Basic Information
| Name | Uncharacterized mitochondrial hydrolase FMP41 (EC 3.-.-.-) |
| Uniprot ID | P53889 |
| Systematic gene name | YNL168C |
| Standard gene name | FMP41 |
| Gene names | FMP41 YNL168C N1696 |
| Description from SGD | YNL168C FMP41 SGDID:S000005112, Chr XIV from 318809-318030, Genome Release 64-3-1, reverse complement, Uncharacterized ORF, "Putative protein of unknown function; GFP-fusion protein is induced in response to the DNA-damaging agent MMS; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies" |
| Protein length | 259 |
| Download | sequence (fasta, from Uniprot), modifications (csv format) |
| Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MSYNYLKAAR KIICIGRNYA AHIKELNNST PKQPFFFLKP TSSIVTPLSS
SLVKTTRPAN STFNGLNEDG TNPGPIFIPR GVKVHHEIEL ALIVSKHLSN
VTKMKPEEVY DSISGVALAL DLTARNVQDE AKKKGLPWTI SKGFDTFMPI
SAIVSREKFS SYKSNLQDIF RVKCSVNGQL RQDGGTNLML HPLHKILQHI
STMISLEPGD IILTGTPAGV GELKPGDRVH CELLQNNDNI VDMNFECENR
PGPYEFRET
SLVKTTRPAN STFNGLNEDG TNPGPIFIPR GVKVHHEIEL ALIVSKHLSN
VTKMKPEEVY DSISGVALAL DLTARNVQDE AKKKGLPWTI SKGFDTFMPI
SAIVSREKFS SYKSNLQDIF RVKCSVNGQL RQDGGTNLML HPLHKILQHI
STMISLEPGD IILTGTPAGV GELKPGDRVH CELLQNNDNI VDMNFECENR
PGPYEFRET
Legend
- X Multiple modifications
- X Phoshorylation
- X K-Succinylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
Use imported representation
Loading structure from server... It may take a while.
If you believe something went wrong, please make sure PDB ID is correct.
Please also make sure that WebGL is enabled in your browser.
- Internet Explorer: sorry. IE doesn't support WebGL.
- Firefox (version 4 or later): try force enable WebGL.
- Chrome: try force enable WebGL.
- Safari: enable WebGL.
References
| [24, 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) |
| [24, 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) |
| [49, 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) |
| [132, 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) |