |
| 322 | Phosphorylation | NFLTNLYSKFRGKTD HHHHHHHHHHCCCCC | 28.60 | 26447709 | |
| 323 | Acetylation | FLTNLYSKFRGKTDN HHHHHHHHHCCCCCC | 26.06 | 24489116 | |
| 358 | Acetylation | FLDARGIKYSMLSTE HHHHHCCCHHHHCHH | 33.81 | 24489116 | |
| 389 | Acetylation | ILPKDYQKYFDNSNW CCCHHHHHHHCCCCC | 41.47 | 24489116 | |
| 394 | Phosphorylation | YQKYFDNSNWSLDDI HHHHHCCCCCCHHHH | 41.33 | 28889911 | |
| 397 | Phosphorylation | YFDNSNWSLDDIKGW HHCCCCCCHHHHCHH | 26.60 | 30377154 | |
| 436 | 2-Hydroxyisobutyrylation | SKNTNDAKDQIAKTW HCCCHHHHHHHHHHH | 53.69 | - | |
| 449 | Phosphorylation | TWSNTFQSWSQEDLL HHHHHHHCCCHHHHH | 25.22 | 30377154 | |
| 472 | Succinylation | PVKQTSTKDDLINLA CCCCCCCHHHHHHHH | 49.35 | 23954790 | |
| 472 | Acetylation | PVKQTSTKDDLINLA CCCCCCCHHHHHHHH | 49.35 | 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 MSC1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MSC1_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 MSC1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| Phosphorylation | |
| Reference | PubMed |
| "Profiling phosphoproteins of yeast mitochondria reveals a role ofphosphorylation in assembly of the ATP synthase."; Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.; Mol. Cell. Proteomics 6:1896-1906(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-237 AND SER-243, ANDMASS SPECTROMETRY. | |
