| UniProt ID | THRC_YEAST | |
|---|---|---|
| UniProt AC | P16120 | |
| Protein Name | Threonine synthase | |
| Gene Name | THR4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 514 | |
| Subcellular Localization | ||
| Protein Description | Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.. | |
| Protein Sequence | MPNASQVYRSTRSSSPKTISFEEAIIQGLATDGGLFIPPTIPQVDQATLFNDWSKLSFQDLAFAIMRLYIAQEEIPDADLKDLIKRSYSTFRSDEVTPLVQNVTGDKENLHILELFHGPTYAFKDVALQFVGNLFEYFLQRTNANLPEGEKKQITVVGATSGDTGSAAIYGLRGKKDVSVFILYPTGRISPIQEEQMTTVPDENVQTLSVTGTFDNCQDIVKAIFGDKEFNSKHNVGAVNSINWARILAQMTYYFYSFFQATNGKDSKKVKFVVPSGNFGDILAGYFAKKMGLPIEKLAIATNENDILDRFLKSGLYERSDKVAATLSPAMDILISSNFERLLWYLAREYLANGDDLKAGEIVNNWFQELKTNGKFQVDKSIIEGASKDFTSERVSNEETSETIKKIYESSVNPKHYILDPHTAVGVCATERLIAKDNDKSIQYISLSTAHPAKFADAVNNALSGFSNYSFEKDVLPEELKKLSTLKKKLKFIERADVELVKNAIEEELAKMKL | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 5 | Phosphorylation | ---MPNASQVYRSTR ---CCCHHHHHHCCC | 27.15 | 22369663 | |
| 8 | Phosphorylation | MPNASQVYRSTRSSS CCCHHHHHHCCCCCC | 7.39 | 22369663 | |
| 81 | Acetylation | EIPDADLKDLIKRSY HCCCCCHHHHHHHHH | 51.54 | 24489116 | |
| 85 | Acetylation | ADLKDLIKRSYSTFR CCHHHHHHHHHHCCC | 42.46 | 24489116 | |
| 87 | Phosphorylation | LKDLIKRSYSTFRSD HHHHHHHHHHCCCCC | 20.59 | 19823750 | |
| 88 | Phosphorylation | KDLIKRSYSTFRSDE HHHHHHHHHCCCCCC | 18.76 | 19823750 | |
| 89 | Phosphorylation | DLIKRSYSTFRSDEV HHHHHHHHCCCCCCC | 23.47 | 19823750 | |
| 90 | Phosphorylation | LIKRSYSTFRSDEVT HHHHHHHCCCCCCCC | 18.16 | 19823750 | |
| 93 | Phosphorylation | RSYSTFRSDEVTPLV HHHHCCCCCCCCHHE | 33.65 | 19823750 | |
| 97 | Phosphorylation | TFRSDEVTPLVQNVT CCCCCCCCHHEECCC | 14.62 | 19823750 | |
| 104 | Phosphorylation | TPLVQNVTGDKENLH CHHEECCCCCHHCEE | 47.41 | 22369663 | |
| 121 | Phosphorylation | ELFHGPTYAFKDVAL HHHCCCCCHHHHHHH | 17.11 | 19779198 | |
| 124 | N6-(pyridoxal phosphate)lysine | HGPTYAFKDVALQFV CCCCCHHHHHHHHHH | 43.02 | - | |
| 124 | Other | HGPTYAFKDVALQFV CCCCCHHHHHHHHHH | 43.02 | - | |
| 151 | 2-Hydroxyisobutyrylation | ANLPEGEKKQITVVG CCCCCCCCEEEEEEE | 61.92 | - | |
| 152 | Ubiquitination | NLPEGEKKQITVVGA CCCCCCCEEEEEEEE | 42.50 | 24961812 | |
| 155 | Phosphorylation | EGEKKQITVVGATSG CCCCEEEEEEEECCC | 13.47 | 22369663 | |
| 160 | Phosphorylation | QITVVGATSGDTGSA EEEEEEECCCCCCCC | 27.58 | 22369663 | |
| 161 | Phosphorylation | ITVVGATSGDTGSAA EEEEEECCCCCCCCH | 33.85 | 22369663 | |
| 164 | Phosphorylation | VGATSGDTGSAAIYG EEECCCCCCCCHHEE | 36.24 | 22369663 | |
| 166 | Phosphorylation | ATSGDTGSAAIYGLR ECCCCCCCCHHEECC | 19.33 | 22369663 | |
| 170 | Phosphorylation | DTGSAAIYGLRGKKD CCCCCHHEECCCCCC | 12.84 | 22369663 | |
| 228 | Acetylation | VKAIFGDKEFNSKHN HHHHHCCCCCCCCCC | 65.66 | 24489116 | |
| 233 | Acetylation | GDKEFNSKHNVGAVN CCCCCCCCCCCCCCH | 40.06 | 24489116 | |
| 290 | Acetylation | LAGYFAKKMGLPIEK HHHHHHHHHCCCHHH | 34.47 | 25381059 | |
| 297 | Acetylation | KMGLPIEKLAIATNE HHCCCHHHHHHHCCC | 43.89 | 24489116 | |
| 313 | Acetylation | DILDRFLKSGLYERS HHHHHHHHCCCHHCC | 39.50 | 22865919 | |
