| UniProt ID | MCM6_YEAST | |
|---|---|---|
| UniProt AC | P53091 | |
| Protein Name | DNA replication licensing factor MCM6 | |
| Gene Name | MCM6 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1017 | |
| Subcellular Localization | 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. Required for the entry in S phase and for cell division.. | |
| Protein Sequence | MSSPFPADTPSSNRPSNSSPPPSSIGAGFGSSSGLDSQIGSRLHFPSSSQPHVSNSQTGPFVNDSTQFSSQRLQTDGSATNDMEGNEPARSFKSRALNHVKKVDDVTGEKVREAFEQFLEDFSVQSTDTGEVEKVYRAQIEFMKIYDLNTIYIDYQHLSMRENGALAMAISEQYYRFLPFLQKGLRRVVRKYAPELLNTSDSLKRSEGDEGQADEDEQQDDDMNGSSLPRDSGSSAAPGNGTSAMATRSITTSTSPEQTERVFQISFFNLPTVHRIRDIRSEKIGSLLSISGTVTRTSEVRPELYKASFTCDMCRAIVDNVEQSFKYTEPTFCPNPSCENRAFWTLNVTRSRFLDWQKVRIQENANEIPTGSMPRTLDVILRGDSVERAKPGDRCKFTGVEIVVPDVTQLGLPGVKPSSTLDTRGISKTTEGLNSGVTGLRSLGVRDLTYKISFLACHVISIGSNIGASSPDANSNNRETELQMAANLQANNVYQDNERDQEVFLNSLSSDEINELKEMVKDEHIYDKLVRSIAPAVFGHEAVKKGILLQMLGGVHKSTVEGIKLRGDINICVVGDPSTSKSQFLKYVVGFAPRSVYTSGKASSAAGLTAAVVRDEEGGDYTIEAGALMLADNGICCIDEFDKMDISDQVAIHEAMEQQTISIAKAGIHATLNARTSILAAANPVGGRYNRKLSLRGNLNMTAPIMSRFDLFFVILDDCNEKIDTELASHIVDLHMKRDEAIEPPFSAEQLRRYIKYARTFKPILTKEARSYLVEKYKELRKDDAQGFSRSSYRITVRQLESMIRLSEAIARANCVDEITPSFIAEAYDLLRQSIIRVDVDDVEMDEEFDNIESQSHAASGNNDDNDDGTGSGVITSEPPADIEEGQSEATARPGTSEKKKTTVTYDKYVSMMNMIVRKIAEVDREGAEELTAVDIVDWYLLQKENDLGSLAEYWEERRLAFKVIKRLVKDRILMEIHGTRHNLRDLENEENENNKTVYVIHPNCEVLDQLEPQDSS | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSSPFPADT ------CCCCCCCCC | 59.01 | 30377154 | |
| 3 | Phosphorylation | -----MSSPFPADTP -----CCCCCCCCCC | 42.28 | 28889911 | |
| 9 | Phosphorylation | SSPFPADTPSSNRPS CCCCCCCCCCCCCCC | 27.46 | 28889911 | |
| 11 | Phosphorylation | PFPADTPSSNRPSNS CCCCCCCCCCCCCCC | 42.19 | 30377154 | |
| 12 | Phosphorylation | FPADTPSSNRPSNSS CCCCCCCCCCCCCCC | 37.75 | 30377154 | |
| 16 | Phosphorylation | TPSSNRPSNSSPPPS CCCCCCCCCCCCCCC | 46.21 | 30377154 | |
| 18 | Phosphorylation | SSNRPSNSSPPPSSI CCCCCCCCCCCCCCC | 48.86 | 27214570 | |
| 19 | Phosphorylation | SNRPSNSSPPPSSIG CCCCCCCCCCCCCCC | 45.75 | 28889911 | |
| 31 | Phosphorylation | SIGAGFGSSSGLDSQ CCCCCCCCCCCCCCC | 21.04 | 28889911 | |
| 37 | Phosphorylation | GSSSGLDSQIGSRLH CCCCCCCCCCCCCCC | 28.83 | 21070963 | |
| 49 | Phosphorylation | RLHFPSSSQPHVSNS CCCCCCCCCCCCCCC | 52.66 | 21070963 | |
| 56 | Phosphorylation | SQPHVSNSQTGPFVN CCCCCCCCCCCCCCC | 22.93 | 21070963 | |
| 58 | Phosphorylation | PHVSNSQTGPFVNDS CCCCCCCCCCCCCCC | 46.79 | 21440633 | |
| 66 | Phosphorylation | GPFVNDSTQFSSQRL CCCCCCCCCCCCCCC | 36.17 | 21070963 | |
| 70 | Phosphorylation | NDSTQFSSQRLQTDG CCCCCCCCCCCCCCC | 22.17 | 21070963 | |
| 75 | Phosphorylation | FSSQRLQTDGSATND CCCCCCCCCCCCCCC | 47.09 | 22369663 | |
| 78 | Phosphorylation | QRLQTDGSATNDMEG CCCCCCCCCCCCCCC | 34.43 | 22369663 | |
| 80 | Phosphorylation | LQTDGSATNDMEGNE CCCCCCCCCCCCCCC | 33.19 | 22369663 | |
