| UniProt ID | MPP6_YEAST | |
|---|---|---|
| UniProt AC | P53725 | |
| Protein Name | M-phase phosphoprotein 6 homolog | |
| Gene Name | MPP6 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 186 | |
| Subcellular Localization | Nucleus . Colocalizes with the nuclear exosome and ribosomes. | |
| Protein Description | Involved in surveillance of pre-rRNAs and pre-mRNAs, and the degradation of cryptic non-coding RNAs (ncRNA) derived from intergenic regions and the ribosomal DNA spacer heterochromatin. Binds RNA.. | |
| Protein Sequence | MSANNGVTGKLSSRVMNMKFMKFGKTDDEESSNSNTPSNINSDVEPIEQKGKLFGLDDSAWDLNSYKDDLKKISGKEKKKVKRVVYKKRPNLIISNVGYSELRKPEGVISGRKTFGDNSDDSGSRKRKFDEGEQNEDEKRDAKDKEFTGSQDDGEDEYDLDKLFKDSIKKKKTNHNGKNKNRNSKK | |
| 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 | Acetylation | ------MSANNGVTG ------CCCCCCCCC | 39.44 | 22814378 | |
| 8 | Phosphorylation | MSANNGVTGKLSSRV CCCCCCCCCCHHHHH | 29.96 | 30377154 | |
| 10 | Acetylation | ANNGVTGKLSSRVMN CCCCCCCCHHHHHHH | 35.51 | 24489116 | |
| 12 | Phosphorylation | NGVTGKLSSRVMNMK CCCCCCHHHHHHHHE | 21.42 | 30377154 | |
| 13 | Phosphorylation | GVTGKLSSRVMNMKF CCCCCHHHHHHHHEE | 39.05 | 30377154 | |
| 26 | Phosphorylation | KFMKFGKTDDEESSN EEEECCCCCCCCCCC | 49.41 | 22369663 | |
| 31 | Phosphorylation | GKTDDEESSNSNTPS CCCCCCCCCCCCCCC | 32.54 | 22369663 | |
| 32 | Phosphorylation | KTDDEESSNSNTPSN CCCCCCCCCCCCCCC | 47.78 | 22369663 | |
| 34 | Phosphorylation | DDEESSNSNTPSNIN CCCCCCCCCCCCCCC | 43.99 | 22369663 | |
| 36 | Phosphorylation | EESSNSNTPSNINSD CCCCCCCCCCCCCCC | 28.10 | 22369663 | |
| 38 | Phosphorylation | SSNSNTPSNINSDVE CCCCCCCCCCCCCCC | 48.59 | 22369663 | |
| 42 | Phosphorylation | NTPSNINSDVEPIEQ CCCCCCCCCCCCHHH | 38.96 | 22369663 | |
| 59 | Phosphorylation | KLFGLDDSAWDLNSY CCCCCCCCCCCHHHH | 30.81 | 21440633 | |
| 119 | Phosphorylation | RKTFGDNSDDSGSRK CCCCCCCCCCCCCCC | 47.75 | 23749301 | |
| 122 | Phosphorylation | FGDNSDDSGSRKRKF CCCCCCCCCCCCCCC | 43.59 | 28889911 | |
| 124 | Phosphorylation | DNSDDSGSRKRKFDE CCCCCCCCCCCCCCC | 38.28 | 27717283 | |
| 128 | Acetylation | DSGSRKRKFDEGEQN CCCCCCCCCCCCCCC | 61.27 | 22865919 | |
| 148 | Phosphorylation | DAKDKEFTGSQDDGE HHHHHCCCCCCCCCC | 36.69 | 22369663 | |
| 150 | Phosphorylation | KDKEFTGSQDDGEDE HHHCCCCCCCCCCCC | 27.64 | 25521595 | |
| 158 | Phosphorylation | QDDGEDEYDLDKLFK CCCCCCCCCHHHHHH | 33.84 | 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 MPP6_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MPP6_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 MPP6_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-42; THR-148 AND SER-150,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-42 AND SER-150, AND MASSSPECTROMETRY. | |