Basic Information
Name | Ubiquinone biosynthesis protein COQ9, mitochondrial |
Uniprot ID | Q05779 |
Systematic gene name | YLR201C |
Standard gene name | COQ9 |
Gene names | COQ9 YLR201C |
Description from SGD | YLR201C COQ9 SGDID:S000004191, Chr XII from 550293-549511, Genome Release 64-3-1, reverse complement, Verified ORF, "Protein required for ubiquinone biosynthesis and respiratory growth; localizes to matrix face of mitochondrial inner membrane in a large complex with ubiquinone biosynthetic enzymes; ubiquinone is also known as coenzyme Q; human homolog COQ9 can complement yeast coq9 null mutant" |
Protein length | 260 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MLCRNTARTG CKFFRLYHSN PIEHVKPIHI KPLTYGKESP QYKVLSLALQ
KFVPEHGFSE RSIVESLNEL GYPSSMISSI GAPNSPSFFH SSTAVMELIK
FQLVDKRYRL TEGINPDVTP QYKLPSLEHL LLKRLEMDKP IGGHLSELMS
QLAIPSAFLF ETAIPELHRL SDDMIYFSNE KDHHDSAWYA KRLAVSSTYI
GSKLFMAQDK SHNYKETFTF AKDKLHRVMR LGEYYNNTEE FAWYTLMSTV
NLIKSQLVRG
KFVPEHGFSE RSIVESLNEL GYPSSMISSI GAPNSPSFFH SSTAVMELIK
FQLVDKRYRL TEGINPDVTP QYKLPSLEHL LLKRLEMDKP IGGHLSELMS
QLAIPSAFLF ETAIPELHRL SDDMIYFSNE KDHHDSAWYA KRLAVSSTYI
GSKLFMAQDK SHNYKETFTF AKDKLHRVMR LGEYYNNTEE FAWYTLMSTV
NLIKSQLVRG
Legend
- X Phoshorylation
- X K-Succinylation
- X Multiple modifications
- X K-acetylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[9, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[9, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[34, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[34, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[123, K-succ] | Frankovsky, J., Keresztesová, B., Bellová, J., et al. (2021). The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids. Journal of Biological Chemistry, 297(4): 101155. (Publication) (All modifications) |
[133, K-succ] | Frankovsky, J., Keresztesová, B., Bellová, J., et al. (2021). The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids. Journal of Biological Chemistry, 297(4): 101155. (Publication) (All modifications) |
[133, K-acetyl] | Henriksen, P., Wagner, S. A., Weinert, B. T., et al. (2012). Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & Cellular Proteomics, 11(11), 1510-1522. (Publication) (All modifications) |
[178, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[215, K-acetyl] | Henriksen, P., Wagner, S. A., Weinert, B. T., et al. (2012). Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & Cellular Proteomics, 11(11), 1510-1522. (Publication) (All modifications) |