| UniProt ID | KIN82_YEAST | |
|---|---|---|
| UniProt AC | P25341 | |
| Protein Name | Serine/threonine-protein kinase KIN82 | |
| Gene Name | KIN82 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 720 | |
| Subcellular Localization | ||
| Protein Description | Flippase activator that phosphorylates DFN1 and DFN2 and which is involved in the generation of phospholipid asymmetry in membranes by the inward translocation of phospholipids.. | |
| Protein Sequence | MTQQEYRSPSQRLSKGRSMSLPKIFARNLRSLQNNAPPGKNINVNCLNVNSCSLSASPSSQINMACNGNKQDLPIPFPLHVECNDSWSSSKLNKFKSMFNHNRSKSSGTTDASTSEKGTHKREPRSTIHTELLQSSIIGEPNVHSTTSSTLIPNEAICSTPNEISGSSSPDAELFTFDMPTDPSSFHTPSSPSYIAKDSRNLSNGSLNDINENEELQNFHRKISENGSASPLANLSLSNSPIDSPRKNSETRKDQIPMNITPRLRRAASEPFNTAKDGLMREDYIALKQPPSLGDIVEPRRSRRLRTKSFGNKFQDITVEPQSFEKIRLLGQGDVGKVYLVRERDTNQIFALKVLNKHEMIKRKKIKRVLTEQEILATSDHPFIVTLYHSFQTKDYLYLCMEYCMGGEFFRALQTRKSKCIAEEDAKFYASEVVAALEYLHLLGFIYRDLKPENILLHQSGHVMLSDFDLSIQATGSKKPTMKDSTYLDTKICSDGFRTNSFVGTEEYLAPEVIRGNGHTAAVDWWTLGILIYEMLFGCTPFKGDNSNETFSNILTKDVKFPHDKEVSKNCKDLIKKLLNKNEAKRLGSKSGAADIKRHPFFKKVQWSFLRNQDPPLIPALNDNGCELPFILSCNKHPKRNSVSEQETKMFCEKVANDDEIDEADPFHDFNSMSLTKKDHNILTYSENYTYGKILYKATCTRPRHNSSHRSFFKDIIPEL | |
| 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 | ------MTQQEYRSP ------CCHHHHCCH | 38.67 | 30377154 | |
| 8 | Phosphorylation | MTQQEYRSPSQRLSK CCHHHHCCHHHHHHC | 28.18 | 30377154 | |
| 10 | Phosphorylation | QQEYRSPSQRLSKGR HHHHCCHHHHHHCCC | 29.22 | 30377154 | |
| 14 | Phosphorylation | RSPSQRLSKGRSMSL CCHHHHHHCCCCCCH | 34.94 | 28889911 | |
| 20 | Phosphorylation | LSKGRSMSLPKIFAR HHCCCCCCHHHHHHH | 42.65 | 28889911 | |
| 106 | Phosphorylation | FNHNRSKSSGTTDAS HCCCCCCCCCCCCCC | 34.93 | 28889911 | |
| 107 | Phosphorylation | NHNRSKSSGTTDAST CCCCCCCCCCCCCCC | 43.85 | 28889911 | |
| 199 | Phosphorylation | PSYIAKDSRNLSNGS CCCCCCCCCCCCCCC | 23.51 | 24961812 | |
| 203 | Phosphorylation | AKDSRNLSNGSLNDI CCCCCCCCCCCCCCC | 42.57 | 22369663 | |
| 206 | Phosphorylation | SRNLSNGSLNDINEN CCCCCCCCCCCCCCC | 28.40 | 22369663 | |
| 224 | Phosphorylation | QNFHRKISENGSASP HHHHHHHHCCCCCCC | 28.22 | 19779198 | |
| 230 | Phosphorylation | ISENGSASPLANLSL HHCCCCCCCCCCCCC | 23.34 | 28889911 | |
| 240 | Phosphorylation | ANLSLSNSPIDSPRK CCCCCCCCCCCCCCC | 21.61 | 28889911 | |
| 249 | Phosphorylation | IDSPRKNSETRKDQI CCCCCCCCCCCHHCC | 43.30 | 27214570 | |
| 261 | Phosphorylation | DQIPMNITPRLRRAA HCCCCCCCHHHHHHH | 9.43 | 28889911 | |
| 269 | Phosphorylation | PRLRRAASEPFNTAK HHHHHHHCCCCCCCC | 44.83 | 24930733 | |
| 292 | Phosphorylation | IALKQPPSLGDIVEP EEECCCCCHHHCCCC | 52.23 | 28889911 | |
| 309 | Phosphorylation | SRRLRTKSFGNKFQD HCCCCCCCCCCCCCC | 37.46 | 28152593 | |
| 318 | Phosphorylation | GNKFQDITVEPQSFE CCCCCCCEECCCCHH | 27.40 | 24961812 | |
| 396 | Phosphorylation | HSFQTKDYLYLCMEY ECCCCCCHHHHHHHH | 9.98 | 29688323 | |
| 398 | Phosphorylation | FQTKDYLYLCMEYCM CCCCCHHHHHHHHHH | 7.51 | 29688323 | |
| 403 | Phosphorylation | YLYLCMEYCMGGEFF HHHHHHHHHHCHHHH | 2.10 | 29688323 | |
| 415 | Phosphorylation | EFFRALQTRKSKCIA HHHHHHHHHHHCCCC | 40.70 | 29688323 | |
| 494 | Phosphorylation | YLDTKICSDGFRTNS CCCCEECCCCCCCCC | 44.21 | 23749301 | |
| 499 | Phosphorylation | ICSDGFRTNSFVGTE ECCCCCCCCCCCCCH | 32.71 | 22369663 | |
| 501 | Phosphorylation | SDGFRTNSFVGTEEY CCCCCCCCCCCCHHH | 22.24 | 17330950 | |
| 505 | Phosphorylation | RTNSFVGTEEYLAPE CCCCCCCCHHHHCCC | 21.97 | 28889911 | |
| 508 | Phosphorylation | SFVGTEEYLAPEVIR CCCCCHHHHCCCHHC | 11.26 | 19779198 | |
| 552 | Phosphorylation | DNSNETFSNILTKDV CCCCCCHHHHHCCCC | 30.31 | 27017623 | |
| 556 | Phosphorylation | ETFSNILTKDVKFPH CCHHHHHCCCCCCCC | 22.77 | 27017623 | |
| 642 | Phosphorylation | NKHPKRNSVSEQETK CCCCCCCCCCHHHHH | 30.93 | 17563356 |
| 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 KIN82_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KIN82_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 KIN82_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 SER-203; SER-206; THR-499;SER-501 AND THR-505, 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-642, AND MASSSPECTROMETRY. | |
