Basic Information

NameExternal NADH-ubiquinone oxidoreductase 2, mitochondrial (EC 1.6.5.9) (External NADH dehydrogenase 2)
Uniprot IDQ07500
Systematic gene nameYDL085W
Standard gene nameNDE2
Gene namesNDE2 NDH2 YDL085W
Description from SGDYDL085W NDE2 SGDID:S000002243, Chr IV from 303211-304848, Genome Release 64-3-1, Verified ORF, "Mitochondrial external NADH dehydrogenase; catalyzes the oxidation of cytosolic NADH; Nde1p and Nde2p are involved in providing the cytosolic NADH to the mitochondrial respiratory chain; NDE2 has a paralog, NDE1, that arose from the whole genome duplication"
Protein length545
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MLPRLGFART ARSIHRFKMT QISKPFFHST EVGKPGPQQK LSKSYTAVFK
KWFVRGLKLT FYTTLAGTLY VSYELYKESN PPKQVPQSTA FANGLKKKEL
VILGTGWGAI SLLKKLDTSL YNVTVVSPRS FFLFTPLLPS TPVGTIEMKS
IVEPVRSIAR RTPGEVHYIE AEALDVDPKA KKVMVQSVSE DEYFVSSLSY
DYLVVSVGAK TTTFNIPGVY GNANFLKEIE DAQNIRMKLM KTIEQASSFP
VNDPERKRLL TFVVVGGGPT GVEFAAELQD YINQDLRKWM PDLSKEMKVI
LIEALPNILN MFDKTLIKYA EDLFARDEID LQVNTAVKVV EPTYIRTLQN
GQTNTDIEYG MLVWATGNEP IDFSKTLMSR IPEQTNRRGL LINDKLELLG
SENSIYAIGD CTAHTGFFPT AQVAHQEGEY LAKILDKKLQ IEQLEWDMLN
STDETEVSRL QKEVNLRKSK LDKFNYKHMG ALAYIGSETA IADLHMGDSS
YQLKGMFAFL FWKSAYLAMC LSIRNRILIA MDWTKVYFLG RDSSV

Legend

  • X Phoshorylation
  • X K-Succinylation

Structure

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


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References

[79, 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)
[79, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[88, 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)
[88, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[89, 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)
[89, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[462, 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)
[499, Phos]Papinski, D., Schuschnig, M., Reiter, W., Wilhelm, L., Barnes, C.A., Maiolica, A., Hansmann, I., Pfaffenwimmer, T., Kijanska, M., Stoffel, I., Lee, S.S., Brezovich, A., Lou, J.H., Turk, B.E., Aebersold, R., Ammerer, G., Peter, M., Kraft, C. (2014). Early steps in autophagy depend on direct phosphorylation of Atg9 by the Atg1 kinase. Mol Cell 53: 471-483. (Publication) (All modifications)