| UniProt ID | MCM3_YEAST | |
|---|---|---|
| UniProt AC | P24279 | |
| Protein Name | DNA replication licensing factor MCM3 | |
| Gene Name | MCM3 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 971 | |
| 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. Necessary for cell growth.. | |
| Protein Sequence | MEGSTGFDGDATTFFAPDAVFGDRVRRFQEFLDTFTSYRDSVRSIQVYNSNNAANYNDDQDDADERDLLGDDDGDDLEKEKKAASSTSLNILPHRIIISLDDLREFDRSFWSGILVEPAYFIPPAEKALTDLADSMDDVPHPNASAVSSRHPWKLSFKGSFGAHALSPRTLTAQHLNKLVSVEGIVTKTSLVRPKLIRSVHYAAKTGRFHYRDYTDATTTLTTRIPTPAIYPTEDTEGNKLTTEYGYSTFIDHQRITVQEMPEMAPAGQLPRSIDVILDDDLVDKTKPGDRVNVVGVFKSLGAGGMNQSNSNTLIGFKTLILGNTVYPLHARSTGVAARQMLTDFDIRNINKLSKKKDIFDILSQSLAPSIYGHDHIKKAILLMLMGGVEKNLENGSHLRGDINILMVGDPSTAKSQLLRFVLNTASLAIATTGRGSSGVGLTAAVTTDRETGERRLEAGAMVLADRGVVCIDEFDKMTDVDRVAIHEVMEQQTVTIAKAGIHTTLNARCSVIAAANPVFGQYDVNRDPHQNIALPDSLLSRFDLLFVVTDDINEIRDRSISEHVLRTHRYLPPGYLEGEPVRERLNLSLAVGEDADINPEEHSNSGAGVENEGEDDEDHVFEKFNPLLQAGAKLAKNKGNYNGTEIPKLVTIPFLRKYVQYAKERVIPQLTQEAINVIVKNYTDLRNDDNTKKSPITARTLETLIRLATAHAKVRLSKTVNKVDAKVAANLLRFALLGEDIGNDIDEEESEYEEALSKRSPQKSPKKRQRVRQPASNSGSPIKSTPRRSTASSVNATPSSARRILRFQDDEQNAGEDDNDIMSPLPADEEAELQRRLQLGLRVSPRRREHLHAPEEGSSGPLTEVGTPRLPNVSSAGQDDEQQQSVISFDNVEPGTISTGRLSLISGIIARLMQTEIFEEESYPVASLFERINEELPEEEKFSAQEYLAGLKIMSDRNNLMVADDKVWRV | |
| 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 |
|---|---|---|---|---|---|
| 4 | Phosphorylation | ----MEGSTGFDGDA ----CCCCCCCCCCC | 16.44 | 30377154 | |
| 85 | Phosphorylation | EKEKKAASSTSLNIL HHHHHHHHCCCCCCC | 38.72 | 23749301 | |
| 88 | Phosphorylation | KKAASSTSLNILPHR HHHHHCCCCCCCCCE | 22.74 | 28889911 | |
| 130 | Phosphorylation | PPAEKALTDLADSMD CHHHHHHHHHHHCCC | 33.55 | 27017623 | |
| 145 | Phosphorylation | DVPHPNASAVSSRHP CCCCCCCHHHCCCCC | 35.52 | 27017623 | |
| 148 | Phosphorylation | HPNASAVSSRHPWKL CCCCHHHCCCCCEEE | 22.75 | 27017623 | |
| 178 | Ubiquitination | LTAQHLNKLVSVEGI HHHHHHHHCCCEECE | 57.54 | 17644757 | |
| 202 | Phosphorylation | KLIRSVHYAAKTGRF HHHHHHHHHHHHCCC | 13.19 | 21440633 | |
| 215 | Phosphorylation | RFHYRDYTDATTTLT CCCCCCCCCCCCEEE | 24.36 | 28889911 | |
| 227 | Phosphorylation | TLTTRIPTPAIYPTE EEEEECCCCCCCCCC | 23.99 | 27214570 | |
| 231 | Phosphorylation | RIPTPAIYPTEDTEG ECCCCCCCCCCCCCC | 13.25 | 29650682 | |
| 240 | Ubiquitination | TEDTEGNKLTTEYGY CCCCCCCEEEECCCC | 59.05 | 17644757 | |
| 318 | Ubiquitination | SNTLIGFKTLILGNT CCCEEEEEEEECCCE | 36.89 | 17644757 | |
| 364 | Phosphorylation | KDIFDILSQSLAPSI CCHHHHHHHHCCHHH | 20.32 | 21440633 | |
| 366 | Phosphorylation | IFDILSQSLAPSIYG HHHHHHHHCCHHHHC | 24.11 | 21440633 | |
| 370 | Phosphorylation | LSQSLAPSIYGHDHI HHHHCCHHHHCCHHH | 23.88 | 21440633 | |
| 425 | Phosphorylation | LLRFVLNTASLAIAT HHHHHHHHHCCEEEC | 17.29 | 28889911 | |
| 432 | Phosphorylation | TASLAIATTGRGSSG HHCCEEECCCCCCCC | 24.54 | 28889911 | |
| 433 | Phosphorylation | ASLAIATTGRGSSGV HCCEEECCCCCCCCC | 18.83 | 28889911 | |
| 447 | Phosphorylation | VGLTAAVTTDRETGE CCCEEEEECCCCCCC | 20.46 | 19779198 | |
| 448 | Phosphorylation | GLTAAVTTDRETGER CCEEEEECCCCCCCH | 26.85 | 19779198 | |
| 452 | Phosphorylation | AVTTDRETGERRLEA EEECCCCCCCHHHHH | 45.28 | 19779198 | |
| 634 | Ubiquitination | PLLQAGAKLAKNKGN HHHHHHHHHHHCCCC | 48.32 | 24961812 | |
