| UniProt ID | COM1_YEAST | |
|---|---|---|
| UniProt AC | P46946 | |
| Protein Name | DNA endonuclease SAE2 | |
| Gene Name | SAE2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 345 | |
| Subcellular Localization | Cytoplasm . Nucleus . Accumulates in foci at the precise time when MRE11 foci disassemble and RAD52 foci assemble (PubMed:18670132). Remains associated with DSBs along with MRE11 in nuclease-deficient cells (PubMed:18670132). | |
| Protein Description | Endonuclease that cooperates with the MRX complex in processing meiotic and mitotic double-strand breaks by allowing the endonucleolytic removal of SPO11 from the break sites and ensuring both resection and intrachromosomal association of the broken ends. Required for proper recovery from checkpoint-mediated cell cycle arrest after DNA damage. MRX complex and SAE2 remove a small oligonucleotide(s) from the DNA ends to form an early intermediate which is rapidly processed by EXO1 and/or SGS1 to generate extensive tracts of single-stranded DNA that serve as substrate for RAD51. Plays a transitional role in the dissociation of MRE11 from, and the recruitment of RAD52 to, repair foci. Ensures that both ends of a DSB participate in a recombination event and impairs the formation of palindromic structures in the genome. With TEL1, promotes microhomology-mediated end joining (MMEJ) but inhibits non-homologous end joining (NHEJ), likely by regulating MRE11-dependent ssDNA accumulation at DNA break. SAE2 and MRX are particularly important for removal of hairpins, bulky adducts and other irregular end structures. Facilitates telomere length reequilibration and subsequent checkpoint switch off. Involved in homing efficiency of VMA1 intein VDE and in repair of transposon excision sites.. | |
| Protein Sequence | MVTGEENVYLKSSLSILKELSLDELLNVQYDVTTLIAKRVQALQNRNKCVLEEPNSKLAEILCHEKNAPQQSSQTSAGPGEQDSEDFILTQFDEDIKKESAEVHYRNENKHTVQLPLVTMPPNRHKRKISEFSSPLNGLNNLSDLEDCSDTVIHEKDNDKENKTRKLLGIELENPESTSPNLYKNVKDNFLFDFNTNPLTKRAWILEDFRPNEDIAPVKRGRRKLERFYAQVGKPEDSKHRSLSVVIESQNSDYEFAFDNLRNRSKSPPGFGRLDFPSTQEGNEDKKKSQEIIRRKTKYRFLMASNNKIPPYEREYVFKREQLNQIVDDGCFFWSDKLLQIYARC | |
| 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 |
|---|---|---|---|---|---|
| 73 | Phosphorylation | KNAPQQSSQTSAGPG CCCCCCCCCCCCCCC | 32.89 | 23749301 | |
| 76 | Phosphorylation | PQQSSQTSAGPGEQD CCCCCCCCCCCCCCC | 24.48 | 23749301 | |
| 90 | Phosphorylation | DSEDFILTQFDEDIK CHHCEEECCCCHHHH | 23.52 | 18670132 | |
| 133 | Phosphorylation | KRKISEFSSPLNGLN CCCHHHCCCCCCCCC | 27.31 | 21551504 | |
| 134 | Phosphorylation | RKISEFSSPLNGLNN CCHHHCCCCCCCCCC | 38.43 | 21440633 | |
| 143 | Phosphorylation | LNGLNNLSDLEDCSD CCCCCCHHHHHHCCC | 42.12 | 20377248 | |
| 149 | Phosphorylation | LSDLEDCSDTVIHEK HHHHHHCCCCEEECC | 48.95 | 20377248 | |
| 177 | Phosphorylation | IELENPESTSPNLYK EEECCCCCCCCCHHH | 35.13 | 28889911 | |
| 178 | Phosphorylation | ELENPESTSPNLYKN EECCCCCCCCCHHHH | 46.68 | 24961812 | |
| 179 | Phosphorylation | LENPESTSPNLYKNV ECCCCCCCCCHHHHC | 22.52 | 21551504 | |
| 249 | Phosphorylation | SLSVVIESQNSDYEF EEEEEEEECCCCCEE | 24.44 | 18670132 | |
| 265 | Phosphorylation | FDNLRNRSKSPPGFG HHHHHCCCCCCCCCC | 40.82 | 28889911 | |
| 267 | Phosphorylation | NLRNRSKSPPGFGRL HHHCCCCCCCCCCCC | 37.26 | 25521595 | |
| 279 | Phosphorylation | GRLDFPSTQEGNEDK CCCCCCCCCCCCCCH | 30.77 | 18670132 | |
| 289 | Phosphorylation | GNEDKKKSQEIIRRK CCCCHHHHHHHHHHH | 41.76 | 18670132 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 267 | S | Phosphorylation | Kinase | CDC28 | P00546 | Uniprot |
* 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 COM1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Processing of meiotic DNA double strand breaks requires cyclin-dependent kinase and multiple nucleases."; Manfrini N., Guerini I., Citterio A., Lucchini G., Longhese M.P.; J. Biol. Chem. 285:11628-11637(2010). Cited for: FUNCTION, MUTAGENESIS OF SER-267, AND PHOSPHORYLATION AT SER-267. | |
| "CDK targets Sae2 to control DNA-end resection and homologousrecombination."; Huertas P., Cortes-Ledesma F., Sartori A.A., Aguilera A.,Jackson S.P.; Nature 455:689-692(2008). Cited for: FUNCTION, MUTAGENESIS OF ARG-223; LEU-225 AND SER-267, ANDPHOSPHORYLATION AT SER-267. | |
| "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-177, AND MASSSPECTROMETRY. | |
