| UniProt ID | LRS4_YEAST | |
|---|---|---|
| UniProt AC | Q04087 | |
| Protein Name | Monopolin complex subunit LRS4 | |
| Gene Name | LRS4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 347 | |
| Subcellular Localization | Nucleus, nucleolus. Chromosome, centromere. Transiently released from the nucleolus and localized to the centromere regions during late pachytene. This relocation is CDC5 dependent. | |
| Protein Description | Component of the monopolin complex which promotes monoorientation during meiosis I, required for chromosome segregation during meiosis. Involved in rDNA silencing.. | |
| Protein Sequence | MTTLLQLLSNYYKAKLDSERIYNEYVQSQYEFASLDKLNNNKGDPKKVVDETLFLQRQIAQLNKQLQLSFQENEKLLSVQKNQKALYQSKLSSKDAFIDDLKLKLKVEQISVDKHNKERTPSTGRDEQQRNSKAAHTSKPTIHLLSPIVNRDKPNNQTNDRGGNDPDSPTSQRRSRGLRSLLSSGKNTIFDSISKNLDDEINENAHIRNDTTSSKIAGKSPSRLSALQKSPELRKERNNMILKEHILRSKDDQNITSSRKLDNIELSSIGDSTAMTSRSSTVNANDILGNEENDGITKLKRVNKLTSSPVKRDCSTNKKRKLTKQRIATLPNSDEELSNNLNVDEFV | |
| 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 |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MTTLLQLLSN -----CHHHHHHHHH | 24.95 | 21440633 | |
| 11 | Phosphorylation | LLQLLSNYYKAKLDS HHHHHHHHHHHHCCH | 11.72 | 30377154 | |
| 12 | Phosphorylation | LQLLSNYYKAKLDSE HHHHHHHHHHHCCHH | 14.55 | 30377154 | |
| 89 | Phosphorylation | NQKALYQSKLSSKDA HHHHHHHHHHCCCCC | 23.23 | 28889911 | |
| 92 | Phosphorylation | ALYQSKLSSKDAFID HHHHHHHCCCCCCHH | 38.79 | 27214570 | |
| 93 | Phosphorylation | LYQSKLSSKDAFIDD HHHHHHCCCCCCHHH | 45.02 | 27214570 | |
| 120 | Phosphorylation | DKHNKERTPSTGRDE CCCCCCCCCCCCCHH | 23.76 | 28132839 | |
| 122 | Phosphorylation | HNKERTPSTGRDEQQ CCCCCCCCCCCHHHH | 42.77 | 28132839 | |
| 123 | Phosphorylation | NKERTPSTGRDEQQR CCCCCCCCCCHHHHH | 37.12 | 27717283 | |
| 132 | Phosphorylation | RDEQQRNSKAAHTSK CHHHHHHHHHCCCCC | 26.34 | 27717283 | |
| 138 | Phosphorylation | NSKAAHTSKPTIHLL HHHHCCCCCCCEECC | 27.11 | 28889911 | |
| 146 | Phosphorylation | KPTIHLLSPIVNRDK CCCEECCCCCCCCCC | 20.95 | 21082442 | |
| 168 | Phosphorylation | RGGNDPDSPTSQRRS CCCCCCCCHHHHHHH | 35.15 | 21082442 | |
| 170 | Phosphorylation | GNDPDSPTSQRRSRG CCCCCCHHHHHHHHH | 41.25 | 22890988 | |
| 171 | Phosphorylation | NDPDSPTSQRRSRGL CCCCCHHHHHHHHHH | 25.69 | 22890988 | |
| 184 | Phosphorylation | GLRSLLSSGKNTIFD HHHHHHHCCCCHHHH | 54.48 | 30377154 | |
| 194 | Phosphorylation | NTIFDSISKNLDDEI CHHHHHHHHCCCHHH | 21.31 | 30377154 | |
| 220 | Phosphorylation | SSKIAGKSPSRLSAL CHHHCCCCHHHHHHH | 27.47 | 28152593 | |
| 222 | Phosphorylation | KIAGKSPSRLSALQK HHCCCCHHHHHHHHH | 53.60 | 21440633 | |
| 225 | Phosphorylation | GKSPSRLSALQKSPE CCCHHHHHHHHHCHH | 26.31 | 29688323 | |
| 230 | Phosphorylation | RLSALQKSPELRKER HHHHHHHCHHHHHHH | 15.62 | 21082442 | |
| 279 | Phosphorylation | STAMTSRSSTVNAND CCCCCCCCCCCCHHH | 30.08 | 22369663 | |
| 280 | Phosphorylation | TAMTSRSSTVNANDI CCCCCCCCCCCHHHH | 34.95 | 22369663 | |
| 281 | Phosphorylation | AMTSRSSTVNANDIL CCCCCCCCCCHHHHC | 21.01 | 22369663 | |
| 304 | Acetylation | TKLKRVNKLTSSPVK HHHHHHHHHCCCCCC | 50.73 | 25381059 | |
| 307 | Phosphorylation | KRVNKLTSSPVKRDC HHHHHHCCCCCCCCC | 42.98 | 19684113 | |
| 308 | Phosphorylation | RVNKLTSSPVKRDCS HHHHHCCCCCCCCCC | 28.60 | 19684113 | |
| 329 | Phosphorylation | LTKQRIATLPNSDEE CCHHHHCCCCCCHHH | 40.14 | 19823750 | |
| 333 | Phosphorylation | RIATLPNSDEELSNN HHCCCCCCHHHHHHC | 44.45 | 20377248 | |
| 338 | Phosphorylation | PNSDEELSNNLNVDE CCCHHHHHHCCCHHH | 27.27 | 19823750 |
| 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 LRS4_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LRS4_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 LRS4_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-146; SER-168 ANDSER-230, 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-168 AND SER-230, ANDMASS SPECTROMETRY. | |
