P00724

Name	Invertase 2 (EC 3.2.1.26) (Beta-fructofuranosidase 2) (Saccharase)
Uniprot ID	P00724
Systematic gene name	YIL162W
Standard gene name	SUC2
Gene names	SUC2 YIL162W
Description from SGD	YIL162W SUC2 SGDID:S000001424, Chr IX from 37385-38983, Genome Release 64-3-1, Verified ORF, "Invertase; sucrose hydrolyzing enzyme; a secreted, glycosylated form is regulated by glucose repression, and an intracellular, nonglycosylated enzyme is produced constitutively"
Protein length	532
Download	sequence (fasta, from Uniprot), modifications (csv format)
Database links	Uniprot, SGD, TheCellVision.org, FungiDB

MLLQAFLFLL AGFAAKISAS MTNETSDRPL VHFTPNKGWM NDPNGLWYDE
KDAKWHLYFQ YNPNDTVWGT PLFWGHATSD DLTNWEDQPI AIAPKRNDSG
AFSGSMVVDY NNTSGFFNDT IDPRQRCVAI WTYNTPESEE QYISYSLDGG
YTFTEYQKNP VLAANSTQFR DPKVFWYEPS QKWIMTAAKS QDYKIEIYSS
DDLKSWKLES AFANEGFLGY QYECPGLIEV PTEQDPSKSY WVMFISINPG
APAGGSFNQY FVGSFNGTHF EAFDNQSRVV DFGKDYYALQ TFFNTDPTYG
SALGIAWASN WEYSAFVPTN PWRSSMSLVR KFSLNTEYQA NPETELINLK
AEPILNISNA GPWSRFATNT TLTKANSYNV DLSNSTGTLE FELVYAVNTT
QTISKSVFAD LSLWFKGLED PEEYLRMGFE VSASSFFLDR GNSKVKFVKE
NPYFTNRMSV NNQPFKSEND LSYYKVYGLL DQNILELYFN DGDVVSTNTY
FMTTGNALGS VNMTTGVDNL FYIDKFQVRE VK

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[23, Glyc]	Ziegler, F.D., Maley, F., Trimble, R.B. (1988). Characterization of the glycosylation sites in yeast external invertase. II. Location of the endo-beta-N-acetylglucosaminidase H-resistant sequons. J Biol Chem 263: 6986-6992. (Publication) (All modifications)
[23, Glyc]	Yang, F., Zhang, X., Lu, Y., Wang, B., Chen, X., Sun, Z., Li, X. (2020). Inulin catabolism in Saccharomyces cerevisiae is affected by some key glycosylation sequons of invertase Suc2. Biotechnol Lett 42: 471-479. (Publication) (All modifications)
[64, Glyc]	Ziegler, F.D., Maley, F., Trimble, R.B. (1988). Characterization of the glycosylation sites in yeast external invertase. II. Location of the endo-beta-N-acetylglucosaminidase H-resistant sequons. J Biol Chem 263: 6986-6992. (Publication) (All modifications)
[64, Glyc]	Yang, F., Zhang, X., Lu, Y., Wang, B., Chen, X., Sun, Z., Li, X. (2020). Inulin catabolism in Saccharomyces cerevisiae is affected by some key glycosylation sequons of invertase Suc2. Biotechnol Lett 42: 471-479. (Publication) (All modifications)
[97, Glyc]	Ziegler, F.D., Maley, F., Trimble, R.B. (1988). Characterization of the glycosylation sites in yeast external invertase. II. Location of the endo-beta-N-acetylglucosaminidase H-resistant sequons. J Biol Chem 263: 6986-6992. (Publication) (All modifications)
[97, Glyc]	Yang, F., Zhang, X., Lu, Y., Wang, B., Chen, X., Sun, Z., Li, X. (2020). Inulin catabolism in Saccharomyces cerevisiae is affected by some key glycosylation sequons of invertase Suc2. Biotechnol Lett 42: 471-479. (Publication) (All modifications)
[111, Glyc]	Ziegler, F.D., Maley, F., Trimble, R.B. (1988). Characterization of the glycosylation sites in yeast external invertase. II. Location of the endo-beta-N-acetylglucosaminidase H-resistant sequons. J Biol Chem 263: 6986-6992. (Publication) (All modifications)
