| UniProt ID | MCM4_YEAST | |
|---|---|---|
| UniProt AC | P30665 | |
| Protein Name | DNA replication licensing factor MCM4 | |
| Gene Name | MCM4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 933 | |
| 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 S phase execution.. | |
| Protein Sequence | MSQQSSSPTKEDNNSSSPVVPNPDSVPPQLSSPALFYSSSSSQGDIYGRNNSQNLSQGEGNIRAAIGSSPLNFPSSSQRQNSDVFQSQGRQGRIRSSASASGRSRYHSDLRSDRALPTSSSSLGRNGQNRVHMRRNDIHTSDLSSPRRIVDFDTRSGVNTLDTSSSSAPPSEASEPLRIIWGTNVSIQECTTNFRNFLMSFKYKFRKILDEREEFINNTTDEELYYIKQLNEMRELGTSNLNLDARNLLAYKQTEDLYHQLLNYPQEVISIMDQTIKDCMVSLIVDNNLDYDLDEIETKFYKVRPYNVGSCKGMRELNPNDIDKLINLKGLVLRSTPVIPDMKVAFFKCNVCDHTMAVEIDRGVIQEPARCERIDCNEPNSMSLIHNRCSFADKQVIKLQETPDFVPDGQTPHSISLCVYDELVDSCRAGDRIEVTGTFRSIPIRANSRQRVLKSLYKTYVDVVHVKKVSDKRLDVDTSTIEQELMQNKVDHNEVEEVRQITDQDLAKIREVAAREDLYSLLARSIAPSIYELEDVKKGILLQLFGGTNKTFTKGGRYRGDINILLCGDPSTSKSQILQYVHKITPRGVYTSGKGSSAVGLTAYITRDVDTKQLVLESGALVLSDGGVCCIDEFDKMSDSTRSVLHEVMEQQTISIAKAGIITTLNARSSILASANPIGSRYNPNLPVTENIDLPPPLLSRFDLVYLVLDKVDEKNDRELAKHLTNLYLEDKPEHISQDDVLPVEFLTMYISYAKEHIHPIITEAAKTELVRAYVGMRKMGDDSRSDEKRITATTRQLESMIRLAEAHAKMKLKNVVELEDVQEAVRLIRSAIKDYATDPKTGKIDMNLVQTGKSVIQRKLQEDLSREIMNVLKDQASDSMSFNELIKQINEHSQDRVESSDIQEALSRLQQEDKVIVLGEGVRRSVRLNNRV | |
| 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 | ------MSQQSSSPT ------CCCCCCCCC | 36.61 | 28889911 | |
| 5 | Phosphorylation | ---MSQQSSSPTKED ---CCCCCCCCCCCC | 25.75 | 27717283 | |
| 6 | Phosphorylation | --MSQQSSSPTKEDN --CCCCCCCCCCCCC | 35.68 | 27717283 | |
| 7 | Phosphorylation | -MSQQSSSPTKEDNN -CCCCCCCCCCCCCC | 41.66 | 28889911 | |
| 9 | Phosphorylation | SQQSSSPTKEDNNSS CCCCCCCCCCCCCCC | 49.35 | 27717283 | |
| 17 | Phosphorylation | KEDNNSSSPVVPNPD CCCCCCCCCCCCCCC | 22.87 | 21070963 | |
| 31 | Phosphorylation | DSVPPQLSSPALFYS CCCCCCCCCCEEEEE | 29.09 | 21070963 | |
| 42 | Phosphorylation | LFYSSSSSQGDIYGR EEEECCCCCCCCCCC | 39.88 | 21070963 | |
| 52 | Phosphorylation | DIYGRNNSQNLSQGE CCCCCCCCCCCCCCC | 24.80 | 22369663 | |
| 56 | Phosphorylation | RNNSQNLSQGEGNIR CCCCCCCCCCCCCHH | 43.63 | 22369663 | |
| 68 | Phosphorylation | NIRAAIGSSPLNFPS CHHHHHCCCCCCCCC | 23.75 | 22369663 | |
| 69 | Phosphorylation | IRAAIGSSPLNFPSS HHHHHCCCCCCCCCC | 28.35 | 22369663 | |
| 75 | Phosphorylation | SSPLNFPSSSQRQNS CCCCCCCCCHHHCCC | 38.18 | 22369663 | |
| 76 | Phosphorylation | SPLNFPSSSQRQNSD CCCCCCCCHHHCCCH | 30.63 | 22369663 | |
| 77 | Phosphorylation | PLNFPSSSQRQNSDV CCCCCCCHHHCCCHH | 33.45 | 22369663 | |
| 82 | Phosphorylation | SSSQRQNSDVFQSQG CCHHHCCCHHHHCCC | 27.15 | 22369663 | |
| 87 | Phosphorylation | QNSDVFQSQGRQGRI CCCHHHHCCCCCCCC | 24.12 | 23749301 | |
| 96 | Phosphorylation | GRQGRIRSSASASGR CCCCCCCCCCCCCCC | 28.08 | 28889911 | |
| 97 | Phosphorylation | RQGRIRSSASASGRS CCCCCCCCCCCCCCC | 19.18 | 30377154 | |
| 99 | Phosphorylation | GRIRSSASASGRSRY CCCCCCCCCCCCCCC | 25.56 | 27214570 | |
| 101 | Phosphorylation | IRSSASASGRSRYHS CCCCCCCCCCCCCCC | 32.04 | 28889911 | |
