| UniProt ID | CYS3_YEAST | |
|---|---|---|
| UniProt AC | P31373 | |
| Protein Name | Cystathionine gamma-lyase | |
| Gene Name | CYS3 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 394 | |
| Subcellular Localization | Cytoplasm. | |
| Protein Description | ||
| Protein Sequence | MTLQESDKFATKAIHAGEHVDVHGSVIEPISLSTTFKQSSPANPIGTYEYSRSQNPNRENLERAVAALENAQYGLAFSSGSATTATILQSLPQGSHAVSIGDVYGGTHRYFTKVANAHGVETSFTNDLLNDLPQLIKENTKLVWIETPTNPTLKVTDIQKVADLIKKHAAGQDVILVVDNTFLSPYISNPLNFGADIVVHSATKYINGHSDVVLGVLATNNKPLYERLQFLQNAIGAIPSPFDAWLTHRGLKTLHLRVRQAALSANKIAEFLAADKENVVAVNYPGLKTHPNYDVVLKQHRDALGGGMISFRIKGGAEAASKFASSTRLFTLAESLGGIESLLEVPAVMTHGGIPKEAREASGVFDDLVRISVGIEDTDDLLEDIKQALKQATN | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MTLQESDKF ------CCCHHHHHH | 36.83 | 28889911 | |
| 25 | Phosphorylation | EHVDVHGSVIEPISL CCEECCCCEEEEEEC | 12.68 | 24961812 | |
| 39 | Phosphorylation | LSTTFKQSSPANPIG CCCCCCCCCCCCCCC | 38.59 | 22369663 | |
| 40 | Phosphorylation | STTFKQSSPANPIGT CCCCCCCCCCCCCCC | 26.07 | 22369663 | |
| 47 | Phosphorylation | SPANPIGTYEYSRSQ CCCCCCCCCCCCCCC | 17.56 | 22369663 | |
| 48 | Phosphorylation | PANPIGTYEYSRSQN CCCCCCCCCCCCCCC | 13.99 | 29136822 | |
| 50 | Phosphorylation | NPIGTYEYSRSQNPN CCCCCCCCCCCCCCC | 10.04 | 29136822 | |
| 51 | Phosphorylation | PIGTYEYSRSQNPNR CCCCCCCCCCCCCCH | 17.32 | 29136822 | |
| 113 | Ubiquitination | GTHRYFTKVANAHGV CCHHHHHEEHHHCCC | 29.47 | 23749301 | |
| 141 | Ubiquitination | QLIKENTKLVWIETP HHHHHCCEEEEEECC | 53.26 | 24961812 | |
| 141 | Acetylation | QLIKENTKLVWIETP HHHHHCCEEEEEECC | 53.26 | 24489116 | |
| 147 | Phosphorylation | TKLVWIETPTNPTLK CEEEEEECCCCCCCC | 26.69 | 24961812 | |
| 149 | Phosphorylation | LVWIETPTNPTLKVT EEEEECCCCCCCCCC | 62.34 | 24961812 | |
| 154 | Ubiquitination | TPTNPTLKVTDIQKV CCCCCCCCCCCHHHH | 45.63 | 24961812 | |
| 160 | Acetylation | LKVTDIQKVADLIKK CCCCCHHHHHHHHHH | 39.46 | 24489116 | |
| 166 | Succinylation | QKVADLIKKHAAGQD HHHHHHHHHHCCCCC | 45.89 | 23954790 | |
| 166 | 2-Hydroxyisobutyrylation | QKVADLIKKHAAGQD HHHHHHHHHHCCCCC | 45.89 | - | |
| 204 | Other | IVVHSATKYINGHSD EEEEECCHHHCCCCC | 43.80 | - | |
| 204 | N6-(pyridoxal phosphate)lysine | IVVHSATKYINGHSD EEEEECCHHHCCCCC | 43.80 | - | |
| 222 | Acetylation | GVLATNNKPLYERLQ EEEECCCCHHHHHHH | 38.17 | 24489116 | |
| 267 | Acetylation | QAALSANKIAEFLAA HHHHHHHHHHHHHHC | 42.90 | 24489116 | |
| 276 | Acetylation | AEFLAADKENVVAVN HHHHHCCCCCEEEEE | 46.60 | 24489116 | |
| 288 | Acetylation | AVNYPGLKTHPNYDV EEECCCCCCCCCCHH | 51.18 | 24489116 | |
| 289 | Phosphorylation | VNYPGLKTHPNYDVV EECCCCCCCCCCHHE | 47.83 | 22369663 | |
| 293 | Phosphorylation | GLKTHPNYDVVLKQH CCCCCCCCHHEEEEC | 17.99 | 22369663 | |
| 298 | Acetylation | PNYDVVLKQHRDALG CCCHHEEEECHHHHC | 32.23 | 22865919 | |
| 314 | 2-Hydroxyisobutyrylation | GMISFRIKGGAEAAS CEEEEEEECHHHHHH | 47.22 | - | |
| 322 | Acetylation | GGAEAASKFASSTRL CHHHHHHHHHHCHHH | 39.98 | 24489116 | |
| 322 | 2-Hydroxyisobutyrylation | GGAEAASKFASSTRL CHHHHHHHHHHCHHH | 39.98 | - | |
| 356 | Ubiquitination | MTHGGIPKEAREASG HCCCCCCHHHHHHHC | 63.18 | 23749301 | |
| 362 | Phosphorylation | PKEAREASGVFDDLV CHHHHHHHCCCCHHH | 30.64 | 27214570 | |
| 390 | Ubiquitination | EDIKQALKQATN--- HHHHHHHHHHHC--- | 40.68 | 23749301 |
| 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 CYS3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CYS3_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 CYS3_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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 THR-2; SER-39; SER-40 ANDSER-362, AND MASS SPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND MASSSPECTROMETRY. | |
