| UniProt ID | TPM1_YEAST | |
|---|---|---|
| UniProt AC | P17536 | |
| Protein Name | Tropomyosin-1 | |
| Gene Name | TPM1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 199 | |
| Subcellular Localization | Cytoplasm, cytoskeleton . | |
| Protein Description | ||
| Protein Sequence | MDKIREKLSNLKLEAESWQEKYEELKEKNKDLEQENVEKENQIKSLTVKNQQLEDEIEKLEAGLSDSKQTEQDNVEKENQIKSLTVKNHQLEEEIEKLEAELAESKQLSEDSHHLQSNNDNFSKKNQQLEEDLEESDTKLKETTEKLRESDLKADQLERRVAALEEQREEWERKNEELTVKYEDAKKELDEIAASLENL | |
| 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 |
|---|---|---|---|---|---|
| 7 | Acetylation | -MDKIREKLSNLKLE -CHHHHHHHHHCHHH | 47.57 | 24489116 | |
| 9 | Phosphorylation | DKIREKLSNLKLEAE HHHHHHHHHCHHHHH | 51.70 | 19795423 | |
| 12 | Ubiquitination | REKLSNLKLEAESWQ HHHHHHCHHHHHHHH | 48.83 | 24961812 | |
| 12 | Acetylation | REKLSNLKLEAESWQ HHHHHHCHHHHHHHH | 48.83 | 24489116 | |
| 17 | Phosphorylation | NLKLEAESWQEKYEE HCHHHHHHHHHHHHH | 40.90 | 22369663 | |
| 21 | Acetylation | EAESWQEKYEELKEK HHHHHHHHHHHHHHH | 42.75 | 24489116 | |
| 26 | Acetylation | QEKYEELKEKNKDLE HHHHHHHHHHCHHHH | 70.67 | 24489116 | |
| 30 | 2-Hydroxyisobutyrylation | EELKEKNKDLEQENV HHHHHHCHHHHHHHH | 74.82 | - | |
| 30 | Acetylation | EELKEKNKDLEQENV HHHHHHCHHHHHHHH | 74.82 | 24489116 | |
| 39 | Acetylation | LEQENVEKENQIKSL HHHHHHHHHHHHHHH | 58.65 | 24489116 | |
| 39 | Ubiquitination | LEQENVEKENQIKSL HHHHHHHHHHHHHHH | 58.65 | 22106047 | |
| 44 | Acetylation | VEKENQIKSLTVKNQ HHHHHHHHHHHHHCH | 29.64 | 22865919 | |
| 59 | Acetylation | QLEDEIEKLEAGLSD HHHHHHHHHHHHCCC | 58.24 | 24489116 | |
| 59 | Ubiquitination | QLEDEIEKLEAGLSD HHHHHHHHHHHHCCC | 58.24 | 23749301 | |
| 65 | Phosphorylation | EKLEAGLSDSKQTEQ HHHHHHCCCCHHHHH | 38.63 | 22369663 | |
| 67 | Phosphorylation | LEAGLSDSKQTEQDN HHHHCCCCHHHHHHH | 24.24 | 22369663 | |
| 68 | Acetylation | EAGLSDSKQTEQDNV HHHCCCCHHHHHHHH | 67.25 | 24489116 | |
| 68 | Succinylation | EAGLSDSKQTEQDNV HHHCCCCHHHHHHHH | 67.25 | 23954790 | |
| 70 | Phosphorylation | GLSDSKQTEQDNVEK HCCCCHHHHHHHHHH | 39.07 | 22369663 | |
| 77 | Ubiquitination | TEQDNVEKENQIKSL HHHHHHHHHHHHHHH | 58.65 | 23749301 | |
| 82 | Acetylation | VEKENQIKSLTVKNH HHHHHHHHHHHHHCH | 29.64 | 24489116 | |
| 97 | Acetylation | QLEEEIEKLEAELAE HHHHHHHHHHHHHHH | 58.24 | 24489116 | |
| 105 | Phosphorylation | LEAELAESKQLSEDS HHHHHHHHHCCCCCH | 21.79 | 24909858 | |
| 109 | Phosphorylation | LAESKQLSEDSHHLQ HHHHHCCCCCHHHHH | 36.54 | 22369663 | |
| 112 | Phosphorylation | SKQLSEDSHHLQSNN HHCCCCCHHHHHHCC | 14.57 | 22369663 | |
| 117 | Phosphorylation | EDSHHLQSNNDNFSK CCHHHHHHCCCCHHH | 43.91 | 22369663 | |
| 123 | Phosphorylation | QSNNDNFSKKNQQLE HHCCCCHHHHHHHHH | 49.31 | 22369663 | |
| 125 | Ubiquitination | NNDNFSKKNQQLEED CCCCHHHHHHHHHHH | 59.81 | 23749301 | |
| 136 | Phosphorylation | LEEDLEESDTKLKET HHHHHHHHHHHHHHH | 41.00 | 19795423 | |
| 138 | Phosphorylation | EDLEESDTKLKETTE HHHHHHHHHHHHHHH | 47.78 | 19795423 | |
| 139 | Acetylation | DLEESDTKLKETTEK HHHHHHHHHHHHHHH | 63.65 | 24489116 | |
| 141 | Acetylation | EESDTKLKETTEKLR HHHHHHHHHHHHHHH | 55.35 | 24489116 | |
| 141 | 2-Hydroxyisobutyrylation | EESDTKLKETTEKLR HHHHHHHHHHHHHHH | 55.35 | - | |
| 153 | Acetylation | KLRESDLKADQLERR HHHHHHHCHHHHHHH | 55.71 | 24489116 | |
| 153 | Succinylation | KLRESDLKADQLERR HHHHHHHCHHHHHHH | 55.71 | 23954790 | |
| 182 | Phosphorylation | NEELTVKYEDAKKEL CCCCCCCHHHHHHHH | 18.07 | 19779198 | |
| 186 | 2-Hydroxyisobutyrylation | TVKYEDAKKELDEIA CCCHHHHHHHHHHHH | 60.13 | - | |
| 187 | Ubiquitination | VKYEDAKKELDEIAA CCHHHHHHHHHHHHH | 66.29 | 22106047 | |
| 195 | Phosphorylation | ELDEIAASLENL--- HHHHHHHHHHCC--- | 27.48 | 22369663 |
| 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 TPM1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TPM1_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 TPM1_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-195, AND MASSSPECTROMETRY. | |
