| UniProt ID | KOG1_YEAST | |
|---|---|---|
| UniProt AC | P38873 | |
| Protein Name | Target of rapamycin complex 1 subunit KOG1 | |
| Gene Name | KOG1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1557 | |
| Subcellular Localization |
Cell membrane Peripheral membrane protein Cytoplasmic side. Vacuole membrane Peripheral membrane protein Cytoplasmic side. Also localizes to membranous structures within the cell interior, probably endosomal or Golgi membranes. |
|
| Protein Description | Component of TORC1, which regulates multiple cellular processes to control cell growth in response to environmental signals. Nutrient limitation and environmental stress signals cause inactivation of TORC1. Active TORC1 positively controls ribosome biogenesis via control of rRNA, ribosomal protein and tRNA gene expression, and rRNA processing. TORC1 positively controls protein biosynthesis by regulation of mRNA stability, translation initiation factor activity, and high-affinity amino acid permeases that serve to provide amino acids for use by the translation machinery. TORC1 also promotes growth by sequestering a number of nutrient and general stress-responsive transcription factors in the cytoplasm. TORC1 negatively controls macroautophagy, a process to recycle surplus cytoplasmic mass under nutrient starvation conditions. KOG1 may have a role in binding and recruiting substrates of TORC1.. | |
| Protein Sequence | MPEIYGPQPLKPLNTVMRHGFEEQYQSDQLLQSLANDFIFYFDDKRHKTNGNPIPEEDKQRDVNRYYQPITDWKIMKDRQKTVSAALLLCLNLGVDPPDVMKTHPCARVEAWVDPLNFQDSKKAIEQIGKNLQAQYETLSLRTRYKQSLDPCVEDVKRFCNSLRRTSKEDRILFHYNGHGVPKPTKSGEIWVFNRGYTQYIPVSLYDLQTWLGAPCIFVYDCNSAENILINFQKFVQKRIKDDEEGNHDVAAPSPTSAYQDCFQLASCTSDELLLMSPELPADLFSCCLTCPIEISIRIFLMQSPLKDSKYKIFFENSTSNQPFGDSKNSFKSKIPNVNIPGMLSDRRTPLGELNWIFTAITDTIAWTSLPRPLFKKLFRHDLMIAALFRNFLLAKRIMPWYNCHPVSDPELPDSITTHPMWKSWDLAMDEVLTKIVIDLKNAPPATALESQMILQQQETLQNGGSSKSNAQDTKAGSIQTQSRFAVANLSTMSLVNNPALQSRKSISLQSSQQQLQQQQQQQQQFTGFFEQNLTAFELWLKYASNVRHPPEQLPIVLQVLLSQVHRIRALVLLSRFLDLGPWAVYLSLSIGIFPYVLKLLQSPAPELKPILVFIWARIMSIDYKNTQSELIKEKGYMYFVTVLVPDWGVNGMSATNGSAMINSGNPLTMTASQNINGPSSRYYERQQGNRTSNLGHNNLPFYHSNDTTDEQKAMAVFVLASFVRNFPLGQKNCFSLELVNKLCFYIDNSEIPLLRQWCVILLGLLFADNPLNRFVCMNTGAVEILLKSLKDPVPEVRTASIFALKHFISGFQDAEVILRLQQEFEEQYQQLHSQLQHLQNQSHLQQQQSQQQQQHLEQQQMKIEKQIRHCQVMQNQLEVIDLRKLKRQEIGNLISILPLINDGSSLVRKELVVYFSHIVSRYSNFFIVVVFNDLLEEIKLLEKSDINTRNTSDKYSVSQGSIFYTVWKSLLILAEDPFLENKELSKQVIDYILLELSAHKELGGPFAVMEKFLLKRSSKAHQTGKFGFNSSQVQFVKSSLRSFSPNERVDNNAFKKEQQQHDPKISHPMRTSLAKLFQSLGFSESNSDSDTQSSNTSMKSHTSKKGPSGLYLLNGNNNIYPTAETPRFRKHTEPLQLPLNSSFLDYSREYFQEPQMKKQEADEPGSVEYNARLWRRNRNETIIQETQGEKKLSIYGNWSKKLISLNNKSQPKLMKFAQFEDQLITADDRSTITVFDWEKGKTLSKFSNGTPFGTKVTDLKLINEDDSALLLTGSSDGVIKIYRDYQDVDTFKIVSAWRGLTDMLLTPRSTGLLTEWLQIRGSLLTTGDVKVIRVWDAHTETVEVDIPAKTSSLITSLTADQLAGNIFVAGFADGSLRVYDRRLDPRDSMIRRWRAGNDKQGVWINNVHLQRGGYRELVSGATNGVVELWDIRSEDPVESFVDQNVTSQYGSQQKPTTMTCMQVHEHAPIIATGTKQIKIWTTSGDLLNSFKNSHNNGVTSTLAATGIPKSLSYSSTSDAFLSSMAFHPHRMMIAATNSHDSIVNIYKCEDERIDYF | |