| 649 | Acetylation | YNGTEIPKLVTIPFL CCCCCCCHHHHHHHH | 62.34 | 24489116 | |
| 695 | Phosphorylation | NDDNTKKSPITARTL CCCCCCCCCCHHHHH | 24.08 | 27017623 | |
| 701 | Phosphorylation | KSPITARTLETLIRL CCCCHHHHHHHHHHH | 26.87 | 27017623 | |
| 710 | Phosphorylation | ETLIRLATAHAKVRL HHHHHHHHHHHHHHH | 24.46 | 23749301 | |
| 751 | Phosphorylation | NDIDEEESEYEEALS CCCCHHHHHHHHHHH | 49.08 | 21440633 | |
| 753 | Phosphorylation | IDEEESEYEEALSKR CCHHHHHHHHHHHHC | 28.48 | 21440633 | |
| 758 | Phosphorylation | SEYEEALSKRSPQKS HHHHHHHHHCCCCCC | 32.82 | 19823750 | |
| 761 | Phosphorylation | EEALSKRSPQKSPKK HHHHHHCCCCCCHHH | 35.10 | 19823750 | |
| 765 | Phosphorylation | SKRSPQKSPKKRQRV HHCCCCCCHHHHHHH | 36.38 | 19823750 | |
| 777 | Phosphorylation | QRVRQPASNSGSPIK HHHCCCCCCCCCCCC | 37.91 | 22369663 | |
| 779 | Phosphorylation | VRQPASNSGSPIKST HCCCCCCCCCCCCCC | 37.85 | 22369663 | |
| 781 | Phosphorylation | QPASNSGSPIKSTPR CCCCCCCCCCCCCCC | 24.23 | 22369663 | |
| 784 | Ubiquitination | SNSGSPIKSTPRRST CCCCCCCCCCCCCCC | 52.22 | 17644757 | |
| 785 | Phosphorylation | NSGSPIKSTPRRSTA CCCCCCCCCCCCCCC | 44.35 | 19684113 | |
| 786 | Phosphorylation | SGSPIKSTPRRSTAS CCCCCCCCCCCCCCC | 18.80 | 17563356 | |
| 790 | Phosphorylation | IKSTPRRSTASSVNA CCCCCCCCCCCCCCC | 29.60 | 22369663 | |
| 791 | Phosphorylation | KSTPRRSTASSVNAT CCCCCCCCCCCCCCC | 28.84 | 22369663 | |
| 793 | Phosphorylation | TPRRSTASSVNATPS CCCCCCCCCCCCCHH | 34.60 | 22369663 | |
| 794 | Phosphorylation | PRRSTASSVNATPSS CCCCCCCCCCCCHHH | 19.54 | 22369663 | |
| 798 | Phosphorylation | TASSVNATPSSARRI CCCCCCCCHHHHHHH | 20.64 | 22369663 | |
| 800 | Phosphorylation | SSVNATPSSARRILR CCCCCCHHHHHHHHC | 32.07 | 22369663 | |
| 801 | Phosphorylation | SVNATPSSARRILRF CCCCCHHHHHHHHCC | 27.31 | 22369663 | |
| 824 | Phosphorylation | EDDNDIMSPLPADEE CCCCCCCCCCCCCHH | 24.50 | 28152593 | |
| 845 | Phosphorylation | LQLGLRVSPRRREHL HHHCCCCCHHHHHHC | 13.27 | 22369663 | |
| 868 | Phosphorylation | GPLTEVGTPRLPNVS CCCCCCCCCCCCCCC | 15.48 | 17330950 | |
| 904 | Phosphorylation | TISTGRLSLISGIIA CCCHHHHHHHHHHHH | 23.46 | 22369663 | |
| 907 | Phosphorylation | TGRLSLISGIIARLM HHHHHHHHHHHHHHH | 29.27 | 22369663 | |
| 944 | Phosphorylation | LPEEEKFSAQEYLAG CCHHHCCCHHHHHHC | 39.86 | 28132839 | |
| 948 | Phosphorylation | EKFSAQEYLAGLKIM HCCCHHHHHHCCEEC | 6.97 | 28132839 | |
| 956 | Phosphorylation | LAGLKIMSDRNNLMV HHCCEECCCCCCEEE | 36.57 | 28132839 | |
| 967 | Ubiquitination | NLMVADDKVWRV--- CEEECCCEECCC--- | 44.22 | 24961812 |
| 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 MCM3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MCM3_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 MCM3_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-227; SER-777; SER-781;SER-794 AND SER-845, AND MASS SPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-777; SER-779; SER-781;THR-786; SER-790; THR-791; SER-794 AND SER-801, AND MASS SPECTROMETRY. | |
| "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-777 AND SER-781, ANDMASS SPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-845, AND MASSSPECTROMETRY. | |
| "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 SER-777; SER-781; SER-794AND SER-800, 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-868, AND MASSSPECTROMETRY. | |
