| UniProt ID | SNU66_YEAST | |
|---|---|---|
| UniProt AC | Q12420 | |
| Protein Name | 66 kDa U4/U6.U5 small nuclear ribonucleoprotein component | |
| Gene Name | SNU66 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 587 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Component of the U4/U6.U5 tri-snRNP particle, one of the building blocks of the spliceosome. Required for pre-mRNA splicing.. | |
| Protein Sequence | MNKTENLSIEETNEIREKLGMKPIPVFQEKNTDHKESLSIEETNELRASLGLKLIPPQQNFNSSPPNVHNTSKIDELREKITKFQKKANAPLRMAHLLEETNVNDDSSWLENMDAIPSSHESKRSSTLPRKGATKEDENIDLHNVQVSYNIEALSPKKDTILTLKESSIFDDTDSTEVLENVKAAEENADREKLRLRQMNKDRRQKKKILNVSSLDIEEEEEGEKHSITTTHLIIGAEQGVMKAPNTISAKPPTGKVKVNFDSANNMSDEDGGDFKPLKIKKRKIKDPRSTKARKSKITDKMEIVKLVDEDESLSWMEEEQPVTIINPRTSSNNELKGPEDLAREIEKARDEEKRRTESILKMREISNSIVVDEKVTFLNTLDTSLSERSATENKVKVHGEGEKNIGDVTNGHTKEGSGNNTLTEAVNNEPNYEGDAENAPNFFSGLASTLGYLRKKSVFTTGDVDLKPGKDVNNSESLRRDVRNKEHTGTGTYTKDKLHGLEQFTSSDSSNANTHSKRQDHYDPDIKLVYRDEKGNRLTTKEAYKKLSQKFHGTKSNKKKRAKMKSRIEARKNTPENGSLFEFDDN | |
| 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 |
|---|---|---|---|---|---|
| 8 | Phosphorylation | MNKTENLSIEETNEI CCCCCCCCHHHHHHH | 39.26 | 29688323 | |
| 12 | Phosphorylation | ENLSIEETNEIREKL CCCCHHHHHHHHHHH | 25.92 | 29688323 | |
| 63 | Phosphorylation | PPQQNFNSSPPNVHN CCCCCCCCCCCCCCC | 39.83 | 23749301 | |
| 64 | Phosphorylation | PQQNFNSSPPNVHNT CCCCCCCCCCCCCCC | 45.54 | 23749301 | |
| 125 | Phosphorylation | SSHESKRSSTLPRKG CCCHHHHCCCCCCCC | 31.26 | 17563356 | |
| 134 | Phosphorylation | TLPRKGATKEDENID CCCCCCCCCCCCCCC | 43.57 | 29136822 | |
| 148 | Phosphorylation | DLHNVQVSYNIEALS CCEEEEEEEEEEECC | 8.72 | 29136822 | |
| 149 | Phosphorylation | LHNVQVSYNIEALSP CEEEEEEEEEEECCC | 22.69 | 29136822 | |
| 155 | Phosphorylation | SYNIEALSPKKDTIL EEEEEECCCCCCEEE | 41.54 | 29136822 | |
| 167 | Phosphorylation | TILTLKESSIFDDTD EEEEEEHHHCCCCCC | 27.44 | 21551504 | |
| 168 | Phosphorylation | ILTLKESSIFDDTDS EEEEEHHHCCCCCCC | 28.50 | 27214570 | |
| 176 | Phosphorylation | IFDDTDSTEVLENVK CCCCCCCHHHHHHHH | 32.68 | 21551504 | |
| 254 | Phosphorylation | TISAKPPTGKVKVNF EEECCCCCCCEEECC | 59.15 | 28889911 | |
| 263 | Phosphorylation | KVKVNFDSANNMSDE CEEECCCCCCCCCCC | 28.85 | 22369663 | |
| 268 | Phosphorylation | FDSANNMSDEDGGDF CCCCCCCCCCCCCCC | 39.72 | 22369663 | |
| 313 | Phosphorylation | KLVDEDESLSWMEEE EECCCCCCCCCCCCC | 39.77 | 27017623 | |
| 315 | Phosphorylation | VDEDESLSWMEEEQP CCCCCCCCCCCCCCC | 33.39 | 21440633 | |
| 330 | Phosphorylation | VTIINPRTSSNNELK CEEECCCCCCCCCCC | 37.45 | 27017623 | |
| 331 | Phosphorylation | TIINPRTSSNNELKG EEECCCCCCCCCCCC | 32.14 | 21440633 | |
| 332 | Phosphorylation | IINPRTSSNNELKGP EECCCCCCCCCCCCH | 42.96 | 21082442 | |
| 367 | Phosphorylation | ILKMREISNSIVVDE HHHHHHHCCCEEECC | 21.55 | 21440633 | |
| 369 | Phosphorylation | KMREISNSIVVDEKV HHHHHCCCEEECCEE | 15.23 | 28889911 | |
| 404 | Acetylation | KVHGEGEKNIGDVTN EECCCCCCCCCCCCC | 65.80 | 22865919 | |
| 458 | Phosphorylation | LGYLRKKSVFTTGDV HHHHHHCCEEECCCC | 26.04 | 24961812 | |
| 489 | Phosphorylation | DVRNKEHTGTGTYTK HHHCCCCCCCCCCCH | 37.21 | 28889911 | |
| 491 | Phosphorylation | RNKEHTGTGTYTKDK HCCCCCCCCCCCHHH | 27.75 | 28889911 | |
| 494 | Phosphorylation | EHTGTGTYTKDKLHG CCCCCCCCCHHHCCC | 17.09 | 28889911 | |
| 551 | Acetylation | AYKKLSQKFHGTKSN HHHHHHHHHCCCCCC | 35.63 | 25381059 | |
| 567 | Phosphorylation | KKRAKMKSRIEARKN HHHHHHHHHHHHHHC | 34.68 | 24961812 | |
| 575 | Phosphorylation | RIEARKNTPENGSLF HHHHHHCCCCCCCCC | 34.71 | 22369663 | |
| 580 | Phosphorylation | KNTPENGSLFEFDDN HCCCCCCCCCCCCCC | 41.28 | 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 SNU66_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SNU66_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 SNU66_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-268; SER-332; SER-369AND THR-575, 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-125 AND SER-268, ANDMASS 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 SER-268, AND MASSSPECTROMETRY. | |
