| UniProt ID | RQC2_SCHPO | |
|---|---|---|
| UniProt AC | Q9USN8 | |
| Protein Name | Ribosome quality control complex subunit 2 {ECO:0000250|UniProtKB:Q12532} | |
| Gene Name | mtr1 {ECO:0000303|PubMed:24928430} | |
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). | |
| Sequence Length | 1021 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. Mtr1/rqc2 is responsible for selective recognition of stalled 60S subunits by recognizing an exposed, nascent chain-conjugated tRNA moiety. Mtr1/rqc2 is important for the stable association of rkr1/ltn1 to the complex. Mtr1/rqc2 recruits alanine- and threonine-charged tRNA to the A site and directs the elongation of stalled nascent chains independently of mRNA or 40S subunits, leading to non-templated C-terminal Ala and Thr extensions (CAT tails). CAT tails induce a heat shock response.. | |
| Protein Sequence | MKQRFSALDIAAIAAELREQVVGCRLNNFYDLNARTFLLKFGKQDAKYSIVIESGFRAHLTKFDRENAPLSGFVTKLRKHIKSRRLTGVSQLGTDRVLVFTFGGGANDQDPDWTYYLVCEFFAAGNVLLLDGHYKILSLLRVVTFDKDQVYAVGQKYNLDKNNLVNDNKSQSTIPHMTAERLNILLDEISTAYASPTSINEPLPDQQLSSSTKPIKVPKPVSLRKALTIRLGEYGNALIEHCLRRSKLDPLFPACQLCADETKKNDLLAAFQEADSILAAVNKPPVKGYIFSLEQALTNAADPQHPEECTTLYEDFHPFQPLQLVQANRKCMEFPTYNECVDEFFSSIEAQKLKKRAHDRLATAERRLESAKEDQARKLQSLQDAQATCALRAQAIEMNPELVEAIISYINSLLNQGMDWLDIEKLIQSQKRRSPVAAAIQIPLKLIKNAVTVFLPNPESVDNSDESSETSDDDLDDSDDDNKVKEGKVSSKFIAVELDLSLGAFANARKQYELRREALIKETKTAEAASKALKSTQRKIEQDLKRSTTADTQRILLGRKTFFFEKFHWFISSEGYLVLGGRDAQQNELLFQKYCNTGDIFVCADLPKSSIIIVKNKNPHDPIPPNTLQQAGSLALASSKAWDSKTVISAWWVRIDEVSKLAPTGEILPTGSFAIRAKKNYLPPTVLIMGYGILWQLDEKSSERRKARRLEMEVVETQGKVSELKMEGTSVTSEDNIQDVVSEVSYNEDTNNQSTPDTTGSDIHIVSEKRGKKGSKVITAKKVSAKERREARRARRQTALEESLKAPISIEDATDPQTILAILKQKKAKKKHAAREMEISSQIPSNDSSNVQTPTAESEIEEDGVSEPISAEVIEDQSRNSEAENEKGLSTEQRDEKKHAKVESFQRQEMPRSLFEEIFFAIDSLTPNPQQQDTVINAVPTFAPYNAMTKFNQKVKVMPGTGKVGKAARESIAYFMKKLPKSSKEAAYLENLKDGEIVAPISVSRLKMVFGSSGNTKKSKK | |
| 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 |
|---|---|---|---|---|---|
| 470 | Phosphorylation | NSDESSETSDDDLDD CCCCCCCCCCCCCCC | 25720772 | ||
| 471 | Phosphorylation | SDESSETSDDDLDDS CCCCCCCCCCCCCCC | 25720772 | ||
| 478 | Phosphorylation | SDDDLDDSDDDNKVK CCCCCCCCCCCCCHH | 28889911 | ||
| 561 | Phosphorylation | RILLGRKTFFFEKFH HHHHCCCEEEEEEEE | 25720772 | ||
| 848 | Phosphorylation | SQIPSNDSSNVQTPT HCCCCCCCCCCCCCC | 27738172 | ||
| 855 | Phosphorylation | SSNVQTPTAESEIEE CCCCCCCCCCCHHCC | 27738172 |
| 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 RQC2_SCHPO !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RQC2_SCHPO !! | ||||||
* 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 RQC2_SCHPO !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of RQC2_SCHPO !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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