| 313 | 2-Hydroxyisobutyrylation | DILDRFLKSGLYERS HHHHHHHHCCCHHCC | 39.50 | - | |
| 320 | Phosphorylation | KSGLYERSDKVAATL HCCCHHCCHHHHHHC | 29.82 | 19779198 | |
| 322 | Acetylation | GLYERSDKVAATLSP CCHHCCHHHHHHCCH | 34.71 | 24489116 | |
| 326 | Phosphorylation | RSDKVAATLSPAMDI CCHHHHHHCCHHHHH | 20.31 | 22369663 | |
| 328 | Phosphorylation | DKVAATLSPAMDILI HHHHHHCCHHHHHHH | 13.27 | 19779198 | |
| 336 | Phosphorylation | PAMDILISSNFERLL HHHHHHHCCCHHHHH | 18.78 | 22369663 | |
| 337 | Phosphorylation | AMDILISSNFERLLW HHHHHHCCCHHHHHH | 38.25 | 22369663 | |
| 371 | Acetylation | NNWFQELKTNGKFQV HHHHHHHHHCCCCEE | 38.91 | 24489116 | |
| 380 | 2-Hydroxyisobutyrylation | NGKFQVDKSIIEGAS CCCCEECHHHHCCCC | 44.70 | - | |
| 380 | Acetylation | NGKFQVDKSIIEGAS CCCCEECHHHHCCCC | 44.70 | 24489116 | |
| 388 | Succinylation | SIIEGASKDFTSERV HHHCCCCCCCCCCCC | 57.22 | 23954790 | |
| 388 | 2-Hydroxyisobutyrylation | SIIEGASKDFTSERV HHHCCCCCCCCCCCC | 57.22 | - | |
| 388 | Acetylation | SIIEGASKDFTSERV HHHCCCCCCCCCCCC | 57.22 | 24489116 | |
| 401 | Phosphorylation | RVSNEETSETIKKIY CCCCHHHHHHHHHHH | 35.70 | 23749301 | |
| 405 | Acetylation | EETSETIKKIYESSV HHHHHHHHHHHHHCC | 40.30 | 25381059 | |
| 405 | Succinylation | EETSETIKKIYESSV HHHHHHHHHHHHHCC | 40.30 | 23954790 | |
| 405 | 2-Hydroxyisobutyrylation | EETSETIKKIYESSV HHHHHHHHHHHHHCC | 40.30 | - | |
| 408 | Phosphorylation | SETIKKIYESSVNPK HHHHHHHHHHCCCCC | 20.73 | 19823750 | |
| 410 | Phosphorylation | TIKKIYESSVNPKHY HHHHHHHHCCCCCCC | 23.71 | 27821475 | |
| 411 | Phosphorylation | IKKIYESSVNPKHYI HHHHHHHCCCCCCCC | 17.61 | 27821475 | |
| 415 | Acetylation | YESSVNPKHYILDPH HHHCCCCCCCCCCCC | 43.78 | 24489116 | |
| 436 | Succinylation | ATERLIAKDNDKSIQ CCHHHEECCCCCCEE | 50.50 | 23954790 | |
| 436 | Acetylation | ATERLIAKDNDKSIQ CCHHHEECCCCCCEE | 50.50 | 25381059 | |
| 440 | Acetylation | LIAKDNDKSIQYISL HEECCCCCCEEEEEC | 56.57 | 24489116 | |
| 441 | Phosphorylation | IAKDNDKSIQYISLS EECCCCCCEEEEECC | 20.14 | 28889911 | |
| 464 | Phosphorylation | DAVNNALSGFSNYSF HHHHHHHCCCCCCCC | 35.07 | 28889911 | |
| 467 | Phosphorylation | NNALSGFSNYSFEKD HHHHCCCCCCCCCCC | 38.08 | 22369663 | |
| 469 | Phosphorylation | ALSGFSNYSFEKDVL HHCCCCCCCCCCCCC | 17.34 | 22369663 | |
| 470 | Phosphorylation | LSGFSNYSFEKDVLP HCCCCCCCCCCCCCH | 31.05 | 22369663 | |
| 481 | Acetylation | DVLPEELKKLSTLKK CCCHHHHHHHHHHHH | 55.75 | 24489116 | |
| 481 | Succinylation | DVLPEELKKLSTLKK CCCHHHHHHHHHHHH | 55.75 | 23954790 | |
| 502 | Acetylation | RADVELVKNAIEEEL HHCHHHHHHHHHHHH | 53.97 | 24489116 | |
| 502 | Ubiquitination | RADVELVKNAIEEEL HHCHHHHHHHHHHHH | 53.97 | 23749301 | |
| 511 | Acetylation | AIEEELAKMKL---- HHHHHHHHCCC---- | 49.55 | 24489116 |
| 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 THRC_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of THRC_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 THRC_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| 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-467; TYR-469 ANDSER-470, AND MASS SPECTROMETRY. | |
