Basic Information
Name | Riboflavin kinase (EC 2.7.1.26) (Flavin mononucleotide kinase 1) |
Uniprot ID | Q03778 |
Systematic gene name | YDR236C |
Standard gene name | FMN1 |
Gene names | FMN1 YDR236C YD8419.03C |
Description from SGD | YDR236C FMN1 SGDID:S000002644, Chr IV from 935892-935236, Genome Release 64-3-1, reverse complement, Verified ORF, "Riboflavin kinase, produces riboflavin monophosphate (FMN); FMN is a necessary cofactor for many enzymes; predominantly localizes to the microsomal fraction and also found in the mitochondrial inner membrane; human RFK functionally complements the lethality of the null mutation" |
Protein length | 218 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MFTWTIYVSL LLVLAGTFLM NRNTNTDIID TFKREVDLPI PAQPGPPFPL
VTDYCDIVCG FGRGSAELGI PTANVPINQL PKGINDLDLG VYFGFAHIKT
VDGQELSVET RRDGRTVVYN YGQYLSEAND DLSVLPMVLS VGKNPFYGND
FKTMELHIIH DFKNDFYGAR VKFNILGHIR PELNYTTKEA LIEDINIDIR
TAQTVLATPP YQVFKQQL
VTDYCDIVCG FGRGSAELGI PTANVPINQL PKGINDLDLG VYFGFAHIKT
VDGQELSVET RRDGRTVVYN YGQYLSEAND DLSVLPMVLS VGKNPFYGND
FKTMELHIIH DFKNDFYGAR VKFNILGHIR PELNYTTKEA LIEDINIDIR
TAQTVLATPP YQVFKQQL
Legend
- X Phoshorylation
- X Glycosylation
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
[3, 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) |
[3, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[7, 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) |
[7, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[17, 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) |
[17, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[147, 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) |
[147, Phos] | Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications) |
[147, 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) |
[147, Phos] | Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications) |
[147, Phos] | Albuquerque, C.P., Smolka, M.B., Payne, S.H., Bafna, V., Eng, J., Zhou, H. (2008). A multidimensional chromatography technology for in-depth phosphoproteome analysis. Molecular and Cellular Proteomics 7(7):1389-1396. (Publication) (All modifications) |
[147, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[187, 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) |