| UniProt ID | MCM7_YEAST | |
|---|---|---|
| UniProt AC | P38132 | |
| Protein Name | DNA replication licensing factor MCM7 | |
| Gene Name | MCM7 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 845 | |
| Subcellular Localization | Cytoplasm . Nucleus . | |
| Protein Description | Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity.. | |
| Protein Sequence | MSAALPSIQLPVDYNNLFNEITDFLVTFKQDTLSSDATRNENEDENLDAENIEQHLLEKGPKYMAMLQKVANRELNSVIIDLDDILQYQNEKFLQGTQADDLVSAIQQNANHFTELFCRAIDNNMPLPTKEIDYKDDVLDVILNQRRLRNERMLSDRTNEIRSENLMDTTMDPPSSMNDALREVVEDETELFPPNLTRRYFLYFKPLSQNCARRYRKKAISSKPLSVRQIKGDFLGQLITVRGIITRVSDVKPAVEVIAYTCDQCGYEVFQEVNSRTFTPLSECTSEECSQNQTKGQLFMSTRASKFSAFQECKIQELSQQVPVGHIPRSLNIHVNGTLVRSLSPGDIVDVTGIFLPAPYTGFKALKAGLLTETYLEAQFVRQHKKKFASFSLTSDVEERVMELITSGDVYNRLAKSIAPEIYGNLDVKKALLLLLVGGVDKRVGDGMKIRGDINVCLMGDPGVAKSQLLKAICKISPRGVYTTGKGSSGVGLTAAVMKDPVTDEMILEGGALVLADNGICCIDEFDKMDESDRTAIHEVMEQQTISISKAGINTTLNARTSILAAANPLYGRYNPRLSPLDNINLPAALLSRFDILFLMLDIPSRDDDEKLAEHVTYVHMHNKQPDLDFTPVEPSKMREYIAYAKTKRPVMSEAVNDYVVQAYIRLRQDSKREMDSKFSFGQATPRTLLGIIRLSQALAKLRLADMVDIDDVEEALRLVRVSKESLYQETNKSKEDESPTTKIFTIIKKMLQETGKNTLSYENIVKTVRLRGFTMLQLSNCIQEYSYLNVWHLINEGNTLKFVDDGTMDTDQEDSLVSTPKLAPQTTASANVSAQDSDIDLQDA | |
| 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 |
|---|---|---|---|---|---|
| 22 | Phosphorylation | NNLFNEITDFLVTFK HHHHHHHHHHHHHCC | 17.96 | 30377154 | |
| 27 | Phosphorylation | EITDFLVTFKQDTLS HHHHHHHHCCCCCCC | 27.54 | 30377154 | |
| 92 | Ubiquitination | ILQYQNEKFLQGTQA HHHHCHHHHHCCCCH | 59.95 | 17644757 | |
| 97 | Phosphorylation | NEKFLQGTQADDLVS HHHHHCCCCHHHHHH | 13.97 | 21070963 | |
| 197 | Phosphorylation | ELFPPNLTRRYFLYF CCCCCCCCCCEEEEE | 21.53 | 27017623 | |
| 205 | Ubiquitination | RRYFLYFKPLSQNCA CCEEEEECCCCHHHH | 31.34 | 17644757 | |
| 231 | Ubiquitination | PLSVRQIKGDFLGQL CCCHHHCCCCHHHHH | 44.05 | 17644757 | |
| 279 | Phosphorylation | EVNSRTFTPLSECTS HHHCCCCCCHHHCCC | 23.78 | 27214570 | |
| 295 | Ubiquitination | ECSQNQTKGQLFMST HHHCCCCCCCEEEEC | 34.59 | 17644757 | |
| 344 | Phosphorylation | GTLVRSLSPGDIVDV CEEEECCCCCCEEEE | 28.25 | 21070963 | |
| 364 | Ubiquitination | PAPYTGFKALKAGLL CCCCCCHHHHHHCCC | 54.90 | 17644757 | |
| 488 | Phosphorylation | VYTTGKGSSGVGLTA EEECCCCCCCCCCCE | 27.66 | 19684113 | |
| 489 | Phosphorylation | YTTGKGSSGVGLTAA EECCCCCCCCCCCEE | 46.28 | 19684113 | |
| 631 | Phosphorylation | KQPDLDFTPVEPSKM CCCCCCCCCCCCHHH | 26.54 | 27017623 | |
| 724 | Ubiquitination | LRLVRVSKESLYQET HHHHHHCHHHHHHHH | 48.76 | 23749301 | |
| 742 | Phosphorylation | KEDESPTTKIFTIIK CCCCCHHHHHHHHHH | 26.06 | 24930733 | |
| 808 | Phosphorylation | LKFVDDGTMDTDQED EEEECCCCCCCCCCC | 20.90 | 22369663 | |
| 811 | Phosphorylation | VDDGTMDTDQEDSLV ECCCCCCCCCCCCCC | 28.85 | 22369663 | |
| 816 | Phosphorylation | MDTDQEDSLVSTPKL CCCCCCCCCCCCCCC | 29.89 | 22369663 | |
| 819 | Phosphorylation | DQEDSLVSTPKLAPQ CCCCCCCCCCCCCCC | 44.26 | 22369663 | |
| 820 | Phosphorylation | QEDSLVSTPKLAPQT CCCCCCCCCCCCCCC | 19.57 | 22369663 | |
| 827 | Phosphorylation | TPKLAPQTTASANVS CCCCCCCCCCCCCCC | 24.22 | 22369663 | |
| 828 | Phosphorylation | PKLAPQTTASANVSA CCCCCCCCCCCCCCC | 17.23 | 22369663 | |
| 830 | Phosphorylation | LAPQTTASANVSAQD CCCCCCCCCCCCCCC | 20.48 | 22369663 | |
| 834 | Phosphorylation | TTASANVSAQDSDID CCCCCCCCCCCCCCC | 21.73 | 22369663 | |
| 838 | Phosphorylation | ANVSAQDSDIDLQDA CCCCCCCCCCCCCCC | 25.12 | 20377248 |
| 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 MCM7_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MCM7_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 MCM7_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| 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-811; SER-816 ANDSER-819, AND MASS SPECTROMETRY. | |
| "Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-811 AND SER-819, ANDMASS SPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-811, AND MASSSPECTROMETRY. | |
