Basic Information
Name | Monothiol glutaredoxin-5, mitochondrial |
Uniprot ID | Q02784 |
Systematic gene name | YPL059W |
Standard gene name | GRX5 |
Gene names | GRX5 YPL059W LPE13W |
Description from SGD | YPL059W GRX5 SGDID:S000005980, Chr XVI from 444579-445031, Genome Release 64-3-1, Verified ORF, "Glutathione-dependent oxidoreductase; mitochondrial matrix protein involved at an early step in the biogenesis of iron-sulfur centers along with Bol1p; hydroperoxide and superoxide-radical responsive; monothiol glutaredoxin subfamily member along with Grx3p and Grx4p" |
Protein length | 150 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MFLPKFNPIR SFSPILRAKT LLRYQNRMYL STEIRKAIED AIESAPVVLF
MKGTPEFPKC GFSRATIGLL GNQGVDPAKF AAYNVLEDPE LREGIKEFSE
WPTIPQLYVN KEFIGGCDVI TSMARSGELA DLLEEAQALV PEEEEETKDR
MKGTPEFPKC GFSRATIGLL GNQGVDPAKF AAYNVLEDPE LREGIKEFSE
WPTIPQLYVN KEFIGGCDVI TSMARSGELA DLLEEAQALV PEEEEETKDR
Legend
- X K-Succinylation
- X Multiple modifications
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[52, K-succ] | Weinert, B.T., Schölz, C., Wagner, S.A., et al. (2013). Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. Cell Reports, 4(4), 842-851. (Publication) (All modifications) |
[52, 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) |
[59, 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) |
[59, 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) |