| UniProt ID | POP2_YEAST | |
|---|---|---|
| UniProt AC | P39008 | |
| Protein Name | Poly(A) ribonuclease POP2 | |
| Gene Name | POP2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 433 | |
| Subcellular Localization | Cytoplasm . Nucleus . | |
| Protein Description | Acts as probably catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. In vitro, POP2 has 3'-exoribonuclease activity with a preference for poly(A) RNAs, but also degrades poly(U) and poly(C) RNAs. Is part of a glucose-sensing system involved in growth control in response to glucose availability.. | |
| Protein Sequence | MQSMNVQPRVLAVGGEQFFSQRQASEQHQQQNMGPQVYSPKVNRARMFPQGMPVNTINGSVNQEMNNAYLLKQKNEPLLTQQQQQQQQQQQPFNIGTPVSVASLPPGLNVLQQQQQQQQQQQQQQQGVGLNRPLASQLPKHLTNQSMPPIFLPPPNYLFVRDVWKSNLYSEFAVIRQLVSQYNHVSISTEFVGTLARPIGTFRSKVDYHYQTMRANVDFLNPIQLGLSLSDANGNKPDNGPSTWQFNFEFDPKKEIMSTESLELLRKSGINFEKHENLGIDVFEFSQLLMDSGLMMDDSVTWITYHAAYDLGFLINILMNDSMPNNKEDFEWWVHQYMPNFYDLNLVYKIIQEFKNPQLQQSSQQQQQQQYSLTTLADELGLPRFSIFTTTGGQSLLMLLSFCQLSKLSMHKFPNGTDFAKYQGVIYGIDGDQ | |
| 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 | -------MQSMNVQP -------CCCCCCCC | 6.33 | 22814378 | |
| 25 | Phosphorylation | FFSQRQASEQHQQQN HHCHHHHHHHHHHHC | 29.47 | 22890988 | |
| 38 | Phosphorylation | QNMGPQVYSPKVNRA HCCCCCCCCCCCCHH | 17.63 | 22890988 | |
| 39 | Phosphorylation | NMGPQVYSPKVNRAR CCCCCCCCCCCCHHC | 21.27 | 22369663 | |
| 97 | Phosphorylation | QQPFNIGTPVSVASL HCCCCCCCCCCHHHC | 19.40 | 14618157 | |
| 228 | Phosphorylation | NPIQLGLSLSDANGN CHHHHCCCHHHCCCC | 24.83 | 28132839 | |
| 230 | Phosphorylation | IQLGLSLSDANGNKP HHHCCCHHHCCCCCC | 31.16 | 28132839 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 97 | T | Phosphorylation | Kinase | YAK1 | P14680 | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of POP2_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 POP2_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-39, AND MASSSPECTROMETRY. | |
| "Yak1p, a DYRK family kinase, translocates to the nucleus andphosphorylates yeast Pop2p in response to a glucose signal."; Moriya H., Shimizu-Yoshida Y., Omori A., Iwashita S., Katoh M.,Sakai A.; Genes Dev. 15:1217-1228(2001). Cited for: PHOSPHORYLATION AT THR-97, AND MUTAGENESIS OF THR-97. | |
