| UniProt ID | TPS2_YEAST | |
|---|---|---|
| UniProt AC | P31688 | |
| Protein Name | Trehalose-phosphatase | |
| Gene Name | TPS2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 896 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Phosphatase catalytic subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-alpha-D-glucose in a two step process.. | |
| Protein Sequence | MTTTAQDNSPKKRQRIINCVTQLPYKIQLGESNDDWKISATTGNSALFSSLEYLQFDSTEYEQHVVGWTGEITRTERNLFTREAKEKPQDLDDDPLYLTKEQINGLTTTLQDHMKSDKEAKTDTTQTAPVTNNVHPVWLLRKNQSRWRNYAEKVIWPTFHYILNPSNEGEQEKNWWYDYVKFNEAYAQKIGEVYRKGDIIWIHDYYLLLLPQLLRMKFNDESIIIGYFHHAPWPSNEYFRCLPRRKQILDGLVGANRICFQNESFSRHFVSSCKRLLDATAKKSKNSSNSDQYQVSVYGGDVLVDSLPIGVNTTQILKDAFTKDIDSKVLSIKQAYQNKKIIIGRDRLDSVRGVVQKLRAFETFLAMYPEWRDQVVLIQVSSPTANRNSPQTIRLEQQVNELVNSINSEYGNLNFSPVQHYYMRIPKDVYLSLLRVADLCLITSVRDGMNTTALEYVTVKSHMSNFLCYGNPLILSEFSGSSNVLKDAIVVNPWDSVAVAKSINMALKLDKEEKSNLESKLWKEVPTIQDWTNKFLSSLKEQASSNDDMERKMTPALNRPVLLENYKQAKRRLFLFDYDGTLTPIVKDPAAAIPSARLYTILQKLCADPHNQIWIISGRDQKFLNKWLGGKLPQLGLSAEHGCFMKDVSCQDWVNLTEKVDMSWQVRVNEVMEEFTTRTPGSFIERKKVALTWHYRRTVPELGEFHAKELKEKLLSFTDDFDLEVMDGKANIEVRPRFVNKGEIVKRLVWHQHGKPQDMLKGISEKLPKDEMPDFVLCLGDDFTDEDMFRQLNTIETCWKEKYPDQKNQWGNYGFYPVTVGSASKKTVAKAHLTDPQQVLETLGLLVGDVSLFQSAGTVDLDSRGHVKNSESSLKSKLASKAYVMKRSASYTGAKV | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MTTTAQDNS ------CCCCCCCCC | 32.62 | 22369663 | |
| 3 | Phosphorylation | -----MTTTAQDNSP -----CCCCCCCCCH | 20.88 | 22369663 | |
| 4 | Phosphorylation | ----MTTTAQDNSPK ----CCCCCCCCCHH | 17.10 | 22369663 | |
| 9 | Phosphorylation | TTTAQDNSPKKRQRI CCCCCCCCHHHHHHH | 46.52 | 22369663 | |
| 26 | Ubiquitination | CVTQLPYKIQLGESN HHHHCCEEEECCCCC | 23.26 | 17644757 | |
| 100 | Acetylation | DDPLYLTKEQINGLT CCCCCCCHHHHCCCH | 45.05 | 24489116 | |
| 121 | Ubiquitination | MKSDKEAKTDTTQTA HHCCCCCCCCCCCCC | 48.28 | 17644757 | |
| 142 | Ubiquitination | HPVWLLRKNQSRWRN CCEEEEECCHHHHHH | 60.35 | 17644757 | |
| 153 | Ubiquitination | RWRNYAEKVIWPTFH HHHHHHHHCHHHHEE | 30.74 | 17644757 | |
| 173 | Ubiquitination | SNEGEQEKNWWYDYV CCCCHHCCCCEEHHH | 58.52 | 17644757 | |
| 189 | Ubiquitination | FNEAYAQKIGEVYRK HHHHHHHHHHHHHHC | 44.50 | 24961812 | |
| 217 | Ubiquitination | LPQLLRMKFNDESII HHHHHCCCCCCCCEE | 34.28 | 17644757 | |
| 323 | Ubiquitination | ILKDAFTKDIDSKVL HHHHHHCCCCCHHHH | 46.35 | 23749301 | |
| 323 | Acetylation | ILKDAFTKDIDSKVL HHHHHHCCCCCHHHH | 46.35 | 24489116 | |
| 327 | Phosphorylation | AFTKDIDSKVLSIKQ HHCCCCCHHHHCHHH | 25.62 | 21440633 | |
| 328 | Ubiquitination | FTKDIDSKVLSIKQA HCCCCCHHHHCHHHH | 43.37 | 24961812 | |
| 333 | 2-Hydroxyisobutyrylation | DSKVLSIKQAYQNKK CHHHHCHHHHHCCCC | 26.04 | - | |
| 350 | Phosphorylation | IGRDRLDSVRGVVQK ECCCHHHHHHHHHHH | 20.50 | 21440633 | |
| 427 | Ubiquitination | HYYMRIPKDVYLSLL EEEECCCHHHHHHHH | 58.41 | 24961812 | |
| 427 | Acetylation | HYYMRIPKDVYLSLL EEEECCCHHHHHHHH | 58.41 | 24489116 | |
| 515 | Phosphorylation | KLDKEEKSNLESKLW HCCHHHHHCHHHHHH | 50.34 | 30377154 | |
