UniProt ID | YPK3_YEAST | |
---|---|---|
UniProt AC | P38070 | |
Protein Name | Serine/threonine-protein kinase YPK3 {ECO:0000305|PubMed:20702584} | |
Gene Name | YPK3 {ECO:0000303|PubMed:20702584} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 525 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | AGC kinase which plays a role in TOR complex 1 (TORC1) signaling pathway which mediates temporal control of cell growth in response to nutrients. [PubMed: 11062466 Required for phosphorylation of ribosomal protein S6 (RPS6A/RPS6B) at 'Ser-232' and 'Ser-233'] | |
Protein Sequence | MIFSLDEELHRVSLDDKKNDIKVDYSSAIYNDINHEQGSSITYEESINHLSVHSNAIPLNGMSPAHRMRRRSSAYSKFPILTPPNTRRFSITGSDAMRTNTNRLSITPQDIISSNIGENELSRNLHDFKPVRVLGQGAYGKVLLVKDVNTSKLYAMKQLRKAEILISQTATDSKREDEDKNDGNNNDNDDGLSKRLERTFAERSILSEIEHPNIVKLFYSFHDNSKLYLLLQYIPGGELFYHLKEHGTLDETTVSFYAAEISCALRFLHTKGVVYRDLKPENCLLNQRGHLVLTDFGLSKKSANDSAVDEEDPENVNALYSIIGTPEYCAPEILLGKAYSQNCDWYSLGCLLYDMLVGKPPYTGSNHKVIINKIQQNKQGPKIPFYLSEGMKDILNALLKKETAKRWNVDKYWAKTGANNKPTKSKKKKSGAARTSLFTEHFIFRKIDWKLLESGQLQKTTLGPIVPVITDLELAENFDTEFTSMSYEETYTDSKPININSVSKSPDMFKGFSYKASGSYLEKYF | |
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 |
---|---|---|---|---|---|
4 | Phosphorylation | ----MIFSLDEELHR ----CCCCCCHHHHC | 24.80 | 30377154 | |
13 | Phosphorylation | DEELHRVSLDDKKND CHHHHCCCCCCCCCC | 26.49 | 30377154 | |
72 | Phosphorylation | AHRMRRRSSAYSKFP HHHHHHCCCCCCCCC | 19.94 | 23749301 | |
73 | Phosphorylation | HRMRRRSSAYSKFPI HHHHHCCCCCCCCCC | 29.43 | 25752575 | |
82 | Phosphorylation | YSKFPILTPPNTRRF CCCCCCCCCCCCCCE | 37.10 | 22369663 | |
86 | Phosphorylation | PILTPPNTRRFSITG CCCCCCCCCCEEEEC | 29.06 | 22369663 | |
90 | Phosphorylation | PPNTRRFSITGSDAM CCCCCCEEEECCHHH | 19.89 | 22369663 | |
92 | Phosphorylation | NTRRFSITGSDAMRT CCCCEEEECCHHHCC | 29.45 | 22369663 | |
94 | Phosphorylation | RRFSITGSDAMRTNT CCEEEECCHHHCCCC | 17.34 | 22369663 | |
99 | Phosphorylation | TGSDAMRTNTNRLSI ECCHHHCCCCCCCCC | 33.05 | 19779198 | |
101 | Phosphorylation | SDAMRTNTNRLSITP CHHHCCCCCCCCCCH | 22.54 | 19779198 | |
105 | Phosphorylation | RTNTNRLSITPQDII CCCCCCCCCCHHHHH | 22.60 | 22369663 | |
107 | Phosphorylation | NTNRLSITPQDIISS CCCCCCCCHHHHHHC | 16.12 | 22369663 | |
113 | Phosphorylation | ITPQDIISSNIGENE CCHHHHHHCCCCCCH | 20.05 | 19779198 | |
114 | Phosphorylation | TPQDIISSNIGENEL CHHHHHHCCCCCCHH | 23.27 | 29688323 | |
122 | Phosphorylation | NIGENELSRNLHDFK CCCCCHHHHCCCCCC | 16.97 | 29688323 | |
146 | Acetylation | YGKVLLVKDVNTSKL CCEEEEEECCCHHHH | 56.80 | 24489116 | |
154 | Phosphorylation | DVNTSKLYAMKQLRK CCCHHHHHHHHHHHH | 14.37 | 19779198 | |
167 | Phosphorylation | RKAEILISQTATDSK HHHEEEEEECCCCCC | 20.31 | 24909858 | |
320 | Phosphorylation | PENVNALYSIIGTPE CCHHHHHHHHHCCHH | 8.73 | 21440633 | |
321 | Phosphorylation | ENVNALYSIIGTPEY CHHHHHHHHHCCHHH | 14.47 | 21440633 | |
411 | Acetylation | AKRWNVDKYWAKTGA HHHCCHHHHHHHCCC | 38.11 | 24489116 | |
490 | Phosphorylation | TSMSYEETYTDSKPI CCCCEEEECCCCCCC | 21.56 | - | |
501 | Phosphorylation | SKPININSVSKSPDM CCCCCCCCCCCCCCC | 24.78 | 21551504 | |
503 | Phosphorylation | PININSVSKSPDMFK CCCCCCCCCCCCCCC | 27.51 | 27717283 | |
505 | Phosphorylation | NINSVSKSPDMFKGF CCCCCCCCCCCCCCC | 20.73 | 21551504 | |
513 | Phosphorylation | PDMFKGFSYKASGSY CCCCCCCEEECCCCH | 34.10 | 28152593 | |
517 | Phosphorylation | KGFSYKASGSYLEKY CCCEEECCCCHHHHC | 24.91 | 22890988 | |
519 | Phosphorylation | FSYKASGSYLEKYF- CEEECCCCHHHHCC- | 24.85 | 21551504 | |
520 | Phosphorylation | SYKASGSYLEKYF-- EEECCCCHHHHCC-- | 23.54 | 22890988 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
321 | S | Phosphorylation | Kinase | PKH1 | Q03407 | Uniprot |
321 | S | Phosphorylation | Kinase | PKH2 | Q12236 | Uniprot |
490 | T | Phosphorylation | Kinase | TORC1 | - | Uniprot |
513 | S | Phosphorylation | Kinase | TORC1 | - | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of YPK3_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 YPK3_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-82; SER-90; SER-105 ANDTHR-107, 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-90, AND MASSSPECTROMETRY. | |
"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 THR-82; SER-90; THR-107 ANDSER-519, AND MASS SPECTROMETRY. |