| UniProt ID | LSM6_YEAST | |
|---|---|---|
| UniProt AC | Q06406 | |
| Protein Name | U6 snRNA-associated Sm-like protein LSm6 | |
| Gene Name | LSM6 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 86 | |
| Subcellular Localization | Cytoplasm. Nucleus, nucleolus. LSM1 and LSM8 act competitively with respect to the localization of LSM1-LSM7 to the cytoplasm and LSM2-LSM8 to the nucleus. LSm proteins shift to the cytoplasm under conditions of stress. | |
| Protein Description | Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner, facilitating the efficient association of RNA processing factors with their substrates. Component of the cytoplasmic LSM1-LSM7 complex, which is involved in mRNA degradation by activating the decapping step in the 5'-to-3' mRNA decay pathway. In association with PAT1, LSM1-LSM7 binds directly to RNAs near the 3'-end and prefers oligoadenylated RNAs over polyadenylated RNAs. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 di-snRNP, spliceosomal U4/U6.U5 tri-snRNP, and free U6 snRNP). It binds directly to the 3'-terminal U-tract of U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. LSM2-LSM8 probably also is involved degradation of nuclear pre-mRNA by targeting them for decapping, and in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA. Component of a nucleolar LSM2-LSM7 complex, which associates with the precursor of the RNA component of RNase P (pre-P RNA) and with the small nucleolar RNA (snoRNA) snR5. It may play a role in the maturation of a subset of nucleolus-associated small RNAs.. | |
| Protein Sequence | MSGKASTEGSVTTEFLSDIIGKTVNVKLASGLLYSGRLESIDGFMNVALSSATEHYESNNNKLLNKFNSDVFLRGTQVMYISEQKI | |
| 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 | Phosphorylation | ------MSGKASTEG ------CCCCCCCCC | 49.34 | 30377154 | |
| 4 | Ubiquitination | ----MSGKASTEGSV ----CCCCCCCCCCH | 31.68 | 24961812 | |
| 6 | Phosphorylation | --MSGKASTEGSVTT --CCCCCCCCCCHHH | 30.40 | 30377154 | |
| 10 | Phosphorylation | GKASTEGSVTTEFLS CCCCCCCCHHHHHHH | 15.28 | 30377154 | |
| 13 | Phosphorylation | STEGSVTTEFLSDII CCCCCHHHHHHHHHC | 23.68 | 30377154 | |
| 66 | Ubiquitination | NNNKLLNKFNSDVFL CCHHHHHHHCCCCEE | 45.98 | 24961812 | |
| 66 | Acetylation | NNNKLLNKFNSDVFL CCHHHHHHHCCCCEE | 45.98 | 24489116 | |
| 69 | Phosphorylation | KLLNKFNSDVFLRGT HHHHHHCCCCEECCC | 37.98 | 30377154 | |
| 82 | Phosphorylation | GTQVMYISEQKI--- CCEEEEEEECCC--- | 19.25 | 30377154 |
| 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 LSM6_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LSM6_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 LSM6_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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