| UniProt ID | PP12_YEAST | |
|---|---|---|
| UniProt AC | P32598 | |
| Protein Name | Serine/threonine-protein phosphatase PP1-2 | |
| Gene Name | GLC7 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 312 | |
| Subcellular Localization | Cytoplasm . Nucleus . | |
| Protein Description | Involved in control of glycogen metabolism, meiosis, translation, chromosome segregation, cell polarity and G2/M cell cycle progression. PP1 may act in opposition to the IPL1 protein kinase in regulating chromosome segregation by dephosphorylating H3S10ph. The BUD14-GLC7 complex is necessary to regulate microtubule dynamics at the cortex and may function as a specific activator of the dynein complex.; Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Component of the APT complex, which may be involved in polyadenylation-independent transcript 3'-end formation.. | |
| Protein Sequence | MDSQPVDVDNIIDRLLEVRGSKPGQQVDLEENEIRYLCSKARSIFIKQPILLELEAPIKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFILRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIIDEKIFCMHGGLSPDLNSMEQIRRVMRPTDIPDVGLLCDLLWSDPDKDIVGWSENDRGVSFTFGPDVVNRFLQKQDMELICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGAMMSVDESLLCSFQILKPAQKSLPRQAGGRKKK | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MDSQPVDV -------CCCCCCCH | 11.46 | 22814378 | |
| 3 | Phosphorylation | -----MDSQPVDVDN -----CCCCCCCHHH | 34.78 | 20190278 | |
| 21 | Phosphorylation | RLLEVRGSKPGQQVD HHHHHHCCCCCCCCC | 25.72 | 30377154 | |
| 22 | Ubiquitination | LLEVRGSKPGQQVDL HHHHHCCCCCCCCCC | 56.86 | 23749301 | |
| 40 | Ubiquitination | EIRYLCSKARSIFIK HHHHHHHHCHHHHCC | 46.99 | 23749301 | |
| 47 | Ubiquitination | KARSIFIKQPILLEL HCHHHHCCCCEEEEE | 38.99 | 24961812 | |
| 47 | Acetylation | KARSIFIKQPILLEL HCHHHHCCCCEEEEE | 38.99 | 24489116 | |
| 112 | Ubiquitination | LLLAYKIKYPENFFI HHHHHHCCCCCCEEE | 51.07 | 23749301 | |
| 140 | Acetylation | YGFYDECKRRYNIKL EEEHHHHHHHHCCCC | 37.55 | 24489116 | |
| 146 | Ubiquitination | CKRRYNIKLWKTFTD HHHHHCCCCCHHHHH | 44.66 | 23749301 | |
| 146 | Acetylation | CKRRYNIKLWKTFTD HHHHHCCCCCHHHHH | 44.66 | 24489116 | |
| 149 | Ubiquitination | RYNIKLWKTFTDCFN HHCCCCCHHHHHHCC | 44.17 | 23749301 | |
| 167 | Ubiquitination | IAAIIDEKIFCMHGG HHHHHCCCEECCCCC | 37.02 | 17644757 | |
| 176 | Phosphorylation | FCMHGGLSPDLNSME ECCCCCCCCCCCHHH | 21.46 | 28889911 | |
| 216 | Phosphorylation | DKDIVGWSENDRGVS CCCCCCCCCCCCCCC | 22.16 | 25371407 | |
| 237 | Ubiquitination | VVNRFLQKQDMELIC HHHHHHHHHCHHHHH | 50.87 | 23749301 | |
| 259 | Ubiquitination | DGYEFFSKRQLVTLF HCHHHCCHHCEEECC | 38.72 | 23749301 | |
| 259 | Acetylation | DGYEFFSKRQLVTLF HCHHHCCHHCEEECC | 38.72 | 24489116 | |
| 300 | Acetylation | QILKPAQKSLPRQAG HHCCHHHHCCCCCCC | 56.94 | 25381059 | |
| 301 | Phosphorylation | ILKPAQKSLPRQAGG HCCHHHHCCCCCCCC | 31.37 | 19795423 |
| 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 PP12_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PP12_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 PP12_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-176, AND MASSSPECTROMETRY. | |