[111, Glyc]	Yang, F., Zhang, X., Lu, Y., Wang, B., Chen, X., Sun, Z., Li, X. (2020). Inulin catabolism in Saccharomyces cerevisiae is affected by some key glycosylation sequons of invertase Suc2. Biotechnol Lett 42: 471-479. (Publication) (All modifications)
[118, Glyc]	Ziegler, F.D., Maley, F., Trimble, R.B. (1988). Characterization of the glycosylation sites in yeast external invertase. II. Location of the endo-beta-N-acetylglucosaminidase H-resistant sequons. J Biol Chem 263: 6986-6992. (Publication) (All modifications)
[118, Glyc]	Yang, F., Zhang, X., Lu, Y., Wang, B., Chen, X., Sun, Z., Li, X. (2020). Inulin catabolism in Saccharomyces cerevisiae is affected by some key glycosylation sequons of invertase Suc2. Biotechnol Lett 42: 471-479. (Publication) (All modifications)
[165, 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)
[165, Glyc]	Cao, L.,  Yu, L.,  Guo, Z.,  Shen, A.,  Guo, Y.,  Liang, X. (2014). N-Glycosylation site analysis of proteins from Saccharomyces cerevisiae by using hydrophilic interaction liquid chromatography-based enrichment, parallel deglycosylation, and mass spectrometry. J Proteome Res 13: 1485-1493. (Publication) (All modifications)
[165, Glyc]	Ziegler, F.D., Maley, F., Trimble, R.B. (1988). Characterization of the glycosylation sites in yeast external invertase. II. Location of the endo-beta-N-acetylglucosaminidase H-resistant sequons. J Biol Chem 263: 6986-6992. (Publication) (All modifications)
[165, Glyc]	Yang, F., Zhang, X., Lu, Y., Wang, B., Chen, X., Sun, Z., Li, X. (2020). Inulin catabolism in Saccharomyces cerevisiae is affected by some key glycosylation sequons of invertase Suc2. Biotechnol Lett 42: 471-479. (Publication) (All modifications)
[167, 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)
[167, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[266, Glyc]	Ziegler, F.D., Maley, F., Trimble, R.B. (1988). Characterization of the glycosylation sites in yeast external invertase. II. Location of the endo-beta-N-acetylglucosaminidase H-resistant sequons. J Biol Chem 263: 6986-6992. (Publication) (All modifications)
[266, Glyc]	Yang, F., Zhang, X., Lu, Y., Wang, B., Chen, X., Sun, Z., Li, X. (2020). Inulin catabolism in Saccharomyces cerevisiae is affected by some key glycosylation sequons of invertase Suc2. Biotechnol Lett 42: 471-479. (Publication) (All modifications)
[275, Glyc]	Ziegler, F.D., Maley, F., Trimble, R.B. (1988). Characterization of the glycosylation sites in yeast external invertase. II. Location of the endo-beta-N-acetylglucosaminidase H-resistant sequons. J Biol Chem 263: 6986-6992. (Publication) (All modifications)
[275, Glyc]	Yang, F., Zhang, X., Lu, Y., Wang, B., Chen, X., Sun, Z., Li, X. (2020). Inulin catabolism in Saccharomyces cerevisiae is affected by some key glycosylation sequons of invertase Suc2. Biotechnol Lett 42: 471-479. (Publication) (All modifications)
[356, Glyc]	Cao, L.,  Yu, L.,  Guo, Z.,  Shen, A.,  Guo, Y.,  Liang, X. (2014). N-Glycosylation site analysis of proteins from Saccharomyces cerevisiae by using hydrophilic interaction liquid chromatography-based enrichment, parallel deglycosylation, and mass spectrometry. J Proteome Res 13: 1485-1493. (Publication) (All modifications)
