| UniProt ID | MCM10_YEAST | |
|---|---|---|
| UniProt AC | P32354 | |
| Protein Name | Minichromosome maintenance protein 10 | |
| Gene Name | MCM10 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 571 | |
| Subcellular Localization | Nucleus . Colocalizes with ORC1 on chromatin independent from cell cycle. According to PubMed:15494305 is recruited to replication origins in a cell cycle regulated manner. | |
| Protein Description | Required for DNA synthesis. Required for entry into or completion of S phase. Involved in DNA replication and seems to participate in the activation of the pre-replication complex (pre-RC) and in transcription elongation. May play a role as a key coordinator in assembling the replication fork. Proposed to function at replication origins following the binding of the MCM2-7 complex prior to the recruitment of CDC45. Probably is required to stimulate phosphorylation of the MCM2-7 complex by the CDC7-DBF4 kinase complex. May recruit the DNA polymerase alpha:primase complex to replication origins and is required to maintain it on chromatin independently of CDC45. May also play a role in transcriptional silencing.. | |
| Protein Sequence | MNDPREILAVDPYNNITSDEEDEQAIARELEFMERKRQALVERLKRKQEFKKPQDPNFEAIEVPQSPTKNRVKVGSHNATQQGTKFEGSNINEVRLSQLQQQPKPPASTTTYFMEKFQNAKKNEDKQIAKFESMMNARVHTFSTDEKKYVPIITNELESFSNLWVKKRYIPEDDLKRALHEIKILRLGKLFAKIRPPKFQEPEYANWATVGLISHKSDIKFTSSEKPVKFFMFTITDFQHTLDVYIFGKKGVERYYNLRLGDVIAILNPEVLPWRPSGRGNFIKSFNLRISHDFKCILEIGSSRDLGWCPIVNKKTHKKCGSPINISLHKCCDYHREVQFRGTSAKRIELNGGYALGAPTKVDSQPSLYKAKGENGFNIIKGTRKRLSEEEERLKKSSHNFTNSNSAKAFFDEKFQNPDMLANLDNKRRKIIETKKSTALSRELGKIMRRRESSGLEDKSVGERQKMKRTTESALQTGLIQRLGFDPTHGKISQVLKSSVSGSEPKNNLLGKKKTVINDLLHYKKEKVILAPSKNEWFKKRSHREEVWQKHFGSKETKETSDGSASDLEII | |
| 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 |
|---|---|---|---|---|---|
| 13 | Phosphorylation | EILAVDPYNNITSDE HCEEECCCCCCCCCH | 19.17 | 22369663 | |
| 17 | Phosphorylation | VDPYNNITSDEEDEQ ECCCCCCCCCHHHHH | 32.05 | 22369663 | |
| 18 | Phosphorylation | DPYNNITSDEEDEQA CCCCCCCCCHHHHHH | 38.95 | 22369663 | |
| 66 | Phosphorylation | EAIEVPQSPTKNRVK CCEECCCCCCCCCEE | 28.59 | 25521595 | |
| 68 | Phosphorylation | IEVPQSPTKNRVKVG EECCCCCCCCCEEEC | 46.31 | 22369663 | |
| 108 | Phosphorylation | QQPKPPASTTTYFME CCCCCCCCCHHHHHH | 31.87 | 19823750 | |
| 109 | Phosphorylation | QPKPPASTTTYFMEK CCCCCCCCHHHHHHH | 25.84 | 19823750 | |
| 110 | Phosphorylation | PKPPASTTTYFMEKF CCCCCCCHHHHHHHH | 19.60 | 19823750 | |
| 111 | Phosphorylation | KPPASTTTYFMEKFQ CCCCCCHHHHHHHHH | 18.17 | 19823750 | |
| 112 | Phosphorylation | PPASTTTYFMEKFQN CCCCCHHHHHHHHHH | 9.99 | 19823750 | |
| 133 | Phosphorylation | KQIAKFESMMNARVH HHHHHHHHHHHCEEE | 26.85 | 19779198 | |
| 143 | Phosphorylation | NARVHTFSTDEKKYV HCEEEECCCCCCCCC | 35.78 | 19779198 | |
| 364 | Phosphorylation | GAPTKVDSQPSLYKA CCCCEECCCCCHHCC | 47.15 | 30377154 | |
| 388 | Phosphorylation | KGTRKRLSEEEERLK CCCHHCCCHHHHHHH | 47.17 | 28889911 | |
| 408 | Acetylation | FTNSNSAKAFFDEKF CCCCHHHHHHHCHHH | 45.61 | 25381059 | |
| 437 | Phosphorylation | KIIETKKSTALSREL HHHHHHHHHHHHHHH | 22.07 | 27017623 | |
| 438 | Phosphorylation | IIETKKSTALSRELG HHHHHHHHHHHHHHH | 40.26 | 28889911 | |
| 453 | Phosphorylation | KIMRRRESSGLEDKS HHHHHHHHCCCCCCC | 28.09 | 17287358 | |
| 454 | Phosphorylation | IMRRRESSGLEDKSV HHHHHHHCCCCCCCH | 42.52 | 16675460 | |
| 460 | Phosphorylation | SSGLEDKSVGERQKM HCCCCCCCHHHHHHH | 47.91 | 28889911 | |
| 491 | Acetylation | GFDPTHGKISQVLKS CCCCCCCHHHHHHHH | 31.42 | 22865919 | |
| 498 | Phosphorylation | KISQVLKSSVSGSEP HHHHHHHHHCCCCCC | 31.63 | 30377154 | |
| 555 | Acetylation | WQKHFGSKETKETSD HHHHHCCCCCCCCCC | 70.54 | 25381059 | |
| 560 | Phosphorylation | GSKETKETSDGSASD CCCCCCCCCCCCHHH | 33.40 | 21551504 | |
| 561 | Phosphorylation | SKETKETSDGSASDL CCCCCCCCCCCHHHC | 40.86 | 19684113 | |
| 564 | Phosphorylation | TKETSDGSASDLEII CCCCCCCCHHHCEEC | 29.59 | 19684113 | |
| 566 | Phosphorylation | ETSDGSASDLEII-- CCCCCCHHHCEEC-- | 44.41 | 19684113 |
| 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 MCM10_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MCM10_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 MCM10_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 THR-17 AND SER-18, 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-453 AND SER-454, ANDMASS SPECTROMETRY. | |
