Basic Information
Name | Phosphatidylserine decarboxylase proenzyme 1, mitochondrial (EC 4.1.1.65) [Cleaved into: Phosphatidylserine decarboxylase 1 beta chain; Phosphatidylserine decarboxylase 1 alpha chain] |
Uniprot ID | P39006 |
Systematic gene name | YNL169C |
Standard gene name | PSD1 |
Gene names | PSD1 YNL169C N1692 |
Description from SGD | YNL169C PSD1 SGDID:S000005113, Chr XIV from 317671-316169, Genome Release 64-3-1, reverse complement, Verified ORF, "Phosphatidylserine decarboxylase of the mitochondrial inner membrane; converts phosphatidylserine to phosphatidylethanolamine; regulates mitochondrial fusion and morphology by affecting lipid mixing in the mitochondrial membrane and by influencing the ratio of long to short forms of Mgm1p; partly exposed to the mitochondrial intermembrane space; autocatalytically processed" |
Protein length | 500 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MSIMPVKNAL AQGRTLLMGR MPAVKFSTRM QLRNRTAVLW NRKFSTRLFV
QQRRSSGEIV DRAKAAAANS GRKQVSMKWV VLTSFTIVLG TILLVSRNDS
TEEDATEGKK GRRTRKIKIF NNNWLFFCYS TLPLNAMSRL WGQVNSLTLP
IWVRPWGYRL YSFLFGVNLD EMEDPDLTHY ANLSEFFYRN IKPGTRPVAQ
GEDVIASPSD GKILQVGIIN SETGEIEQVK GMTYSIKEFL GTHSHPLMSK
SASSLDLTSD EEKHREFARV NRIQLAGSED TEQPLLNFKN EGDQSVREFK
PSVSKNIHLL SQLSLNYFSN GFSCSEPHDT ELFFAVIYLA PGDYHHFHSP
VDWVCKVRRH FPGDLFSVAP YFQRNFPNLF VLNERVALLG SWKYGFFSMT
PVGATNVGSI KLNFDQEFVT NSKSDKHLEP HTCYQAVYEN ASKILGGMPL
VKGEEMGGFE LGSTVVLCFE APTEFKFDVR VGDKVKMGQK LGIIGKNDLK
QQRRSSGEIV DRAKAAAANS GRKQVSMKWV VLTSFTIVLG TILLVSRNDS
TEEDATEGKK GRRTRKIKIF NNNWLFFCYS TLPLNAMSRL WGQVNSLTLP
IWVRPWGYRL YSFLFGVNLD EMEDPDLTHY ANLSEFFYRN IKPGTRPVAQ
GEDVIASPSD GKILQVGIIN SETGEIEQVK GMTYSIKEFL GTHSHPLMSK
SASSLDLTSD EEKHREFARV NRIQLAGSED TEQPLLNFKN EGDQSVREFK
PSVSKNIHLL SQLSLNYFSN GFSCSEPHDT ELFFAVIYLA PGDYHHFHSP
VDWVCKVRRH FPGDLFSVAP YFQRNFPNLF VLNERVALLG SWKYGFFSMT
PVGATNVGSI KLNFDQEFVT NSKSDKHLEP HTCYQAVYEN ASKILGGMPL
VKGEEMGGFE LGSTVVLCFE APTEFKFDVR VGDKVKMGQK LGIIGKNDLK
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
[56, 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) |
[192, 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) |
[253, 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) |
[253, 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) |
[253, 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) |
[253, Phos] | Soulard, A., Cremonesi, A., Moes, S., Schütz, F., Jenö, P., Hall, M.N. (2010). The rapamycin-sensitive phosphoproteome reveals that TOR controls protein kinase A toward some but not all substrates. Molecular Biology of the Cell 21(19): 3475-3486. (Publication) (All modifications) |
[253, Phos] | 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) |
[253, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[254, 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) |
[254, 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) |
[254, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[259, 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) |
[289, 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) |
[423, 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) |