| UniProt ID | DDC1_YEAST | |
|---|---|---|
| UniProt AC | Q08949 | |
| Protein Name | DNA damage checkpoint protein 1 | |
| Gene Name | DDC1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 612 | |
| Subcellular Localization | Cytoplasm. Nucleus. | |
| Protein Description | Component of the checkpoint clamp complex involved in the surveillance mechanism that allows the DNA repair pathways to act to restore the integrity of the DNA prior to DNA synthesis or separation of the replicated chromosomes. Associates with sites of DNA damage and modulates the MEC1 signaling pathway and the activation of RAD53 in response to DNA damage at phase G1. The complex also physically regulates DNA polymerase zeta-dependent mutagenesis by controlling the access of polymerase zeta to damaged DNA.. | |
| Protein Sequence | MSFKATITESGKQNIWFRAIYVLSTIQDDIKITVTTNELIAWSMNETDTTLCQVRFQKSFFEEYEFKPHEIVFGENGVQVIEDTYGNSHKLYSFRVNGRHLTTISRKPDGDGIKSFTIAVNNTSTCPESLANRLIVVIEMDSLIVKEYCPQFQPIKYDPIIINLKYKRRFLDVFGTAASDRNPQEPLDPKLLDVFTNTERELTSALFNEEVESDIRKRNQLTAADEINYICCNSTLLKNFLDNCNVNVTDEVKLEINVHRLSITAFTKAVYGKNNDLLRNALSMSNTISTLDLEHYCLFTTIEDEKQDKRSHSKRREHMKSIIFKLKDFKNFITIGPSWKTTQDGNDNISLWFCHPGDPILMQMQKPGVKLELVEVTDSNINDDILEGKFIKTAISGSKEEAGLKDNKESCESPLKSKTALKRENLPHSVAGTRNSPLKVSYLTPDNGSTVAKTYRNNTARKLFVEEQSQSTNYEQDKRFRQASSVHMNMNREQSFDIGTTHEVACPRNESNSLKRSIADICNETEDPTQQSTFAKRADTTVTWGKALPAADDEVSCSNIDRKGMLKKEKLKHMQGLLNSQNDTSNHKKQDNKEMEDGLGLTQVEKPRGIFD | |
| 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 |
|---|---|---|---|---|---|
| 342 | Phosphorylation | IGPSWKTTQDGNDNI ECCCCEECCCCCCCE | 22.42 | 20005839 | |
| 398 | Phosphorylation | IKTAISGSKEEAGLK HHHHHCCCHHHHCCC | 30.06 | 27214570 | |
| 410 | Phosphorylation | GLKDNKESCESPLKS CCCCCHHHCCCCCCC | 25.46 | 30377154 | |
| 413 | Phosphorylation | DNKESCESPLKSKTA CCHHHCCCCCCCHHH | 39.60 | 23749301 | |
| 429 | Phosphorylation | KRENLPHSVAGTRNS HHCCCCCCCCCCCCC | 16.24 | 22369663 | |
| 433 | Phosphorylation | LPHSVAGTRNSPLKV CCCCCCCCCCCCCEE | 19.55 | 22369663 | |
| 436 | Phosphorylation | SVAGTRNSPLKVSYL CCCCCCCCCCEEEEE | 28.46 | 22369663 | |
| 444 | Phosphorylation | PLKVSYLTPDNGSTV CCEEEEECCCCCCCE | 21.99 | 27214570 | |
| 469 | Phosphorylation | KLFVEEQSQSTNYEQ HEEEEHHHCCCCHHH | 29.40 | 20005839 | |
| 495 | Phosphorylation | MNMNREQSFDIGTTH CCCCHHHCCCCCCCC | 21.82 | 22369663 | |
| 500 | Phosphorylation | EQSFDIGTTHEVACP HHCCCCCCCCEEECC | 25.88 | 22369663 | |
| 511 | Phosphorylation | VACPRNESNSLKRSI EECCCCCCCCHHHHH | 34.96 | 30377154 | |
| 515 | Acetylation | RNESNSLKRSIADIC CCCCCCHHHHHHHHH | 43.87 | 25381059 | |
| 517 | Phosphorylation | ESNSLKRSIADICNE CCCCHHHHHHHHHHC | 22.12 | 27017623 | |
| 529 | Phosphorylation | CNETEDPTQQSTFAK HHCCCCCHHHCHHHH | 52.11 | 20005839 | |
| 543 | Phosphorylation | KRADTTVTWGKALPA HHCCCEEECCCCCCC | 26.80 | 27214570 | |
| 580 | Phosphorylation | HMQGLLNSQNDTSNH HHHHHHHCCCCCCCC | 30.26 | 21440633 | |
| 602 | Phosphorylation | MEDGLGLTQVEKPRG CCCCCCCCCCCCCCC | 28.86 | 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 DDC1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DDC1_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 DDC1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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-495, AND MASSSPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436, AND MASSSPECTROMETRY. | |
