| UniProt ID | RRP6_YEAST | |
|---|---|---|
| UniProt AC | Q12149 | |
| Protein Name | Exosome complex exonuclease RRP6 | |
| Gene Name | RRP6 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 733 | |
| Subcellular Localization | Nucleus, nucleolus . | |
| Protein Description | Nuclear-specific catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. RRP6 has 3'-5' exonuclease activity which is not modulated upon association with Exo-9 suggesting that the complex inner RNA-binding path is not used to access its active site.. | |
| Protein Sequence | MTSENPDVLLSRVINVVRAASSLASQDVDFYKNLDRGFSKDLKSKADKLADMANEIILSIDEHHESFELKEEDISDLWNNFGNIMDNLLEMSDHSLDKLNCAINSKSRGSDLQYLGEFSGKNFSPTKRVEKPQLKFKSPIDNSESHPFIPLLKEKPNALKPLSESLRLVDDDENNPSHYPHPYEYEIDHQEYSPEILQIREEIPSKSWDDSVPIWVDTSTELESMLEDLKNTKEIAVDLEHHDYRSYYGIVCLMQISTRERDYLVDTLKLRENLHILNEVFTNPSIVKVFHGAFMDIIWLQRDLGLYVVGLFDTYHASKAIGLPRHSLAYLLENFANFKTSKKYQLADWRIRPLSKPMTAYARADTHFLLNIYDQLRNKLIESNKLAGVLYESRNVAKRRFEYSKYRPLTPSSEVYSPIEKESPWKILMYQYNIPPEREVLVRELYQWRDLIARRDDESPRFVMPNQLLAALVAYTPTDVIGVVSLTNGVTEHVRQNAKLLANLIRDALRNIKNTNEEATPIPSSETKADGILLETISVPQIRDVMERFSVLCNSNISKSRAKPVTNSSILLGKILPREEHDIAYSKDGLPNKVKTEDIRIRAQNFKSALANLEDIIFEIEKPLVVPVKLEEIKTVDPASAPNHSPEIDNLDDLVVLKKKNIQKKQPAKEKGVTEKDAVDYSKIPNILSNKPGQNNRQQKKRRFDPSSSDSNGPRAAKKRRPAAKGKNLSFKR | |
| 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 |
|---|---|---|---|---|---|
| 22 | Phosphorylation | NVVRAASSLASQDVD HHHHHHHHHHHCCCH | 24.19 | 30377154 | |
| 107 | Phosphorylation | NCAINSKSRGSDLQY CCHHCCCCCCCCCCC | 41.51 | 22369663 | |
| 110 | Phosphorylation | INSKSRGSDLQYLGE HCCCCCCCCCCCHHH | 33.75 | 22369663 | |
| 119 | Phosphorylation | LQYLGEFSGKNFSPT CCCHHHCCCCCCCCC | 44.55 | 30377154 | |
| 121 | Acetylation | YLGEFSGKNFSPTKR CHHHCCCCCCCCCCC | 54.33 | 24489116 | |
| 124 | Phosphorylation | EFSGKNFSPTKRVEK HCCCCCCCCCCCCCC | 40.84 | 25704821 | |
| 138 | Phosphorylation | KPQLKFKSPIDNSES CCCCCCCCCCCCCCC | 30.16 | 17330950 | |
| 269 | Acetylation | DYLVDTLKLRENLHI HHHHHHHHHHCHHHH | 47.82 | 24489116 | |
| 406 | Phosphorylation | RRFEYSKYRPLTPSS HCCCCCCCCCCCCCC | 16.12 | 28889911 | |
| 410 | Phosphorylation | YSKYRPLTPSSEVYS CCCCCCCCCCCCCCC | 24.65 | 27214570 | |
| 412 | Phosphorylation | KYRPLTPSSEVYSPI CCCCCCCCCCCCCCC | 33.62 | 27214570 | |
| 413 | Phosphorylation | YRPLTPSSEVYSPIE CCCCCCCCCCCCCCC | 32.08 | 24961812 | |
| 416 | Phosphorylation | LTPSSEVYSPIEKES CCCCCCCCCCCCCCC | 12.51 | 21440633 | |
| 417 | Phosphorylation | TPSSEVYSPIEKESP CCCCCCCCCCCCCCC | 25.28 | 21440633 | |
| 421 | Acetylation | EVYSPIEKESPWKIL CCCCCCCCCCCCEEE | 65.30 | 24489116 | |
| 515 | Phosphorylation | ALRNIKNTNEEATPI HHHHHHCCCCCCCCC | 38.72 | 29136822 | |
| 520 | Phosphorylation | KNTNEEATPIPSSET HCCCCCCCCCCCCCC | 25.65 | 29136822 | |
| 524 | Phosphorylation | EEATPIPSSETKADG CCCCCCCCCCCCCCC | 41.34 | 30377154 | |
| 525 | Phosphorylation | EATPIPSSETKADGI CCCCCCCCCCCCCCE | 43.88 | 30377154 | |
| 574 | Acetylation | NSSILLGKILPREEH CCHHHHCCCCCHHHC | 40.83 | 24489116 | |
| 587 | Acetylation | EHDIAYSKDGLPNKV HCCCCCCCCCCCCCC | 43.04 | 24489116 | |
| 635 | Phosphorylation | VKLEEIKTVDPASAP EEHHHCEECCCCCCC | 35.48 | 22369663 | |
| 640 | Phosphorylation | IKTVDPASAPNHSPE CEECCCCCCCCCCCC | 50.04 | 22369663 | |
| 645 | Phosphorylation | PASAPNHSPEIDNLD CCCCCCCCCCCCCHH | 30.76 | 22369663 | |
| 676 | Acetylation | KEKGVTEKDAVDYSK HHCCCCHHHHCCHHH | 41.44 | 22865919 | |
| 683 | Acetylation | KDAVDYSKIPNILSN HHHCCHHHCCHHHCC | 56.82 | 22865919 | |
| 708 | Phosphorylation | KRRFDPSSSDSNGPR HHCCCCCCCCCCCCH | 43.48 | 30377154 | |
| 709 | Phosphorylation | RRFDPSSSDSNGPRA HCCCCCCCCCCCCHH | 49.77 | 23749301 | |
| 711 | Phosphorylation | FDPSSSDSNGPRAAK CCCCCCCCCCCHHHH | 45.71 | 28889911 | |
| 727 | Acetylation | RRPAAKGKNLSFKR- CCCCCCCCCCCCCC- | 54.75 | 25381059 | |
| 732 | Acetylation | KGKNLSFKR------ CCCCCCCCC------ | 54.55 | 25381059 |
| 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 RRP6_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RRP6_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 RRP6_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-110; TYR-406; THR-410;SER-412; THR-520; SER-640 AND SER-645, 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-110 AND SER-645, 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-138 AND SER-645, ANDMASS SPECTROMETRY. | |
