| UniProt ID | PUB1_YEAST | |
|---|---|---|
| UniProt AC | P32588 | |
| Protein Name | Nuclear and cytoplasmic polyadenylated RNA-binding protein PUB1 | |
| Gene Name | PUB1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 453 | |
| Subcellular Localization | Cytoplasm. Nucleus. | |
| Protein Description | May be associated with hnRNA within the nucleus and remains associated during nucleocytoplasmic mRNA transport, once the proteins are in the cytoplasm, disassembly of PUB1-RNA complexes may occur prior to PAB1 binding and formation of a translationally competent RNP complex. Binds to polyadenylated RNA; prefers to bind poly(rU); binds to T-rich single-stranded DNA.. | |
| Protein Sequence | MSENNEEQHQQQQQQQPVAVETPSAVEAPASADPSSEQSVAVEGNSEQAEDNQGENDPSVVPANAITGGRETSDRVLYVGNLDKAITEDILKQYFQVGGPIANIKIMIDKNNKNVNYAFVEYHQSHDANIALQTLNGKQIENNIVKINWAFQSQQSSSDDTFNLFVGDLNVNVDDETLRNAFKDFPSYLSGHVMWDMQTGSSRGYGFVSFTSQDDAQNAMDSMQGQDLNGRPLRINWAAKRDNNNNNNYQQRRNYGNNNRGGFRQYNSNNNNNMNMGMNMNMNMNMNNSRGMPPSSMGMPIGAMPLPSQGQPQQSQTIGLPPQVNPQAVDHIIRSAPPRVTTAYIGNIPHFATEADLIPLFQNFGFILDFKHYPEKGCCFIKYDTHEQAAVCIVALANFPFQGRNLRTGWGKERSNFMPQQQQQGGQPLIMNDQQQPVMSEQQQQQQQQQQQQ | |
| 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 | Acetylation | ------MSENNEEQH ------CCCCHHHHH | 49.37 | 9298649 | |
| 84 | Acetylation | LYVGNLDKAITEDIL EEEECCCHHHHHHHH | 44.87 | 24489116 | |
| 92 | Acetylation | AITEDILKQYFQVGG HHHHHHHHHHHCCCC | 43.20 | 24489116 | |
| 110 | Acetylation | NIKIMIDKNNKNVNY EEEEEEECCCCEEEE | 52.04 | 25381059 | |
| 209 | Phosphorylation | SRGYGFVSFTSQDDA CCCCEEEEECCHHHH | 22.12 | 27017623 | |
| 240 | Ubiquitination | LRINWAAKRDNNNNN CEEEEEECCCCCCCC | 53.16 | 22106047 | |
| 268 | Phosphorylation | GGFRQYNSNNNNNMN CCCCCCCCCCCCCCC | 35.68 | 28132839 | |
| 289 | Phosphorylation | MNMNMNNSRGMPPSS CCCCCCCCCCCCCHH | 25.80 | 28889911 | |
| 376 | Acetylation | DFKHYPEKGCCFIKY EECCCCCCCEEEEEE | 53.39 | 25381059 | |
| 415 | Phosphorylation | TGWGKERSNFMPQQQ CCCCCCCCCCCHHHH | 35.20 | 29136822 | |
| 440 | Phosphorylation | DQQQPVMSEQQQQQQ CCCCCCCCHHHHHHH | 32.27 | 29136822 |
| 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 PUB1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PUB1_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 PUB1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Proteome studies of Saccharomyces cerevisiae: identification andcharacterization of abundant proteins."; Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,Kobayashi R., Schwender B., Volpe T., Anderson D.S.,Mesquita-Fuentes R., Payne W.E.; Electrophoresis 18:1347-1360(1997). Cited for: ACETYLATION AT SER-2. | |