| 520 | Ubiquitination | EKSNLESKLWKEVPT HHHCHHHHHHHCCCC | 49.33 | 23749301 | |
| 523 | Acetylation | NLESKLWKEVPTIQD CHHHHHHHCCCCHHH | 60.31 | 24489116 | |
| 552 | Ubiquitination | SNDDMERKMTPALNR CCHHHHHHHCHHHCC | 33.54 | 17644757 | |
| 554 | Phosphorylation | DDMERKMTPALNRPV HHHHHHHCHHHCCHH | 14.40 | 19779198 | |
| 567 | Ubiquitination | PVLLENYKQAKRRLF HHHHHHHHHHCCEEE | 56.19 | 17644757 | |
| 578 | Phosphorylation | RRLFLFDYDGTLTPI CEEEEEECCCCEEEC | 14.67 | 22369663 | |
| 581 | Phosphorylation | FLFDYDGTLTPIVKD EEEECCCCEEECCCC | 25.26 | 22369663 | |
| 583 | Phosphorylation | FDYDGTLTPIVKDPA EECCCCEEECCCCHH | 15.71 | 22369663 | |
| 587 | Ubiquitination | GTLTPIVKDPAAAIP CCEEECCCCHHHHCC | 59.73 | 24961812 | |
| 604 | Ubiquitination | RLYTILQKLCADPHN HHHHHHHHHHCCCCC | 41.93 | 17644757 | |
| 626 | Acetylation | RDQKFLNKWLGGKLP CCHHHHHHHHCCCCC | 46.04 | 24489116 | |
| 631 | Acetylation | LNKWLGGKLPQLGLS HHHHHCCCCCCCCCC | 56.02 | 24489116 | |
| 638 | Phosphorylation | KLPQLGLSAEHGCFM CCCCCCCCCCCCCCC | 29.79 | 28889911 | |
| 682 | Phosphorylation | FTTRTPGSFIERKKV HHCCCCCCCHHHHHE | 25.01 | 30377154 | |
| 708 | Acetylation | ELGEFHAKELKEKLL CHHHHCHHHHHHHHH | 55.82 | 24489116 | |
| 741 | Acetylation | VRPRFVNKGEIVKRL ECCCCCCHHHHHHHH | 53.25 | 24489116 | |
| 755 | Acetylation | LVWHQHGKPQDMLKG HHHHHCCCHHHHHHH | 37.06 | 24489116 | |
| 764 | Phosphorylation | QDMLKGISEKLPKDE HHHHHHHHHCCCCCC | 37.03 | 27017623 | |
| 802 | Acetylation | IETCWKEKYPDQKNQ HHHHHHHHCCCCCCC | 59.36 | 24489116 | |
| 807 | Ubiquitination | KEKYPDQKNQWGNYG HHHCCCCCCCCCCCC | 59.49 | 17644757 | |
| 819 | Phosphorylation | NYGFYPVTVGSASKK CCCEEEEEECCCCCC | 18.04 | 27017623 | |
| 825 | Ubiquitination | VTVGSASKKTVAKAH EEECCCCCCEEHHHH | 52.78 | 17644757 | |
| 826 | Ubiquitination | TVGSASKKTVAKAHL EECCCCCCEEHHHHC | 45.82 | 17644757 | |
| 870 | Phosphorylation | SRGHVKNSESSLKSK CCCCCCCCHHHHHHH | 32.89 | 30377154 | |
| 872 | Phosphorylation | GHVKNSESSLKSKLA CCCCCCHHHHHHHHH | 40.57 | 28889911 | |
| 881 | Acetylation | LKSKLASKAYVMKRS HHHHHHHHHHHHHHH | 37.82 | 22865919 | |
| 883 | Phosphorylation | SKLASKAYVMKRSAS HHHHHHHHHHHHHHC | 12.57 | 21440633 | |
| 888 | Phosphorylation | KAYVMKRSASYTGAK HHHHHHHHHCCCCCC | 18.95 | 22890988 | |
| 890 | Phosphorylation | YVMKRSASYTGAKV- HHHHHHHCCCCCCC- | 25.19 | 22369663 | |
| 891 | Phosphorylation | VMKRSASYTGAKV-- HHHHHHCCCCCCC-- | 14.65 | 22369663 | |
| 892 | Phosphorylation | MKRSASYTGAKV--- HHHHHCCCCCCC--- | 28.33 | 22890988 |
| 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 TPS2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TPS2_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 TPS2_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-890, AND MASSSPECTROMETRY. | |
| "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-890, 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 SER-890, AND MASSSPECTROMETRY. | |
| "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-890, AND MASSSPECTROMETRY. | |
