Basic Information
Name | 3-ketodihydrosphingosine reductase TSC10 (EC 1.1.1.102) (3-dehydrosphinganine reductase) (KDS reductase) (Temperature-sensitive CSG2 suppressor protein 10) |
Uniprot ID | P38342 |
Systematic gene name | YBR265W |
Standard gene name | TSC10 |
Gene names | TSC10 YBR265W YBR1734 |
Description from SGD | YBR265W TSC10 SGDID:S000000469, Chr II from 738582-739544, Genome Release 64-3-1, Verified ORF, "3-ketosphinganine reductase; catalyzes the second step in phytosphingosine synthesis; essential for growth in the absence of exogenous dihydrosphingosine or phytosphingosine; localized to lipid droplets; member of short chain dehydrogenase/reductase protein family; mutations in human homolog KDSR cause recessive progressive symmetric erythrokeratoderma" |
Protein length | 320 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MKFTLEDQVV LITGGSQGLG KEFAKKYYNE AENTKIIIVS RSEARLLDTC
NEIRIEAHLR RETTDEGQVQ HKLAAPLDLE QRLFYYPCDL SCYESVECLF
NALRDLDLLP TQTLCCAGGA VPKLFRGLSG HELNLGMDIN YKTTLNVAHQ
IALAEQTKEH HLIIFSSATA LYPFVGYSQY APAKAAIKSL VAILRQELTN
FRISCVYPGN FESEGFTVEQ LTKPEITKLI EGPSDAIPCK QACDIIAKSL
ARGDDDVFTD FVGWMIMGMD LGLTAKKSRF VPLQWIFGVL SNILVVPFYM
VGCSWYIRKW FRENDGKKAN
NEIRIEAHLR RETTDEGQVQ HKLAAPLDLE QRLFYYPCDL SCYESVECLF
NALRDLDLLP TQTLCCAGGA VPKLFRGLSG HELNLGMDIN YKTTLNVAHQ
IALAEQTKEH HLIIFSSATA LYPFVGYSQY APAKAAIKSL VAILRQELTN
FRISCVYPGN FESEGFTVEQ LTKPEITKLI EGPSDAIPCK QACDIIAKSL
ARGDDDVFTD FVGWMIMGMD LGLTAKKSRF VPLQWIFGVL SNILVVPFYM
VGCSWYIRKW FRENDGKKAN
Legend
- X Phoshorylation
- X Ubiquitination
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[63, 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) |
[63, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[64, 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) |
[64, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[72, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[223, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[240, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |