| UniProt ID | YPK2_YEAST | |
|---|---|---|
| UniProt AC | P18961 | |
| Protein Name | Serine/threonine-protein kinase YPK2/YKR2 | |
| Gene Name | YPK2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 677 | |
| Subcellular Localization | Nucleus. Cytoplasm. | |
| Protein Description | May act as a downstream kinase in the sphingolipid-mediated signaling pathway. Plays an essential role in the proliferation of yeast cells. Involved in a signaling pathway, required for optimal cell wall integrity, that acts in parallel with the PKC1-SLT2-dependent pathway. A substrate of TOR complex 2 (TORC2) and required for TORC2 to regulate spatial aspects of cell growth. Phosphorylation of residue Thr-501 is indispensable for function.. | |
| Protein Sequence | MHSWRISKFKLGRSKEDDGSSEDENEKSWGNGLFHFHHGEKHHDGSPKNHNHEHEHHIRKINTNETLPSSLSSPKLRNDASFKNPSGIGNDNSKASERKASQSSTETQGPSSESGLMTVKVYSGKDFTLPFPITSNSTILQKLLSSGILTSSSNDASEVAAIMRQLPRYKRVDQDSAGEGLIDRAFATKFIPSSILLPGSTNSSPLLYFTIEFDNSITTISPDMGTMEQPVFNKISTFDVTRKLRFLKIDVFARIPSLLLPSKNWQQEIGEQDEVLKEILKKINTNQDIHLDSFHLPLNLKIDSAAQIRLYNHHWISLERGYGKLNITVDYKPSKNKPLSIDDFDLLKVIGKGSFGKVMQVRKKDTQKIYALKALRKAYIVSKCEVTHTLAERTVLARVDCPFIVPLKFSFQSPEKLYLVLAFINGGELFYHLQHEGRFSLARSRFYIAELLCALDSLHKLDVIYRDLKPENILLDYQGHIALCDFGLCKLNMKDNDKTDTFCGTPEYLAPEILLGQGYTKTVDWWTLGILLYEMMTGLPPYYDENVPVMYKKILQQPLLFPDGFDPAAKDLLIGLLSRDPSRRLGVNGTDEIRNHPFFKDISWKKLLLKGYIPPYKPIVKSEIDTANFDQEFTKEKPIDSVVDEYLSASIQKQFGGWTYIGDEQLGDSPSQGRSIS | |
| 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 |
|---|---|---|---|---|---|
| 20 | Phosphorylation | RSKEDDGSSEDENEK CCCCCCCCCCCCCCC | 37.23 | 28889911 | |
| 21 | Phosphorylation | SKEDDGSSEDENEKS CCCCCCCCCCCCCCC | 55.38 | 24603354 | |
| 46 | Phosphorylation | GEKHHDGSPKNHNHE CCCCCCCCCCCCCCC | 38.46 | 28889911 | |
| 60 | Ubiquitination | EHEHHIRKINTNETL CCHHHEEECCCCCCC | 39.44 | 17644757 | |
| 63 | Phosphorylation | HHIRKINTNETLPSS HHEEECCCCCCCCCC | 37.59 | 19823750 | |
| 66 | Phosphorylation | RKINTNETLPSSLSS EECCCCCCCCCCCCC | 46.14 | 21551504 | |
| 69 | Phosphorylation | NTNETLPSSLSSPKL CCCCCCCCCCCCCCC | 47.20 | 20377248 | |
| 70 | Phosphorylation | TNETLPSSLSSPKLR CCCCCCCCCCCCCCC | 30.26 | 20377248 | |
| 72 | Phosphorylation | ETLPSSLSSPKLRND CCCCCCCCCCCCCCC | 46.68 | 21551504 | |
| 73 | Phosphorylation | TLPSSLSSPKLRNDA CCCCCCCCCCCCCCC | 31.20 | 29136822 | |
| 75 | Ubiquitination | PSSLSSPKLRNDASF CCCCCCCCCCCCCCC | 63.12 | 17644757 | |
| 81 | Phosphorylation | PKLRNDASFKNPSGI CCCCCCCCCCCCCCC | 39.35 | 29136822 | |
| 83 | Acetylation | LRNDASFKNPSGIGN CCCCCCCCCCCCCCC | 66.51 | 25381059 | |
| 94 | Ubiquitination | GIGNDNSKASERKAS CCCCCCCHHHHHHHH | 63.29 | 23749301 | |
| 96 | Phosphorylation | GNDNSKASERKASQS CCCCCHHHHHHHHCC | 41.49 | 19823750 | |
| 101 | Phosphorylation | KASERKASQSSTETQ HHHHHHHHCCCCCCC | 33.36 | 19823750 | |
| 103 | Phosphorylation | SERKASQSSTETQGP HHHHHHCCCCCCCCC | 36.41 | 20377248 | |
| 104 | Phosphorylation | ERKASQSSTETQGPS HHHHHCCCCCCCCCC | 23.72 | 19823750 | |
| 105 | Phosphorylation | RKASQSSTETQGPSS HHHHCCCCCCCCCCC | 48.58 | 19823750 | |
| 107 | Phosphorylation | ASQSSTETQGPSSES HHCCCCCCCCCCCCC | 38.62 | 23749301 | |
| 112 | Phosphorylation | TETQGPSSESGLMTV CCCCCCCCCCCEEEE | 38.63 | 19779198 | |
| 120 | Ubiquitination | ESGLMTVKVYSGKDF CCCEEEEEEEECCCE | 26.70 | 17644757 | |
| 122 | Phosphorylation | GLMTVKVYSGKDFTL CEEEEEEEECCCEEE | 13.14 | 27017623 | |
| 123 | Phosphorylation | LMTVKVYSGKDFTLP EEEEEEEECCCEEEC | 42.21 | 27017623 | |
| 125 | Ubiquitination | TVKVYSGKDFTLPFP EEEEEECCCEEECCC | 43.67 | 17644757 | |
| 128 | Phosphorylation | VYSGKDFTLPFPITS EEECCCEEECCCCCC | 43.59 | 27017623 | |
| 142 | Ubiquitination | SNSTILQKLLSSGIL CCCHHHHHHHHCCCC | 48.20 | 17644757 | |
| 241 | Phosphorylation | KISTFDVTRKLRFLK CCCCCHHHHHCCCCC | 24.75 | 21440633 | |
| 282 | Ubiquitination | VLKEILKKINTNQDI HHHHHHHHHCCCCCC | 37.43 | 17644757 | |
| 301 | Ubiquitination | FHLPLNLKIDSAAQI ECCCCCEEECCCHHH | 43.31 | 17644757 | |
| 335 | Ubiquitination | TVDYKPSKNKPLSID EEEECCCCCCCCCCC | 77.00 | 17644757 | |
| 337 | Ubiquitination | DYKPSKNKPLSIDDF EECCCCCCCCCCCCC | 51.58 | 17644757 | |
| 340 | Phosphorylation | PSKNKPLSIDDFDLL CCCCCCCCCCCCCCC | 32.28 | 27017623 | |
| 348 | Ubiquitination | IDDFDLLKVIGKGSF CCCCCCCHHHCCCCC | 38.82 | 17644757 | |
| 373 | Acetylation | TQKIYALKALRKAYI HHHHHHHHHHHHHHE | 36.88 | 24489116 | |
| 499 | Phosphorylation | NMKDNDKTDTFCGTP CCCCCCCCCCCCCCH | 43.04 | 21440633 | |
| 501 | Phosphorylation | KDNDKTDTFCGTPEY CCCCCCCCCCCCHHH | 26.51 | 25533186 | |
| 505 | Phosphorylation | KTDTFCGTPEYLAPE CCCCCCCCHHHHCHH | 17.71 | 17330950 | |
| 508 | Phosphorylation | TFCGTPEYLAPEILL CCCCCHHHHCHHHHC | 14.90 | 30377154 | |
| 519 | Phosphorylation | EILLGQGYTKTVDWW HHHCCCCCCCCHHHH | 9.36 | 26447709 | |
| 520 | Phosphorylation | ILLGQGYTKTVDWWT HHCCCCCCCCHHHHH | 27.36 | 26447709 | |
| 522 | Phosphorylation | LGQGYTKTVDWWTLG CCCCCCCCHHHHHHH | 18.85 | 30377154 | |
| 527 | Phosphorylation | TKTVDWWTLGILLYE CCCHHHHHHHHHHHH | 15.73 | 30377154 | |
| 533 | Phosphorylation | WTLGILLYEMMTGLP HHHHHHHHHHHHCCC | 9.80 | 30377154 | |
| 537 | Phosphorylation | ILLYEMMTGLPPYYD HHHHHHHHCCCCCCC | 33.97 | 30377154 | |
| 542 | Phosphorylation | MMTGLPPYYDENVPV HHHCCCCCCCCCCCH | 22.93 | 30377154 | |
| 543 | Phosphorylation | MTGLPPYYDENVPVM HHCCCCCCCCCCCHH | 23.66 | 30377154 | |
| 551 | Phosphorylation | DENVPVMYKKILQQP CCCCCHHHHHHHCCC | 14.90 | 30377154 | |
| 552 | Ubiquitination | ENVPVMYKKILQQPL CCCCHHHHHHHCCCC | 18.42 | 17644757 | |
| 553 | Ubiquitination | NVPVMYKKILQQPLL CCCHHHHHHHCCCCC | 31.03 | 17644757 | |
| 570 | Ubiquitination | DGFDPAAKDLLIGLL CCCCHHHHHHHHHHH | 51.52 | 17644757 | |
| 621 | Ubiquitination | PPYKPIVKSEIDTAN CCCCCCCCCCCCCCC | 42.99 | 17644757 | |
| 622 | Phosphorylation | PYKPIVKSEIDTANF CCCCCCCCCCCCCCC | 28.96 | 27017623 | |
| 635 | Ubiquitination | NFDQEFTKEKPIDSV CCCHHHHCCCCCHHH | 69.89 | 17644757 | |
| 641 | Phosphorylation | TKEKPIDSVVDEYLS HCCCCCHHHHHHHHH | 25.43 | 17330950 | |
| 648 | Phosphorylation | SVVDEYLSASIQKQF HHHHHHHHHHHHHHH | 21.04 | 28889911 | |
| 650 | Phosphorylation | VDEYLSASIQKQFGG HHHHHHHHHHHHHCC | 23.37 | 17330950 | |
| 659 | Phosphorylation | QKQFGGWTYIGDEQL HHHHCCEEEECCCCC | 14.45 | 28889911 | |
| 669 | Phosphorylation | GDEQLGDSPSQGRSI CCCCCCCCCCCCCCC | 25.34 | 28152593 | |
| 671 | Phosphorylation | EQLGDSPSQGRSIS- CCCCCCCCCCCCCC- | 49.58 | 30377154 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of YPK2_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 YPK2_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-63; SER-72 AND THR-501,AND MASS SPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641 AND SER-650, ANDMASS SPECTROMETRY. | |
| "Tor2 directly phosphorylates the AGC kinase Ypk2 to regulate actinpolarization."; Kamada Y., Fujioka Y., Suzuki N.N., Inagaki F., Wullschleger S.,Loewith R., Hall M.N., Ohsumi Y.; Mol. Cell. Biol. 25:7239-7248(2005). Cited for: FUNCTION, PHOSPHORYLATION AT THR-501 BY PKH2, PHOSPHORYLATION ATSER-641 AND THR-659 BY TOR2, REGULATION BY TOR2, AND MUTAGENESIS OFASP-239; SER-641 AND THR-659. | |
| "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 THR-501, AND MASSSPECTROMETRY. | |