P22146

Name	1,3-beta-glucanosyltransferase GAS1 (EC 2.4.1.-) (Glycolipid-anchored surface protein 1) (Glycoprotein GP115)
Uniprot ID	P22146
Systematic gene name	YMR307W
Standard gene name	GAS1
Gene names	GAS1 GGP1 YMR307W YM9952.09
Description from SGD	YMR307W GAS1 SGDID:S000004924, Chr XIII from 887003-888682, Genome Release 64-3-1, Verified ORF, "Beta-1,3-glucanosyltransferase; required for cell wall assembly and also has a role in transcriptional silencing; localizes to cell surface via a glycosylphosphatidylinositol (GPI) anchor; also found at nuclear periphery; genetic interactions with histone H3 lysine acetyltransferases GCN5 and SAS3 indicate previously unsuspected functions for Gas1 in DNA damage response and cell cycle regulation"
Protein length	559
Download	sequence (fasta, from Uniprot), modifications (csv format)
Database links	Uniprot, SGD, TheCellVision.org, FungiDB

MLFKSLSKLA TAAAFFAGVA TADDVPAIEV VGNKFFYSNN GSQFYIRGVA
YQADTANETS GSTVNDPLAN YESCSRDIPY LKKLNTNVIR VYAINTTLDH
SECMKALNDA DIYVIADLAA PATSINRDDP TWTVDLFNSY KTVVDTFANY
TNVLGFFAGN EVTNNYTNTD ASAFVKAAIR DVRQYISDKN YRKIPVGYSS
NDDEDTRVKM TDYFACGDDD VKADFYGINM YEWCGKSDFK TSGYADRTAE
FKNLSIPVFF SEYGCNEVTP RLFTEVEALY GSNMTDVWSG GIVYMYFEET
NKYGLVSIDG NDVKTLDDFN NYSSEINKIS PTSANTKSYS ATTSDVACPA
TGKYWSAATE LPPTPNGGLC SCMNAANSCV VSDDVDSDDY ETLFNWICNE
VDCSGISANG TAGKYGAYSF CTPKEQLSFV MNLYYEKSGG SKSDCSFSGS
ATLQTATTQA SCSSALKEIG SMGTNSASGS VDLGSGTESS TASSNASGSS
SKSNSGSSGS SSSSSSSSAS SSSSSKKNAA TNVKANLAQV VFTSIISLSI
AAGVGFALV

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[40, Glyc]	Poljak, K.,  Selevsek, N.,  Ngwa, E.,  Grossmann, J.,  Losfeld, M.E.,  Aebi, M. (2018). Quantitative Profiling of N-linked Glycosylation Machinery in Yeast Saccharomyces cerevisiae. Mol Cell Proteomics 17: 18-30. (Publication) (All modifications)
[40, 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)
[40, Glyc]	Yeo, K.Y.B., Chrysanthopoulos, P.K., Nouwens, A.S., Marcellin, E., Schulz, B.L. (2016). High-performance targeted mass spectrometry with precision data-independent acquisition reveals site-specific glycosylation macroheterogeneity. Anal Biochem 510: 106-113. (Publication) (All modifications)
[57, 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)
[57, Glyc]	Yeo, K.Y.B., Chrysanthopoulos, P.K., Nouwens, A.S., Marcellin, E., Schulz, B.L. (2016). High-performance targeted mass spectrometry with precision data-independent acquisition reveals site-specific glycosylation macroheterogeneity. Anal Biochem 510: 106-113. (Publication) (All modifications)
[85, 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)
[86, Phos]	Guo X, Niemi NM, Coon JJ, Pagliarini DJ (2017a) Integrative proteomics and biochemical analyses define Ptc6p as the Saccharomyces cerevisiae pyruvate dehydrogenase phosphatase. J Biol Chem 292:11751–11759. (Publication) (All modifications)
[86, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[95, 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)
[95, Glyc]	Yeo, K.Y.B., Chrysanthopoulos, P.K., Nouwens, A.S., Marcellin, E., Schulz, B.L. (2016). High-performance targeted mass spectrometry with precision data-independent acquisition reveals site-specific glycosylation macroheterogeneity. Anal Biochem 510: 106-113. (Publication) (All modifications)
[149, 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)
[149, Glyc]	Yeo, K.Y.B., Chrysanthopoulos, P.K., Nouwens, A.S., Marcellin, E., Schulz, B.L. (2016). High-performance targeted mass spectrometry with precision data-independent acquisition reveals site-specific glycosylation macroheterogeneity. Anal Biochem 510: 106-113. (Publication) (All modifications)
[165, Glyc]	Yeo, K.Y.B., Chrysanthopoulos, P.K., Nouwens, A.S., Marcellin, E., Schulz, B.L. (2016). High-performance targeted mass spectrometry with precision data-independent acquisition reveals site-specific glycosylation macroheterogeneity. Anal Biochem 510: 106-113. (Publication) (All modifications)
[189, K-acetyl]	Henriksen, P., Wagner, S. A., Weinert, B. T., et al. (2012). Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & Cellular Proteomics, 11(11), 1510-1522. (Publication) (All modifications)
[193, 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)
[200, 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)
[200, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[211, 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)
[240, K-succ]	Weinert, B.T., Schölz, C., Wagner, S.A., et al. (2013). Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. Cell Reports, 4(4), 842-851. (Publication) (All modifications)
[240, K-acetyl]	Henriksen, P., Wagner, S. A., Weinert, B. T., et al. (2012). Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & Cellular Proteomics, 11(11), 1510-1522. (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)
[242, 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)
[242, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[253, 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)
[253, Glyc]	Yeo, K.Y.B., Chrysanthopoulos, P.K., Nouwens, A.S., Marcellin, E., Schulz, B.L. (2016). High-performance targeted mass spectrometry with precision data-independent acquisition reveals site-specific glycosylation macroheterogeneity. Anal Biochem 510: 106-113. (Publication) (All modifications)
[337, 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)
[409, 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)
[415, Phos]	Rekstina, V.V., Bykova, A.A., Ziganshin, R.H., Kalebina, T.S. (2019). GPI-Modified Proteins Non-covalently Attached to Saccharomyces cerevisiae Yeast Cell Wall. Biochemistry (Mosc) 84: 1513-1520 (Publication) (All modifications)
[419, 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)
[422, 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)
[478, 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)
[478, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[503, 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)
[503, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[505, 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)
[505, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[507, 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)
[507, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[508, 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)
[508, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[514, 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)
[514, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[516, 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)
[516, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[517, 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)
[517, Phos]	Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)