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 | ||||||
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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-61 AND SER-406, AND MASSSPECTROMETRY. |