[356, Glyc]	Ziegler, F.D., Maley, F., Trimble, R.B. (1988). Characterization of the glycosylation sites in yeast external invertase. II. Location of the endo-beta-N-acetylglucosaminidase H-resistant sequons. J Biol Chem 263: 6986-6992. (Publication) (All modifications)
[356, Glyc]	Yang, F., Zhang, X., Lu, Y., Wang, B., Chen, X., Sun, Z., Li, X. (2020). Inulin catabolism in Saccharomyces cerevisiae is affected by some key glycosylation sequons of invertase Suc2. Biotechnol Lett 42: 471-479. (Publication) (All modifications)
[369, 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)
[369, Glyc]	Cao, L.,  Yu, L.,  Guo, Z.,  Shen, A.,  Guo, Y.,  Liang, X. (2014). N-Glycosylation site analysis of proteins from Saccharomyces cerevisiae by using hydrophilic interaction liquid chromatography-based enrichment, parallel deglycosylation, and mass spectrometry. J Proteome Res 13: 1485-1493. (Publication) (All modifications)
[369, Glyc]	Ziegler, F.D., Maley, F., Trimble, R.B. (1988). Characterization of the glycosylation sites in yeast external invertase. II. Location of the endo-beta-N-acetylglucosaminidase H-resistant sequons. J Biol Chem 263: 6986-6992. (Publication) (All modifications)
[369, Glyc]	Yang, F., Zhang, X., Lu, Y., Wang, B., Chen, X., Sun, Z., Li, X. (2020). Inulin catabolism in Saccharomyces cerevisiae is affected by some key glycosylation sequons of invertase Suc2. Biotechnol Lett 42: 471-479. (Publication) (All modifications)
[384, Glyc]	Ziegler, F.D., Maley, F., Trimble, R.B. (1988). Characterization of the glycosylation sites in yeast external invertase. II. Location of the endo-beta-N-acetylglucosaminidase H-resistant sequons. J Biol Chem 263: 6986-6992. (Publication) (All modifications)
[384, Glyc]	Yang, F., Zhang, X., Lu, Y., Wang, B., Chen, X., Sun, Z., Li, X. (2020). Inulin catabolism in Saccharomyces cerevisiae is affected by some key glycosylation sequons of invertase Suc2. Biotechnol Lett 42: 471-479. (Publication) (All modifications)
[398, Glyc]	Ziegler, F.D., Maley, F., Trimble, R.B. (1988). Characterization of the glycosylation sites in yeast external invertase. II. Location of the endo-beta-N-acetylglucosaminidase H-resistant sequons. J Biol Chem 263: 6986-6992. (Publication) (All modifications)
[398, Glyc]	Yang, F., Zhang, X., Lu, Y., Wang, B., Chen, X., Sun, Z., Li, X. (2020). Inulin catabolism in Saccharomyces cerevisiae is affected by some key glycosylation sequons of invertase Suc2. Biotechnol Lett 42: 471-479. (Publication) (All modifications)
[466, 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)
[512, Glyc]	Ziegler, F.D., Maley, F., Trimble, R.B. (1988). Characterization of the glycosylation sites in yeast external invertase. II. Location of the endo-beta-N-acetylglucosaminidase H-resistant sequons. J Biol Chem 263: 6986-6992. (Publication) (All modifications)
[512, Glyc]	Yang, F., Zhang, X., Lu, Y., Wang, B., Chen, X., Sun, Z., Li, X. (2020). Inulin catabolism in Saccharomyces cerevisiae is affected by some key glycosylation sequons of invertase Suc2. Biotechnol Lett 42: 471-479. (Publication) (All modifications)