UniProt ID | TPS1_YEAST | |
---|---|---|
UniProt AC | Q00764 | |
Protein Name | Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 56 kDa subunit | |
Gene Name | TPS1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 495 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Synthase 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. Can function independently of the complex.. | |
Protein Sequence | MTTDNAKAQLTSSSGGNIIVVSNRLPVTITKNSSTGQYEYAMSSGGLVTALEGLKKTYTFKWFGWPGLEIPDDEKDQVRKDLLEKFNAVPIFLSDEIADLHYNGFSNSILWPLFHYHPGEINFDENAWLAYNEANQTFTNEIAKTMNHNDLIWVHDYHLMLVPEMLRVKIHEKQLQNVKVGWFLHTPFPSSEIYRILPVRQEILKGVLSCDLVGFHTYDYARHFLSSVQRVLNVNTLPNGVEYQGRFVNVGAFPIGIDVDKFTDGLKKESVQKRIQQLKETFKGCKIIVGVDRLDYIKGVPQKLHAMEVFLNEHPEWRGKVVLVQVAVPSRGDVEEYQYLRSVVNELVGRINGQFGTVEFVPIHFMHKSIPFEELISLYAVSDVCLVSSTRDGMNLVSYEYIACQEEKKGSLILSEFTGAAQSLNGAIIVNPWNTDDLSDAINEALTLPDVKKEVNWEKLYKYISKYTSAFWGENFVHELYSTSSSSTSSSATKN | |
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 |
---|---|---|---|---|---|
7 | Ubiquitination | -MTTDNAKAQLTSSS -CCCHHHHHEEECCC | 42.81 | 17644757 | |
11 | Phosphorylation | DNAKAQLTSSSGGNI HHHHHEEECCCCCEE | 17.93 | 22369663 | |
12 | Phosphorylation | NAKAQLTSSSGGNII HHHHEEECCCCCEEE | 30.97 | 22369663 | |
13 | Phosphorylation | AKAQLTSSSGGNIIV HHHEEECCCCCEEEE | 27.97 | 22369663 | |
14 | Phosphorylation | KAQLTSSSGGNIIVV HHEEECCCCCEEEEE | 50.95 | 22369663 | |
31 | Ubiquitination | RLPVTITKNSSTGQY CCEEEEEECCCCCEE | 51.48 | 17644757 | |
33 | Phosphorylation | PVTITKNSSTGQYEY EEEEEECCCCCEEEE | 30.72 | 27017623 | |
49 | Phosphorylation | MSSGGLVTALEGLKK EECCCCCCCCCHHHC | 30.48 | 27017623 | |
169 | 2-Hydroxyisobutyrylation | VPEMLRVKIHEKQLQ CHHHHHHHCCHHHHC | 31.73 | - | |
179 | Ubiquitination | EKQLQNVKVGWFLHT HHHHCCCEEEEEEEC | 42.45 | 17644757 | |
205 | Ubiquitination | PVRQEILKGVLSCDL HHHHHHHHHHHCCCE | 53.27 | 17644757 | |
261 | Acetylation | PIGIDVDKFTDGLKK CCEECHHHCCCCCCH | 50.43 | 24489116 | |
261 | Ubiquitination | PIGIDVDKFTDGLKK CCEECHHHCCCCCCH | 50.43 | 24961812 | |
263 | Phosphorylation | GIDVDKFTDGLKKES EECHHHCCCCCCHHH | 34.59 | 27017623 | |
267 | Acetylation | DKFTDGLKKESVQKR HHCCCCCCHHHHHHH | 61.08 | 24489116 | |
267 | Ubiquitination | DKFTDGLKKESVQKR HHCCCCCCHHHHHHH | 61.08 | 17644757 | |
267 | 2-Hydroxyisobutyrylation | DKFTDGLKKESVQKR HHCCCCCCHHHHHHH | 61.08 | - | |
268 | Ubiquitination | KFTDGLKKESVQKRI HCCCCCCHHHHHHHH | 61.33 | 17644757 | |
273 | 2-Hydroxyisobutyrylation | LKKESVQKRIQQLKE CCHHHHHHHHHHHHH | 49.68 | - | |
279 | Acetylation | QKRIQQLKETFKGCK HHHHHHHHHHHCCCE | 50.82 | 22865919 | |
286 | Ubiquitination | KETFKGCKIIVGVDR HHHHCCCEEEEECCC | 44.10 | 17644757 | |
298 | Acetylation | VDRLDYIKGVPQKLH CCCHHHHCCCCCHHH | 47.85 | 24489116 | |
298 | Ubiquitination | VDRLDYIKGVPQKLH CCCHHHHCCCCCHHH | 47.85 | 24961812 | |
459 | Acetylation | KKEVNWEKLYKYISK HHHCCHHHHHHHHHH | 49.05 | 24489116 | |
459 | Ubiquitination | KKEVNWEKLYKYISK HHHCCHHHHHHHHHH | 49.05 | 24961812 | |
462 | Ubiquitination | VNWEKLYKYISKYTS CCHHHHHHHHHHHHH | 46.69 | 23749301 |
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 TPS1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TPS1_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 TPS1_YEAST !! |
Kegg Drug | ||||||
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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-13, AND MASSSPECTROMETRY. |