UniProt ID | APN1_YEAST | |
---|---|---|
UniProt AC | P22936 | |
Protein Name | DNA-(apurinic or apyrimidinic site) lyase 1 | |
Gene Name | APN1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 367 | |
Subcellular Localization | Nucleus. | |
Protein Description | DNA repair enzyme that cleaves apurinic/apyrimidinic (AP) sites and removes 3'-blocking groups present at single strand breaks of damaged DNA. APN1 accounts for > 97% of both apurinic/ apyrimidinic (AP) lyase and DNA 3'-repair diesterase activities.. | |
Protein Sequence | MPSTPSFVRSAVSKYKFGAHMSGAGGISNSVTNAFNTGCNSFAMFLKSPRKWVSPQYTQEEIDKFKKNCATYNYNPLTDVLPHGQYFINLANPDREKAEKSYESFMDDLNRCEQLGIGLYNLHPGSTLKGDHQLQLKQLASYLNKAIKETKFVKIVLENMAGTGNLVGSSLVDLKEVIGMIEDKSRIGVCIDTCHTFAAGYDISTTETFNNFWKEFNDVIGFKYLSAVHLNDSKAPLGANRDLHERLGQGYLGIDVFRMIAHSEYLQGIPIVLETPYENDEGYGNEIKLMEWLESKSESELLEDKEYKEKNDTLQKLGAKSRKEQLDKFEVKQKKRAGGTKRKKATAEPSDNDILSQMTKKRKTKKE | |
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 |
---|---|---|---|---|---|
3 | Phosphorylation | -----MPSTPSFVRS -----CCCCHHHHHH | 52.21 | 22369663 | |
4 | Phosphorylation | ----MPSTPSFVRSA ----CCCCHHHHHHH | 19.65 | 22369663 | |
54 | Phosphorylation | KSPRKWVSPQYTQEE HCCCCCCCCCCCHHH | 12.74 | 27017623 | |
57 | Phosphorylation | RKWVSPQYTQEEIDK CCCCCCCCCHHHHHH | 17.49 | 27017623 | |
58 | Phosphorylation | KWVSPQYTQEEIDKF CCCCCCCCHHHHHHH | 25.02 | 27017623 | |
295 | Phosphorylation | KLMEWLESKSESELL HHHHHHHCCCHHHHH | 39.03 | 22369663 | |
297 | Phosphorylation | MEWLESKSESELLED HHHHHCCCHHHHHCC | 56.48 | 22369663 | |
299 | Phosphorylation | WLESKSESELLEDKE HHHCCCHHHHHCCHH | 40.41 | 21440633 | |
316 | Acetylation | EKNDTLQKLGAKSRK HHHHHHHHHHHHHHH | 52.59 | 22865919 | |
328 | Acetylation | SRKEQLDKFEVKQKK HHHHHHHHHHHHHHH | 52.60 | 24489116 | |
346 | Phosphorylation | GTKRKKATAEPSDND CCCCCCCCCCCCHHH | 40.20 | 28889911 | |
350 | Phosphorylation | KKATAEPSDNDILSQ CCCCCCCCHHHHHHH | 40.32 | 25752575 | |
356 | Phosphorylation | PSDNDILSQMTKKRK CCHHHHHHHHHHHCC | 20.45 | 28889911 | |
359 | Phosphorylation | NDILSQMTKKRKTKK HHHHHHHHHHCCCCC | 26.27 | 30377154 | |
360 | Acetylation | DILSQMTKKRKTKKE HHHHHHHHHCCCCCC | 45.28 | 25381059 |
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 APN1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of APN1_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 APN1_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 THR-4, AND MASSSPECTROMETRY. |