Basic Information

NameProbable electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial (ETF-QO) (ETF-ubiquinone oxidoreductase) (EC 1.5.5.1) (Changed intracellular redox state protein 2) (Electron-transferring-flavoprotein dehydrogenase) (ETF dehydrogenase)
Uniprot IDQ08822
Systematic gene nameYOR356W
Standard gene nameCIR2
Gene namesCIR2 YOR356W
Description from SGDYOR356W CIR2 SGDID:S000005883, Chr XV from 1007221-1009116, Genome Release 64-3-1, Verified ORF, "Putative ortholog of human ETF-dH; found in a large supramolecular complex with other mitochondrial dehydrogenases; may have a role in oxidative stress response; ETF-dH is also known as electron transfer flavoprotein dehydrogenase"
Protein length631
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MIKFTNENLI RGIRMTISAK SRHLALGTDM TRKFSLSCRF LNKANLTEEE
KELLNEPRAR DYVDVCIVGG GPAGLATAIK LKQLDNSSGT GQLRVVVLEK
SSVLGGQTVS GAILEPGVWK ELFPDEKSDI GIPLPKELAT LVTKEHLKFL
KGKWAISVPE PSQMINKGRN YIVSLNQVVG YLGEKAEEVG VEVYPGIAVS
DLIYDENNAV KGVITKDAGI SKSGKPKETF ERGMEFWARQ TVLAEGCHGS
LTKQALAKYD LRKGRQHQTY GLGIKEVWEV KPENFNKGFA AHTMGYPLTN
DVYGGGFQYH FGDGLVTVGL VVGLDYKNPY VSPYKEFQKM KHHPYYSKVL
EGGKCIAYAA RALNEGGLQS VPKLNFPGGV LVGASAGFMN VPKIKGTHTA
MKSGLLAAES IFESIKGLPV LEEVEDEDAK MAMFDKEATI NLESYESAFK
ESSIYKELYE VRNIRPSFSG KLGGYGGMIY SGIDSLILKG KVPWTLKFDE
KNDGEILEPA SKYKPIEYPK PDGVISFDIL TSVSRTGTYH DDDEPCHLRV
PGQDMVKYAE RSFPVWKGVE SRFCPAGVYE FVKDEKSPVG TRLQINSQNC
IHCKTCDIKA PRQDITWKVP EGGDGPKYTL T

Legend

  • X Ubiquitination
  • X K-Succinylation
  • X Multiple modifications
  • X Phoshorylation

Structure

Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.


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References

[3, Ubi]Kolawa, N., Sweredoski, M.J., Graham, R.L., Oania, R., Hess, S., Deshaies, R.J. (2013). Perturbations to the ubiquitin conjugate proteome in yeast δubx mutants identify Ubx2 as a regulator of membrane lipid composition. Mol Cell Proteomics 12: 2791-2803. (Publication) (All modifications)
[127, 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)
[144, 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)
[335, 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)
[335, 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)
[339, 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)
[467, 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)
[469, 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)
[471, Ubi]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)
[520, 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)
[567, 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)
[583, 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)
[618, 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)