| 91 | Phosphorylation | EGNEPARSFKSRALN CCCCCCHHHHHHHHH | 38.85 | 23749301 | |
| 107 | Phosphorylation | VKKVDDVTGEKVREA CCCHHHCCCHHHHHH | 46.77 | 21440633 | |
| 183 | Acetylation | RFLPFLQKGLRRVVR HHHHHHHHHHHHHHH | 63.16 | 24489116 | |
| 199 | Phosphorylation | YAPELLNTSDSLKRS HHHHHHCCCHHHCCC | 33.60 | 21126336 | |
| 206 | Phosphorylation | TSDSLKRSEGDEGQA CCHHHCCCCCCCCCC | 44.32 | 21440633 | |
| 226 | Phosphorylation | QDDDMNGSSLPRDSG CCCCCCCCCCCCCCC | 24.56 | 23749301 | |
| 227 | Phosphorylation | DDDMNGSSLPRDSGS CCCCCCCCCCCCCCC | 43.73 | 23749301 | |
| 232 | Phosphorylation | GSSLPRDSGSSAAPG CCCCCCCCCCCCCCC | 41.68 | 23749301 | |
| 234 | Phosphorylation | SLPRDSGSSAAPGNG CCCCCCCCCCCCCCC | 22.28 | 22369663 | |
| 235 | Phosphorylation | LPRDSGSSAAPGNGT CCCCCCCCCCCCCCC | 31.79 | 23749301 | |
| 242 | Phosphorylation | SAAPGNGTSAMATRS CCCCCCCCCCEEEEE | 19.81 | 22369663 | |
| 249 | Phosphorylation | TSAMATRSITTSTSP CCCEEEEEEECCCCH | 21.67 | 22369663 | |
| 251 | Phosphorylation | AMATRSITTSTSPEQ CEEEEEEECCCCHHH | 18.88 | 22369663 | |
| 252 | Phosphorylation | MATRSITTSTSPEQT EEEEEEECCCCHHHH | 28.47 | 25371407 | |
| 253 | Phosphorylation | ATRSITTSTSPEQTE EEEEEECCCCHHHHH | 20.45 | 21440633 | |
| 254 | Phosphorylation | TRSITTSTSPEQTER EEEEECCCCHHHHHE | 46.32 | 26447709 | |
| 255 | Phosphorylation | RSITTSTSPEQTERV EEEECCCCHHHHHEE | 26.63 | 25752575 | |
| 259 | Phosphorylation | TSTSPEQTERVFQIS CCCCHHHHHEEEEEE | 24.89 | 26447709 | |
| 358 | Acetylation | SRFLDWQKVRIQENA HHCCCCEEEEEECCC | 29.27 | 24489116 | |
| 372 | Phosphorylation | ANEIPTGSMPRTLDV CCCCCCCCCCCEEEE | 28.26 | 28889911 | |
| 408 | Phosphorylation | EIVVPDVTQLGLPGV EEECCCCCCCCCCCC | 26.00 | 21070963 | |
| 429 | Phosphorylation | DTRGISKTTEGLNSG CCCCCCCCCCCCCCC | 24.24 | 21440633 | |
| 430 | Phosphorylation | TRGISKTTEGLNSGV CCCCCCCCCCCCCCC | 31.62 | 21440633 | |
| 470 | Phosphorylation | GSNIGASSPDANSNN CCCCCCCCCCCCCCC | 26.68 | 27214570 | |
| 509 | Phosphorylation | EVFLNSLSSDEINEL HHHHHHCCHHHHHHH | 35.25 | 27214570 | |
| 766 | Phosphorylation | RTFKPILTKEARSYL HHCHHHCCHHHHHHH | 27.79 | 17330950 | |
| 909 | Phosphorylation | TTVTYDKYVSMMNMI CEEEHHHHHHHHHHH | 8.54 | 27017623 | |
| 911 | Phosphorylation | VTYDKYVSMMNMIVR EEHHHHHHHHHHHHH | 14.82 | 27017623 | |
| 1016 | Phosphorylation | DQLEPQDSS------ HHCCCCCCC------ | 32.47 | 19823750 | |
| 1017 | Phosphorylation | QLEPQDSS------- HCCCCCCC------- | 53.16 | 25521595 |
| 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 MCM6_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MCM6_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 MCM6_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 SER-31; SER-78; SER-249;SER-372; SER-1016 AND SER-1017, AND MASS 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-766, AND MASSSPECTROMETRY. | |
