Basic Information
Name | Mitochondrial intermembrane space cysteine motif-containing protein MIX17 (Mitochondrial intermembrane space CX(n)C motif protein of 17 kDa) |
Uniprot ID | Q03667 |
Systematic gene name | YMR002W |
Standard gene name | MIX17 |
Gene names | MIX17 MIC17 YMR002W YM8270.04 |
Description from SGD | YMR002W MIX17 SGDID:S000004604, Chr XIII from 272193-272663, Genome Release 64-3-1, Verified ORF, "Mitochondrial intermembrane space protein; required for normal oxygen consumption; contains twin cysteine-x9-cysteine motifs; protein abundance increases in response to DNA replication stress" |
Protein length | 156 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MARSRGSSRP ISRSRPTQTR SASTMAAPVH PQQQQQPNAY SHPPAAGAQT
RQPGMFAQMA STAAGVAVGS TIGHTLGAGI TGMFSGSGSD SAPVEQQQQN
MANTSGQTQT DQQLGRTCEI DARNFTRCLD ENNGNFQICD YYLQQLKACQ
EAARQY
RQPGMFAQMA STAAGVAVGS TIGHTLGAGI TGMFSGSGSD SAPVEQQQQN
MANTSGQTQT DQQLGRTCEI DARNFTRCLD ENNGNFQICD YYLQQLKACQ
EAARQY
Legend
- X Phoshorylation
- X Glycosylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[7, Phos] | MacGilvray, M.E., Shishkova, E., Place, M., Wagner, E.R., Coon, J.J., Gasch, A.P. (2020). Phosphoproteome response to dithiothreitol reveals unique versus shared features of Saccharomyces cerevisiae stress responses. Journal of Proteome Research 19(8): 3405-3417. (Publication) (All modifications) |
[12, Phos] | Guo X, Niemi NM, Coon JJ, Pagliarini DJ (2017a) Integrative proteomics and biochemical analyses define Ptc6p as the Saccharomyces cerevisiae pyruvate dehydrogenase phosphatase. J Biol Chem 292:11751–11759. (Publication) (All modifications) |
[12, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[21, 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) |
[21, Phos] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[21, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[23, 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) |
[23, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[124, Glyc] | Zielinska, D.F., Gnad, F., Schropp, K., Wiśniewski, J.R., Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications) |