UniProt ID | QCR1_YEAST | |
---|---|---|
UniProt AC | P07256 | |
Protein Name | Cytochrome b-c1 complex subunit 1, mitochondrial | |
Gene Name | COR1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 457 | |
Subcellular Localization | Mitochondrion inner membrane . | |
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. COR1 may mediate formation of the complex between cytochromes c and c1.. | |
Protein Sequence | MLRTVTSKTVSNQFKRSLATAVATPKAEVTQLSNGIVVATEHNPSAHTASVGVVFGSGAANENPYNNGVSNLWKNIFLSKENSAVAAKEGLALSSNISRDFQSYIVSSLPGSTDKSLDFLNQSFIQQKANLLSSSNFEATKKSVLKQVQDFEENDHPNRVLEHLHSTAFQNTPLSLPTRGTLESLENLVVADLESFANNHFLNSNAVVVGTGNIKHEDLVNSIESKNLSLQTGTKPVLKKKAAFLGSEVRLRDDTLPKAWISLAVEGEPVNSPNYFVAKLAAQIFGSYNAFEPASRLQGIKLLDNIQEYQLCDNFNHFSLSYKDSGLWGFSTATRNVTMIDDLIHFTLKQWNRLTISVTDTEVERAKSLLKLQLGQLYESGNPVNDANLLGAEVLIKGSKLSLGEAFKKIDAITVKDVKAWAGKRLWDQDIAIAGTGQIEGLLDYMRIRSDMSMMRW | |
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 |
---|---|---|---|---|---|
4 | Phosphorylation | ----MLRTVTSKTVS ----CCCCCCCHHHH | 24.95 | 30377154 | |
6 | Phosphorylation | --MLRTVTSKTVSNQ --CCCCCCCHHHHHH | 24.72 | 30377154 | |
9 | Phosphorylation | LRTVTSKTVSNQFKR CCCCCCHHHHHHHHH | 29.00 | 30377154 | |
11 | Phosphorylation | TVTSKTVSNQFKRSL CCCCHHHHHHHHHHH | 30.10 | 30377154 | |
20 | Phosphorylation | QFKRSLATAVATPKA HHHHHHHHHHCCCCH | 27.27 | 28889911 | |
24 | Phosphorylation | SLATAVATPKAEVTQ HHHHHHCCCCHHHEE | 20.80 | 27214570 | |
80 | 2-Hydroxyisobutyrylation | WKNIFLSKENSAVAA HHHHHHCCCCHHHHH | 64.16 | - | |
80 | Acetylation | WKNIFLSKENSAVAA HHHHHHCCCCHHHHH | 64.16 | 24489116 | |
94 | Phosphorylation | AKEGLALSSNISRDF HHHHHCCCCCCCHHH | 18.74 | 27214570 | |
133 | Phosphorylation | QQKANLLSSSNFEAT HHHHHHHCCCCHHHH | 34.58 | 27214570 | |
134 | Phosphorylation | QKANLLSSSNFEATK HHHHHHCCCCHHHHH | 29.30 | 27214570 | |
135 | Phosphorylation | KANLLSSSNFEATKK HHHHHCCCCHHHHHH | 42.01 | 23749301 | |
140 | Phosphorylation | SSSNFEATKKSVLKQ CCCCHHHHHHHHHHH | 31.63 | 28889911 | |
141 | 2-Hydroxyisobutyrylation | SSNFEATKKSVLKQV CCCHHHHHHHHHHHH | 50.53 | - | |
146 | Acetylation | ATKKSVLKQVQDFEE HHHHHHHHHHHHHCC | 46.39 | 24489116 | |
166 | Phosphorylation | RVLEHLHSTAFQNTP HHHHHHHHCCCCCCC | 27.99 | 22369663 | |
167 | Phosphorylation | VLEHLHSTAFQNTPL HHHHHHHCCCCCCCC | 22.27 | 22369663 | |
172 | Phosphorylation | HSTAFQNTPLSLPTR HHCCCCCCCCCCCCC | 18.15 | 22369663 | |
175 | Phosphorylation | AFQNTPLSLPTRGTL CCCCCCCCCCCCCHH | 33.24 | 22369663 | |
178 | Phosphorylation | NTPLSLPTRGTLESL CCCCCCCCCCHHHHH | 47.20 | 22369663 | |
235 | Acetylation | LSLQTGTKPVLKKKA CCCCCCCCCHHHHHH | 34.18 | 24489116 | |
247 | Phosphorylation | KKAAFLGSEVRLRDD HHHHHHCCEEEECCC | 34.76 | 27214570 | |
272 | Phosphorylation | VEGEPVNSPNYFVAK ECCCCCCCCCHHHHH | 18.11 | 27214570 | |
287 | Phosphorylation | LAAQIFGSYNAFEPA HHHHHHCCCCCCCCH | 12.40 | 24909858 | |
357 | Phosphorylation | QWNRLTISVTDTEVE HHCCEEEEEEHHHHH | 17.46 | 26447709 | |
359 | Phosphorylation | NRLTISVTDTEVERA CCEEEEEEHHHHHHH | 30.34 | 26447709 | |
408 | Acetylation | LSLGEAFKKIDAITV CCHHHHHHHCCEEEH | 56.73 | 24489116 | |
408 | Succinylation | LSLGEAFKKIDAITV CCHHHHHHHCCEEEH | 56.73 | 23954790 | |
409 | 2-Hydroxyisobutyrylation | SLGEAFKKIDAITVK CHHHHHHHCCEEEHH | 39.09 | - | |
416 | Acetylation | KIDAITVKDVKAWAG HCCEEEHHHHHHHCC | 48.42 | 24489116 | |
419 | 2-Hydroxyisobutyrylation | AITVKDVKAWAGKRL EEEHHHHHHHCCCCC | 48.63 | - | |
424 | 2-Hydroxyisobutyrylation | DVKAWAGKRLWDQDI HHHHHCCCCCCCCCE | 36.25 | - |
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 QCR1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of QCR1_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 QCR1_YEAST !! |
Kegg Drug | ||||||
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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 THR-140, AND MASSSPECTROMETRY. |