UniProt ID | QCR6_MOUSE | |
---|---|---|
UniProt AC | P99028 | |
Protein Name | Cytochrome b-c1 complex subunit 6, mitochondrial | |
Gene Name | Uqcrh | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 89 | |
Subcellular Localization | Mitochondrion inner membrane . | |
Protein Description | This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This protein may mediate formation of the complex between cytochromes c and c1 (By similarity).. | |
Protein Sequence | MGLEDERKMLTGSGDPKEEEEEELVDPLTTVREHCEQLEKCVKARERLELCDNRVSSRSQTEEDCTEELFDFLHARDHCVAHKLFKNLK | |
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 |
---|---|---|---|---|---|
11 | Phosphorylation | EDERKMLTGSGDPKE HHHHHHHCCCCCCHH | 26.29 | 22817900 | |
13 | Phosphorylation | ERKMLTGSGDPKEEE HHHHHCCCCCCHHHH | 34.48 | 22817900 | |
29 | Phosphorylation | EELVDPLTTVREHCE HHHCCHHHHHHHHHH | 28.74 | - | |
30 | Phosphorylation | ELVDPLTTVREHCEQ HHCCHHHHHHHHHHH | 25.83 | - | |
35 | S-nitrosocysteine | LTTVREHCEQLEKCV HHHHHHHHHHHHHHH | 2.82 | - | |
35 | S-nitrosylation | LTTVREHCEQLEKCV HHHHHHHHHHHHHHH | 2.82 | 21278135 | |
40 | Acetylation | EHCEQLEKCVKARER HHHHHHHHHHHHHHH | 53.58 | 23576753 | |
40 | Malonylation | EHCEQLEKCVKARER HHHHHHHHHHHHHHH | 53.58 | 26320211 | |
51 | S-palmitoylation | ARERLELCDNRVSSR HHHHHHHCCCCCCCC | 2.96 | 26165157 | |
51 | S-nitrosylation | ARERLELCDNRVSSR HHHHHHHCCCCCCCC | 2.96 | 21278135 | |
51 | Glutathionylation | ARERLELCDNRVSSR HHHHHHHCCCCCCCC | 2.96 | 24333276 | |
51 | S-nitrosocysteine | ARERLELCDNRVSSR HHHHHHHCCCCCCCC | 2.96 | - | |
56 | Phosphorylation | ELCDNRVSSRSQTEE HHCCCCCCCCCCCHH | 19.45 | 26643407 | |
57 | Phosphorylation | LCDNRVSSRSQTEED HCCCCCCCCCCCHHH | 32.85 | 26643407 | |
59 | Phosphorylation | DNRVSSRSQTEEDCT CCCCCCCCCCHHHHH | 43.32 | 21082442 | |
61 | Phosphorylation | RVSSRSQTEEDCTEE CCCCCCCCHHHHHHH | 42.46 | 21082442 | |
65 | S-nitrosocysteine | RSQTEEDCTEELFDF CCCCHHHHHHHHHHH | 6.12 | - | |
65 | Glutathionylation | RSQTEEDCTEELFDF CCCCHHHHHHHHHHH | 6.12 | 24333276 | |
65 | S-nitrosylation | RSQTEEDCTEELFDF CCCCHHHHHHHHHHH | 6.12 | 24895380 | |
66 | Phosphorylation | SQTEEDCTEELFDFL CCCHHHHHHHHHHHH | 44.83 | 23140645 | |
83 | Acetylation | RDHCVAHKLFKNLK- HHHHHHHHHHHHCC- | 45.97 | 23576753 | |
83 | Phosphoglycerylation | RDHCVAHKLFKNLK- HHHHHHHHHHHHCC- | 45.97 | - | |
83 | Malonylation | RDHCVAHKLFKNLK- HHHHHHHHHHHHCC- | 45.97 | 26320211 | |
83 | Succinylation | RDHCVAHKLFKNLK- HHHHHHHHHHHHCC- | 45.97 | 24315375 | |
86 | Acetylation | CVAHKLFKNLK---- HHHHHHHHHCC---- | 72.33 | 23864654 | |
86 | Ubiquitination | CVAHKLFKNLK---- HHHHHHHHHCC---- | 72.33 | 27667366 | |
86 | Malonylation | CVAHKLFKNLK---- HHHHHHHHHCC---- | 72.33 | 26073543 |
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 QCR6_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of QCR6_MOUSE !! |
* 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 QCR6_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of QCR6_MOUSE !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-40, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-61, AND MASSSPECTROMETRY. |