UniProt ID | QCR2_YEAST | |
---|---|---|
UniProt AC | P07257 | |
Protein Name | Cytochrome b-c1 complex subunit 2, mitochondrial | |
Gene Name | QCR2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 368 | |
Subcellular Localization | Mitochondrion inner membrane . Mitochondrion intermembrane space . | |
Protein Description | Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c. QCR2 is required for the assembly of the complex.. | |
Protein Sequence | MLSAARLQFAQGSVRRLTVSARDAPTKISTLAVKVHGGSRYATKDGVAHLLNRFNFQNTNTRSALKLVRESELLGGTFKSTLDREYITLKATFLKDDLPYYVNALADVLYKTAFKPHELTESVLPAARYDYAVAEQCPVKSAEDQLYAITFRKGLGNPLLYDGVERVSLQDIKDFADKVYTKENLEVSGENVVEADLKRFVDESLLSTLPAGKSLVSKSEPKFFLGEENRVRFIGDSVAAIGIPVNKASLAQYEVLANYLTSALSELSGLISSAKLDKFTDGGLFTLFVRDQDSAVVSSNIKKIVADLKKGKDLSPAINYTKLKNAVQNESVSSPIELNFDAVKDFKLGKFNYVAVGDVSNLPYLDEL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
27 | 2-Hydroxyisobutyrylation | SARDAPTKISTLAVK ECCCCCCEEEEEEEE | 33.33 | - | |
27 | Acetylation | SARDAPTKISTLAVK ECCCCCCEEEEEEEE | 33.33 | 24489116 | |
44 | Acetylation | GGSRYATKDGVAHLL CCCCEECHHHHHHHH | 44.29 | 24489116 | |
79 | Acetylation | ELLGGTFKSTLDREY HHHCCCHHHHCCCCE | 42.23 | 24489116 | |
110 | Phosphorylation | NALADVLYKTAFKPH HHHHHHHHHHCCCHH | 13.22 | 27017623 | |
115 | Acetylation | VLYKTAFKPHELTES HHHHHCCCHHHCCCC | 42.89 | 24489116 | |
141 | Phosphorylation | AEQCPVKSAEDQLYA HHCCCCCCHHHCEEE | 36.80 | 28889911 | |
161 | Phosphorylation | GLGNPLLYDGVERVS CCCCCCCCCCCEECC | 20.52 | 22369663 | |
168 | Phosphorylation | YDGVERVSLQDIKDF CCCCEECCHHHHHHH | 26.91 | 22369663 | |
173 | Acetylation | RVSLQDIKDFADKVY ECCHHHHHHHHHHCC | 55.90 | 24489116 | |
178 | 2-Hydroxyisobutyrylation | DIKDFADKVYTKENL HHHHHHHHCCCCCCC | 33.44 | - | |
178 | Acetylation | DIKDFADKVYTKENL HHHHHHHHCCCCCCC | 33.44 | 24489116 | |
180 | Phosphorylation | KDFADKVYTKENLEV HHHHHHCCCCCCCEE | 20.17 | 27017623 | |
222 | Acetylation | LVSKSEPKFFLGEEN CCCCCCCCEECCCCC | 44.70 | 24489116 | |
280 | Phosphorylation | SAKLDKFTDGGLFTL HHCCCCCCCCCEEEE | 39.20 | 21126336 | |
302 | Succinylation | AVVSSNIKKIVADLK CEEECCHHHHHHHHH | 40.47 | 23954790 | |
302 | 2-Hydroxyisobutyrylation | AVVSSNIKKIVADLK CEEECCHHHHHHHHH | 40.47 | - | |
309 | Succinylation | KKIVADLKKGKDLSP HHHHHHHHCCCCCCC | 61.09 | 23954790 | |
315 | Phosphorylation | LKKGKDLSPAINYTK HHCCCCCCCCCCHHH | 23.55 | 27214570 | |
321 | Phosphorylation | LSPAINYTKLKNAVQ CCCCCCHHHHHHHHC | 25.97 | 28889911 | |
322 | Acetylation | SPAINYTKLKNAVQN CCCCCHHHHHHHHCC | 47.29 | 24489116 | |
322 | 2-Hydroxyisobutyrylation | SPAINYTKLKNAVQN CCCCCHHHHHHHHCC | 47.29 | - | |
334 | Phosphorylation | VQNESVSSPIELNFD HCCCCCCCCEEECCC | 27.95 | 27214570 | |
344 | Acetylation | ELNFDAVKDFKLGKF EECCCCCCCCCCCCC | 60.20 | 24489116 |
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 QCR2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of QCR2_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 QCR2_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Profiling phosphoproteins of yeast mitochondria reveals a role ofphosphorylation in assembly of the ATP synthase."; Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.; Mol. Cell. Proteomics 6:1896-1906(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, AND MASSSPECTROMETRY. |