| UniProt ID | LSM4_YEAST | |
|---|---|---|
| UniProt AC | P40070 | |
| Protein Name | U6 snRNA-associated Sm-like protein LSm4 | |
| Gene Name | LSM4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 187 | |
| Subcellular Localization | Nucleus . Cytoplasm . | |
| Protein Description | Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner. Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by activating the decapping step. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple spliceosome snRNP complexes containing the U6 snRNA (U4/U6 snRNP, U4/U6.U5 snRNP, and free U6 snRNP). It binds directly to the U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. It probably also is involved in degradation of nuclear pre-mRNA by targeting them for decapping. LSM4 binds specifically to the 3'-terminal U-tract of U6 snRNA. LSM2-LSM8 probably is involved in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA. LSM4, probably in a complex that contains LSM2-LSM7 but not LSM1 or LSM8, associates with the precursor of the RNA component of RNase P (pre-P RNA) and may be involved in maturing pre-P RNA. LSM4 is required for processing of pre-tRNAs, pre-rRNAs and U3 snoRNA.. | |
| Protein Sequence | MLPLYLLTNAKGQQMQIELKNGEIIQGILTNVDNWMNLTLSNVTEYSEESAINSEDNAESSKAVKLNEIYIRGTFIKFIKLQDNIIDKVKQQINSNNNSNSNGPGHKRYYNNRDSNNNRGNYNRRNNNNGNSNRRPYSQNRQYNNSNSSNINNSINSINSNNQNMNNGLGGSVQHHFNSSSPQKVEF | |
| 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 |
|---|---|---|---|---|---|
| 88 | Acetylation | LQDNIIDKVKQQINS CCHHHHHHHHHHHHC | 40.71 | 24489116 | |
| 95 | Phosphorylation | KVKQQINSNNNSNSN HHHHHHHCCCCCCCC | 42.43 | 28889911 | |
| 101 | Phosphorylation | NSNNNSNSNGPGHKR HCCCCCCCCCCCCHH | 42.88 | 28889911 | |
| 107 | Acetylation | NSNGPGHKRYYNNRD CCCCCCCHHCCCCCC | 48.27 | 25381059 | |
| 137 | Phosphorylation | GNSNRRPYSQNRQYN CCCCCCCCCCCCCCC | 22.52 | 26447709 | |
| 138 | Phosphorylation | NSNRRPYSQNRQYNN CCCCCCCCCCCCCCC | 24.54 | 24603354 | |
| 143 | Phosphorylation | PYSQNRQYNNSNSSN CCCCCCCCCCCCCCC | 17.05 | 19779198 | |
| 149 | Phosphorylation | QYNNSNSSNINNSIN CCCCCCCCCCHHHHH | 46.08 | 19779198 | |
| 181 | Phosphorylation | QHHFNSSSPQKVEF- HHHCCCCCCCCCCC- | 31.04 | 28889911 |
| 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 LSM4_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LSM4_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 LSM4_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-181, AND MASSSPECTROMETRY. | |
