| UniProt ID | LSM2_YEAST | |
|---|---|---|
| UniProt AC | P38203 | |
| Protein Name | U6 snRNA-associated Sm-like protein LSm2 | |
| Gene Name | LSM2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 95 | |
| 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 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. LSM2 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. LSM2, 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. LSM2 is required for processing of pre-tRNAs, pre-rRNAs and U3 snoRNA.. | |
| Protein Sequence | MLFFSFFKTLVDQEVVVELKNDIEIKGTLQSVDQFLNLKLDNISCTDEKKYPHLGSVRNIFIRGSTVRYVYLNKNMVDTNLLQDATRREVMTERK | |
| 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 |
|---|---|---|---|---|---|
| 39 | Ubiquitination | VDQFLNLKLDNISCT HHHHHCCEECCEECC | 53.36 | 24961812 | |
| 44 | Phosphorylation | NLKLDNISCTDEKKY CCEECCEECCCCCCC | 19.74 | 30377154 | |
| 46 | Phosphorylation | KLDNISCTDEKKYPH EECCEECCCCCCCCC | 40.16 | 30377154 | |
| 49 | Acetylation | NISCTDEKKYPHLGS CEECCCCCCCCCCCC | 61.49 | 25381059 | |
| 50 | Acetylation | ISCTDEKKYPHLGSV EECCCCCCCCCCCCE | 63.06 | 25381059 | |
| 51 | Phosphorylation | SCTDEKKYPHLGSVR ECCCCCCCCCCCCEE | 13.62 | 25521595 | |
| 74 | Acetylation | VRYVYLNKNMVDTNL EEEEEECCCCCCCCH | 43.77 | 24489116 | |
| 79 | Phosphorylation | LNKNMVDTNLLQDAT ECCCCCCCCHHHHHH | 19.16 | 29688323 | |
| 86 | Phosphorylation | TNLLQDATRREVMTE CCHHHHHHHHHHHHC | 38.25 | 29688323 |
| 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 LSM2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LSM2_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 LSM2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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