| 104 | Phosphorylation | SASASGRSRYHSDLR CCCCCCCCCCCCCCC | 40.49 | 28889911 | |
| 108 | Phosphorylation | SGRSRYHSDLRSDRA CCCCCCCCCCCCCCC | 29.43 | 21070963 | |
| 112 | Phosphorylation | RYHSDLRSDRALPTS CCCCCCCCCCCCCCC | 38.45 | 21070963 | |
| 118 | Phosphorylation | RSDRALPTSSSSLGR CCCCCCCCCCCCCCC | 41.93 | 22369663 | |
| 119 | Phosphorylation | SDRALPTSSSSLGRN CCCCCCCCCCCCCCC | 26.70 | 22369663 | |
| 120 | Phosphorylation | DRALPTSSSSLGRNG CCCCCCCCCCCCCCC | 26.82 | 23749301 | |
| 121 | Phosphorylation | RALPTSSSSLGRNGQ CCCCCCCCCCCCCCC | 29.38 | 22369663 | |
| 122 | Phosphorylation | ALPTSSSSLGRNGQN CCCCCCCCCCCCCCC | 36.47 | 22369663 | |
| 140 | Phosphorylation | MRRNDIHTSDLSSPR ECCCCCCCCCCCCCC | 25.03 | 22369663 | |
| 141 | Phosphorylation | RRNDIHTSDLSSPRR CCCCCCCCCCCCCCE | 23.53 | 22369663 | |
| 144 | Phosphorylation | DIHTSDLSSPRRIVD CCCCCCCCCCCEEEE | 43.20 | 22369663 | |
| 145 | Phosphorylation | IHTSDLSSPRRIVDF CCCCCCCCCCEEEEC | 29.71 | 22369663 | |
| 156 | Phosphorylation | IVDFDTRSGVNTLDT EEECCCCCCCCCCCC | 49.54 | 19779198 | |
| 163 | Phosphorylation | SGVNTLDTSSSSAPP CCCCCCCCCCCCCCC | 33.35 | 28889911 | |
| 165 | Phosphorylation | VNTLDTSSSSAPPSE CCCCCCCCCCCCCHH | 30.33 | 23749301 | |
| 166 | Phosphorylation | NTLDTSSSSAPPSEA CCCCCCCCCCCCHHC | 30.22 | 23749301 | |
| 167 | Phosphorylation | TLDTSSSSAPPSEAS CCCCCCCCCCCHHCC | 46.90 | 23749301 | |
| 171 | Phosphorylation | SSSSAPPSEASEPLR CCCCCCCHHCCCCEE | 44.74 | 23749301 | |
| 174 | Phosphorylation | SAPPSEASEPLRIIW CCCCHHCCCCEEEEE | 35.38 | 23749301 | |
| 239 | Phosphorylation | EMRELGTSNLNLDAR HHHHHCCCCCCCCHH | 37.21 | 27214570 | |
| 264 | Phosphorylation | LYHQLLNYPQEVISI HHHHHHCCCHHHHHH | 13.28 | 28132839 | |
| 324 | Acetylation | LNPNDIDKLINLKGL CCHHHHHHHHCCCCH | 52.15 | 24489116 | |
| 441 | Phosphorylation | EVTGTFRSIPIRANS EEEEEEECCCCCCHH | 28.64 | 28889911 | |
| 448 | Phosphorylation | SIPIRANSRQRVLKS CCCCCCHHHHHHHHH | 28.89 | 28889911 | |
| 529 | Phosphorylation | LARSIAPSIYELEDV HHHHHCCCCCCHHHH | 28.87 | 29136822 | |
| 531 | Phosphorylation | RSIAPSIYELEDVKK HHHCCCCCCHHHHHC | 20.85 | 29136822 | |
| 575 | Phosphorylation | GDPSTSKSQILQYVH CCCCCCHHHHHHHHH | 23.40 | 28889911 | |
| 583 | Acetylation | QILQYVHKITPRGVY HHHHHHHHCCCCCCE | 37.93 | 24489116 | |
| 596 | Phosphorylation | VYTSGKGSSAVGLTA CEECCCCCCCCCEEE | 20.71 | 26447709 | |
| 597 | Phosphorylation | YTSGKGSSAVGLTAY EECCCCCCCCCEEEE | 35.33 | 26447709 | |
| 602 | Phosphorylation | GSSAVGLTAYITRDV CCCCCCEEEEEECCC | 16.10 | 26447709 | |
| 604 | Phosphorylation | SAVGLTAYITRDVDT CCCCEEEEEECCCCC | 9.51 | 26447709 | |
| 606 | Phosphorylation | VGLTAYITRDVDTKQ CCEEEEEECCCCCCC | 14.24 | 26447709 |
| 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 MCM4_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MCM4_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 MCM4_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-52; SER-56; SER-68 ANDSER-69, AND MASS 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-69, AND MASSSPECTROMETRY. | |
