UniProt ID | RNH2C_YEAST | |
---|---|---|
UniProt AC | Q12338 | |
Protein Name | Ribonuclease H2 subunit C | |
Gene Name | RNH203 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 110 | |
Subcellular Localization | Cytoplasm . Nucleus . | |
Protein Description | Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.. | |
Protein Sequence | MTKDAVNLDAYTVSFMPFYTEYQGPTEEFKDYKFEDTIYFRGKELKREKSATPSSSDNTTSNTFSNGAILSGNTITGKIVSVNNYEREGTDRNELARLQELISLIDVINQ | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
50 | Phosphorylation | KELKREKSATPSSSD EECCCCCCCCCCCCC | 32.40 | 23749301 | |
56 | Phosphorylation | KSATPSSSDNTTSNT CCCCCCCCCCCCCCC | 38.94 | 23749301 | |
59 | Phosphorylation | TPSSSDNTTSNTFSN CCCCCCCCCCCCCCC | 36.27 | 27017623 |
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 RNH2C_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RNH2C_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 RNH2C_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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