| UniProt ID | PCNA_YEAST | |
|---|---|---|
| UniProt AC | P15873 | |
| Protein Name | Proliferating cell nuclear antigen | |
| Gene Name | POL30 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 258 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Involved in DNA repair.. | |
| Protein Sequence | MLEAKFEEASLFKRIIDGFKDCVQLVNFQCKEDGIIAQAVDDSRVLLVSLEIGVEAFQEYRCDHPVTLGMDLTSLSKILRCGNNTDTLTLIADNTPDSIILLFEDTKKDRIAEYSLKLMDIDADFLKIEELQYDSTLSLPSSEFSKIVRDLSQLSDSINIMITKETIKFVADGDIGSGSVIIKPFVDMEHPETSIKLEMDQPVDLTFGAKYLLDIIKGSSLSDRVGIRLSSEAPALFQFDLKSGFLQFFLAPKFNDEE | |
| 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 |
|---|---|---|---|---|---|
| 13 | Acetylation | FEEASLFKRIIDGFK HHHHHHHHHHHHHHH | 48.24 | 24489116 | |
| 13 | Succinylation | FEEASLFKRIIDGFK HHHHHHHHHHHHHHH | 48.24 | 23954790 | |
| 77 | Ubiquitination | MDLTSLSKILRCGNN CCHHHHHHHHCCCCC | 51.56 | 23749301 | |
| 127 | Sumoylation | DIDADFLKIEELQYD CCCCCEEEEEECCCC | 48.33 | - | |
| 127 | Sumoylation | DIDADFLKIEELQYD CCCCCEEEEEECCCC | 48.33 | 15166219 | |
| 152 | Phosphorylation | SKIVRDLSQLSDSIN HHHHHHHHHHCCCEE | 33.11 | 19779198 | |
| 155 | Phosphorylation | VRDLSQLSDSINIMI HHHHHHHCCCEEEEE | 22.98 | 19779198 | |
| 164 | Sumoylation | SINIMITKETIKFVA CEEEEEEHHEEEEEE | 41.77 | - | |
| 164 | Ubiquitination | SINIMITKETIKFVA CEEEEEEHHEEEEEE | 41.77 | 23749301 | |
| 164 | Sumoylation | SINIMITKETIKFVA CEEEEEEHHEEEEEE | 41.77 | 15166219 | |
| 217 | Ubiquitination | KYLLDIIKGSSLSDR HHHHHHHCCCCHHHC | 53.74 | 24961812 | |
| 217 | Acetylation | KYLLDIIKGSSLSDR HHHHHHHCCCCHHHC | 53.74 | 24489116 |
* 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 PCNA_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Sumoylation | |
| Reference | PubMed |
| "A proteomic strategy for gaining insights into protein sumoylation inyeast."; Denison C., Rudner A.D., Gerber S.A., Bakalarski C.E., Moazed D.,Gygi S.P.; Mol. Cell. Proteomics 4:246-254(2005). Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-164, AND MASS SPECTROMETRY. | |
| "Global analyses of sumoylated proteins in Saccharomyces cerevisiae.Induction of protein sumoylation by cellular stresses."; Zhou W., Ryan J.J., Zhou H.; J. Biol. Chem. 279:32262-32268(2004). Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-127 AND LYS-164, AND MASSSPECTROMETRY. | |
| "RAD6-dependent DNA repair is linked to modification of PCNA byubiquitin and SUMO."; Hoege C., Pfander B., Moldovan G.-L., Pyrowolakis G., Jentsch S.; Nature 419:135-141(2002). Cited for: FUNCTION, SUMOYLATION AT LYS-127 AND LYS-164, UBIQUITINATION ATLYS-164, AND MASS SPECTROMETRY. | |
