P08679

Name	Citrate synthase, peroxisomal (EC 2.3.3.16)
Uniprot ID	P08679
Systematic gene name	YCR005C
Standard gene name	CIT2
Gene names	CIT2 YCR005C YCR043 YCR5C
Description from SGD	YCR005C CIT2 SGDID:S000000598, Chr III from 122328-120946, Genome Release 64-3-1, reverse complement, Verified ORF, "Citrate synthase, peroxisomal isozyme involved in glyoxylate cycle; catalyzes condensation of acetyl coenzyme A and oxaloacetate to form citrate; expression is controlled by Rtg1p and Rtg2p transcription factors; SCF-Ucc1 regulates level of Cit2p to maintain citrate homeostasis; oxaloacetate-dependent positive feedback loop inhibits Cit2p ubiquitination; CIT2 has a paralog, CIT1, that arose from the whole genome duplication"
Protein length	460
Download	sequence (fasta, from Uniprot), modifications (csv format)
Database links	Uniprot, SGD, TheCellVision.org, FungiDB

MTVPYLNSNR NVASYLQSNS SQEKTLKERF SEIYPIHAQD VRQFVKEHGK
TKISDVLLEQ VYGGMRGIPG SVWEGSVLDP EDGIRFRGRT IADIQKDLPK
AKGSSQPLPE ALFWLLLTGE VPTQAQVENL SADLMSRSEL PSHVVQLLDN
LPKDLHPMAQ FSIAVTALES ESKFAKAYAQ GISKQDYWSY TFEDSLDLLG
KLPVIAAKIY RNVFKDGKMG EVDPNADYAK NLVNLIGSKD EDFVDLMRLY
LTIHSDHEGG NVSAHTSHLV GSALSSPYLS LASGLNGLAG PLHGRANQEV
LEWLFALKEE VNDDYSKDTI EKYLWDTLNS GRVIPGYGHA VLRKTDPRYM
AQRKFAMDHF PDYELFKLVS SIYEVAPGVL TEHGKTKNPW PNVDAHSGVL
LQYYGLKESS FYTVLFGVSR AFGILAQLIT DRAIGASIER PKSYSTEKYK
ELVKNIESKL

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[8, 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)
[8, Phos]	Renvoisé M, Bonhomme L, Davanture M, et al (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. Journal of Proteomics 106:140–150. (Publication) (All modifications)
[8, 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)
[8, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[14, Phos]	Renvoisé M, Bonhomme L, Davanture M, et al (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. Journal of Proteomics 106:140–150. (Publication) (All modifications)
[14, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[15, Phos]	Renvoisé M, Bonhomme L, Davanture M, et al (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. Journal of Proteomics 106:140–150. (Publication) (All modifications)
[15, 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)
[15, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[18, 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)
[20, 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)
[20, 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)
[21, 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)
[21, 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)
[21, 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)
[21, 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)
[21, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[176, 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)
[215, 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)
[218, 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)
[218, Ubi]	Kolawa, N., Sweredoski, M.J., Graham, R.L., Oania, R., Hess, S., Deshaies, R.J. (2013). Perturbations to the ubiquitin conjugate proteome in yeast δubx mutants identify Ubx2 as a regulator of membrane lipid composition. Mol Cell Proteomics 12: 2791-2803. (Publication) (All modifications)
[239, 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)
[239, Ubi]	Kolawa, N., Sweredoski, M.J., Graham, R.L., Oania, R., Hess, S., Deshaies, R.J. (2013). Perturbations to the ubiquitin conjugate proteome in yeast δubx mutants identify Ubx2 as a regulator of membrane lipid composition. Mol Cell Proteomics 12: 2791-2803. (Publication) (All modifications)
[239, Ubi]	Seyfried, N.T., Xu, P., Duong, D.M., Cheng, D., Hanfelt, J., Peng, J. (2008). Systematic approach for validating the ubiquitinated proteome. Anal Chem 80: 4161-4169. (Publication) (All modifications)
[327, 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)
[327, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[330, 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)
[330, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[354, Ubi]	Peng, J.,  Schwartz, D.,  Elias, J.E.,  Thoreen, C.C.,  Cheng, D.,  Marsischky, G.,  Roelofs, J.,  Finley, D.,  Gygi, S.P. (2003). A proteomics approach to understanding protein ubiquitination. Nat Biotechnol 21: 921-926. (Publication) (All modifications)
[385, Ubi]	Peng, J.,  Schwartz, D.,  Elias, J.E.,  Thoreen, C.C.,  Cheng, D.,  Marsischky, G.,  Roelofs, J.,  Finley, D.,  Gygi, S.P. (2003). A proteomics approach to understanding protein ubiquitination. Nat Biotechnol 21: 921-926. (Publication) (All modifications)
[454, Ubi]	Back, S., Gorman, A.W., Vogel, C., Silva, G.M. (2019). Site-specific K63 ubiquitinomics provides insights into translation regulation under stress. Journal of Proteome Research 18(1): 309-318. (Publication) (All modifications)
[454, 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)
[454, Ubi]	Fang, N.N.,  Chan, G.T.,  Zhu, M.,  Comyn, S.A.,  Persaud, A.,  Deshaies, R.J.,  Rotin, D.,  Gsponer, J.,  Mayor, T. (2014). Rsp5/Nedd4 is the main ubiquitin ligase that targets cytosolic misfolded proteins following heat stress. Nature Cell Biology 16(12): 1227-1237. (Publication) (All modifications)