| 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 |
|---|---|---|---|---|---|
| 319 | Phosphorylation | KIFFENSTSNQPFGD EEEEECCCCCCCCCC | 43.19 | 21551504 | |
| 320 | Phosphorylation | IFFENSTSNQPFGDS EEEECCCCCCCCCCC | 33.03 | 21551504 | |
| 327 | Phosphorylation | SNQPFGDSKNSFKSK CCCCCCCCCCCHHHC | 33.83 | 21551504 | |
| 330 | Phosphorylation | PFGDSKNSFKSKIPN CCCCCCCCHHHCCCC | 37.48 | 21551504 | |
| 333 | Phosphorylation | DSKNSFKSKIPNVNI CCCCCHHHCCCCCCC | 33.53 | 21551504 | |
| 474 | Phosphorylation | SKSNAQDTKAGSIQT CCCCCCCCCCCCCCC | 15.66 | 21440633 | |
| 475 | Ubiquitination | KSNAQDTKAGSIQTQ CCCCCCCCCCCCCCH | 60.07 | 23749301 | |
| 478 | Phosphorylation | AQDTKAGSIQTQSRF CCCCCCCCCCCHHHE | 19.18 | 16445868 | |
| 481 | Phosphorylation | TKAGSIQTQSRFAVA CCCCCCCCHHHEEEE | 27.17 | 16445868 | |
| 483 | Phosphorylation | AGSIQTQSRFAVANL CCCCCCHHHEEEECH | 32.52 | 24961812 | |
| 491 | Phosphorylation | RFAVANLSTMSLVNN HEEEECHHHHHCCCC | 23.13 | 22369663 | |
| 492 | Phosphorylation | FAVANLSTMSLVNNP EEEECHHHHHCCCCH | 17.59 | 22369663 | |
| 494 | Phosphorylation | VANLSTMSLVNNPAL EECHHHHHCCCCHHH | 29.29 | 22369663 | |
| 503 | Phosphorylation | VNNPALQSRKSISLQ CCCHHHHCCHHHHHH | 42.39 | 23749301 | |
| 1031 | Phosphorylation | TGKFGFNSSQVQFVK CCCCCCCHHHHHHHH | 21.64 | 28889911 | |
| 1032 | Phosphorylation | GKFGFNSSQVQFVKS CCCCCCHHHHHHHHH | 35.16 | 28152593 | |
| 1043 | Phosphorylation | FVKSSLRSFSPNERV HHHHHHHCCCCCCCC | 35.06 | 21440633 | |
| 1045 | Phosphorylation | KSSLRSFSPNERVDN HHHHHCCCCCCCCCC | 28.23 | 20377248 | |
| 1286 | Phosphorylation | VIKIYRDYQDVDTFK EEEEEECCCCCCHHH | 9.52 | 27017623 | |
| 1537 | Phosphorylation | HRMMIAATNSHDSIV HHEEEEECCCCCCCE | 28.38 | 28889911 | |
| 1542 | Phosphorylation | AATNSHDSIVNIYKC EECCCCCCCEEEEEE | 24.02 | 28889911 | |
| 1547 | Phosphorylation | HDSIVNIYKCEDERI CCCCEEEEEECHHCC | 12.37 | 28889911 |
| 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 KOG1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KOG1_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 KOG1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| Phosphorylation | |
| Reference | PubMed |
| "Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478; THR-481; SER-491AND SER-494, AND MASS SPECTROMETRY. | |
| "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-492, AND MASSSPECTROMETRY. | |
