| UniProt ID | PRI1_YEAST | |
|---|---|---|
| UniProt AC | P10363 | |
| Protein Name | DNA primase small subunit | |
| Gene Name | PRI1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 409 | |
| Subcellular Localization | ||
| Protein Description | DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication. In a complex with DNA polymerase alpha (DNA polymerase alpha:primase) constitutes a replicative polymerase. Both primase components participate in formation of the active center, but the ATP-binding site is exclusively located on p48.. | |
| Protein Sequence | MTNSVKTNGPSSSDMEYYYKSLYPFKHIFNWLNHSPKPSRDMINREFAMAFRSGAYKRYNSFNSVQDFKAQIEKANPDRFEIGAIYNKPPRERDTLLKSELKALEKELVFDIDMDDYDAFRTCCSGAQVCSKCWKFISLAMKITNTALREDFGYKDFIWVFSGRRGAHCWVSDKRARALTDVQRRNVLDYVNVIRDRNTDKRLALKRPYHPHLARSLEQLKPFFVSIMLEEQNPWEDDQHAIQTLLPALYDKQLIDSLKKYWLDNPRRSSKEKWNDIDQIATSLFKGPKQDSHIIKLRECKEDLVLMTLYPKLDVEVTKQTIHLLKAPFCIHPATGNVCVPIDESFAPEKAPKLIDLQTEMEKNNDVSLTALQPFINQFQAYVSSLLKNELGSVKREREDDDEPASLDF | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MTNSVKTNG ------CCCCCCCCC | 35.88 | 24909858 | |
| 13 | Phosphorylation | KTNGPSSSDMEYYYK CCCCCCHHHHHHHHH | 45.36 | 30377154 | |
| 17 | Phosphorylation | PSSSDMEYYYKSLYP CCHHHHHHHHHHHHC | 12.88 | 30377154 | |
| 18 | Phosphorylation | SSSDMEYYYKSLYPF CHHHHHHHHHHHHCH | 7.36 | 30377154 | |
| 61 | Phosphorylation | GAYKRYNSFNSVQDF CHHHHCCCCCCHHHH | 19.50 | 28889911 | |
| 98 | Acetylation | RERDTLLKSELKALE HHHHHHHHHHHHHHH | 45.02 | 24489116 | |
| 326 | Ubiquitination | KQTIHLLKAPFCIHP HHHHHHHCCCEEECC | 61.44 | 17644757 | |
| 350 | Ubiquitination | DESFAPEKAPKLIDL CCCCCCCCCCCHHHH | 69.77 | 17644757 | |
| 406 | Phosphorylation | EDDDEPASLDF---- CCCCCCCCCCC---- | 38.90 | 22369663 |
| 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 PRI1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PRI1_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 PRI1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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-61 AND SER-406, AND MASSSPECTROMETRY. | |