P38138

Name	Glucosidase 2 subunit alpha (EC 3.2.1.207) (Alpha-glucosidase II subunit alpha) (Glucosidase II subunit alpha) (Reversal of TOR2 lethality protein 2)
Uniprot ID	P38138
Systematic gene name	YBR229C
Standard gene name	ROT2
Gene names	ROT2 GLS2 YBR229C YBR1526
Description from SGD	YBR229C ROT2 SGDID:S000000433, Chr II from 679221-676357, Genome Release 64-3-1, reverse complement, Verified ORF, "Glucosidase II catalytic subunit; required to trim the final glucose in N-linked glycans; required for normal cell wall synthesis; mutations in rot2 suppress tor2 mutations, and are synthetically lethal with rot1 mutations"
Protein length	954
Download	sequence (fasta, from Uniprot), modifications (csv format)
Database links	Uniprot, SGD, TheCellVision.org, FungiDB

MVLLKWLVCQ LVFFTAFSHA FTDYLLKKCA QSGFCHRNRV YAENIAKSHH
CYYKVDAESI AHDPLENVLH ATIIKTIPRL EGDDIAVQFP FSLSFLQDHS
VRFTINEKER MPTNSSGLLI SSQRFNETWK YAFDKKFQEE ANRTSIPQFH
FLKQKQTVNS FWSKISSFLS LSNSTADTFH LRNGDVSVEI FAEPFQLKVY
WQNALKLIVN EQNFLNIEHH RTKQENFAHV LPEETTFNMF KDNFLYSKHD
SMPLGPESVA LDFSFMGSTN VYGIPEHATS LRLMDTSGGK EPYRLFNVDV
FEYNIGTSQP MYGSIPFMFS SSSTSIFWVN AADTWVDIKY DTSKNKTMTH
WISENGVIDV VMSLGPDIPT IIDKFTDLTG RPFLPPISSI GYHQCRWNYN
DEMDVLTVDS QMDAHMIPYD FIWLDLEYTN DKKYFTWKQH SFPNPKRLLS
KLKKLGRNLV VLIDPHLKKD YEISDRVINE NVAVKDHNGN DYVGHCWPGN
SIWIDTISKY GQKIWKSFFE RFMDLPADLT NLFIWNDMNE PSIFDGPETT
APKDLIHDNY IEERSVHNIY GLSVHEATYD AIKSIYSPSD KRPFLLTRAF
FAGSQRTAAT WTGDNVANWD YLKISIPMVL SNNIAGMPFI GADIAGFAED
PTPELIARWY QAGLWYPFFR AHAHIDTKRR EPYLFNEPLK SIVRDIIQLR
YFLLPTLYTM FHKSSVTGFP IMNPMFIEHP EFAELYHIDN QFYWSNSGLL
VKPVTEPGQS ETEMVFPPGI FYEFASLHSF INNGTDLIEK NISAPLDKIP
LFIEGGHIIT MKDKYRRSSM LMKNDPYVIV IAPDTEGRAV GDLYVDDGET
FGYQRGEYVE TQFIFENNTL KNVRSHIPEN LTGIHHNTLR NTNIEKIIIA
KNNLQHNITL KDSIKVKKNG EESSLPTRSS YENDNKITIL NLSLDITEDW
EVIF

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[114, 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)
[783, 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)
[791, 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)
[793, 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)
[867, 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)
[880, 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)
[907, 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)