P21375

Name	Fumarate reductase 2 (FRDS2) (EC 1.3.1.6) (NADH-dependent fumarate reductase) (Osmotic sensitivity protein 1) (Soluble fumarate reductase, mitochondrial isozyme)
Uniprot ID	P21375
Systematic gene name	YJR051W
Standard gene name	OSM1
Gene names	OSM1 YJR051W J1659
Description from SGD	YJR051W OSM1 SGDID:S000003812, Chr X from 529861-531366, Genome Release 64-3-1, Verified ORF, "Fumarate reductase, catalyzes the reduction of fumarate to succinate; required for the reoxidation of intracellular NADH under anaerobic conditions; mutations cause osmotic sensitivity; has two translation start sites, one at the annotated start codon which produces an ER-targeted form required for anaerobic growth, and one at codon 32 which produces a mitochondrially-targeted form; OSM1 has a paralog, FRD1, that arose from the whole genome duplication"
Protein length	501
Download	sequence (fasta, from Uniprot), modifications (csv format)
Database links	Uniprot, SGD, TheCellVision.org, FungiDB

MIRSVRRVFI YVSIFVLIIV LKRTLSGTDQ TSMKQPVVVI GSGLAGLTTS
NRLISKYRIP VVLLDKAASI GGNSIKASSG INGAHTDTQQ NLKVMDTPEL
FLKDTLHSAK GRGVPSLMDK LTKESKSAIR WLQTEFDLKL DLLAQLGGHS
VPRTHRSSGK LPPGFEIVQA LSKKLKDISS KDSNLVQIML NSEVVDIELD
NQGHVTGVVY MDENGNRKIM KSHHVVFCSG GFGYSKEMLK EYSPNLIHLP
TTNGKQTTGD GQKILSKLGA ELIDMDQVQV HPTGFIDPND RENNWKFLAA
EALRGLGGIL LHPTTGRRFT NELSTRDTVT MEIQSKCPKN DNRALLVMSD
KVYENYTNNI NFYMSKNLIK KVSINDLIRQ YDLQTTASEL VTELKSYSDV
NTKDTFDRPL IINAFDKDIS TESTVYVGEV TPVVHFTMGG VKINEKSQVI
KKNSESVLSN GIFAAGEVSG GVHGANRLGG SSLLECVVFG KTAADNIAKL
Y

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.

[26, 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)
[26, 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)
[26, 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)
[26, 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)
[26, 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)
[26, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[78, 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)
[78, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[355, 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)