UniProt ID | PSO2_YEAST | |
---|---|---|
UniProt AC | P30620 | |
Protein Name | DNA cross-link repair protein PSO2/SNM1 | |
Gene Name | PSO2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 661 | |
Subcellular Localization | Nucleus . | |
Protein Description | Required for DNA interstrand cross-link repair. This requires cleavage of cross-linked DNA to generate DNA double strand breaks (DSBs). This protein has 5' exonuclease activity on single-stranded and double-stranded DNA, which appears to be necessary for the processing of DNA double strand breaks prior to ligation.. | |
Protein Sequence | MSRKSIVQIRRSEVKRKRSSTASSTSEGKTLHKNTHTSSKRQRTLTEFNIPTSSNLPVRSSSYSFSRFSCSTSNKNTEPVIINDDDHNSICLEDTAKVEITIDTDEEELVSLHDNEVSAIENRTEDRIVTELEEQVNVKVSTEVIQCPICLENLSHLELYERETHCDTCIGSDPSNMGTPKKNIRSFISNPSSPAKTKRDIATSKKPTRVKLVLPSFKIIKFNNGHEIVVDGFNYKASETISQYFLSHFHSDHYIGLKKSWNNPDENPIKKTLYCSKITAILVNLKFKIPMDEIQILPMNKRFWITDTISVVTLDANHCPGAIIMLFQEFLANSYDKPIRQILHTGDFRSNAKMIETIQKWLAETANETIDQVYLDTTYMTMGYNFPSQHSVCETVADFTLRLIKHGKNKTFGDSQRNLFHFQRKKTLTTHRYRVLFLVGTYTIGKEKLAIKICEFLKTKLFVMPNSVKFSMMLTVLQNNENQNDMWDESLLTSNLHESSVHLVPIRVLKSQETIEAYLKSLKELETDYVKDIEDVVGFIPTGWSHNFGLKYQKKNDDDENEMSGNTEYCLELMKNDRDNDDENGFEISSILRQYKKYNKFQVFNVPYSEHSSFNDLVKFGCKLKCSEVIPTVNLNNLWKVRYMTNWFQCWENVRKTRAAK | |
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 |
---|---|---|---|---|---|
172 | Phosphorylation | HCDTCIGSDPSNMGT CCCCCCCCCHHHCCC | 26.83 | 23749301 | |
175 | Phosphorylation | TCIGSDPSNMGTPKK CCCCCCHHHCCCCCH | 44.43 | 23749301 | |
179 | Phosphorylation | SDPSNMGTPKKNIRS CCHHHCCCCCHHHHH | 22.59 | 23749301 | |
186 | Phosphorylation | TPKKNIRSFISNPSS CCCHHHHHHHHCCCC | 24.12 | 24961812 | |
189 | Phosphorylation | KNIRSFISNPSSPAK HHHHHHHHCCCCCCC | 40.45 | 22369663 | |
192 | Phosphorylation | RSFISNPSSPAKTKR HHHHHCCCCCCCCHH | 53.88 | 20377248 | |
193 | Phosphorylation | SFISNPSSPAKTKRD HHHHCCCCCCCCHHH | 30.08 | 22369663 | |
204 | Phosphorylation | TKRDIATSKKPTRVK CHHHHCCCCCCCEEE | 29.65 | 27017623 | |
260 | Phosphorylation | HYIGLKKSWNNPDEN CEECCCCCCCCCCCC | 33.19 | 25704821 | |
433 | Phosphorylation | KTLTTHRYRVLFLVG CCCCCCCEEEEEEEE | 9.47 | 28889911 | |
442 | Phosphorylation | VLFLVGTYTIGKEKL EEEEEEEEECCHHHH | 7.16 | 28889911 |
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 PSO2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PSO2_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 PSO2_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-189 AND SER-193, ANDMASS SPECTROMETRY. |