P33775

Name	Dolichyl-phosphate-mannose--protein mannosyltransferase 1 (EC 2.4.1.109)
Uniprot ID	P33775
Systematic gene name	YDL095W
Standard gene name	PMT1
Gene names	PMT1 YDL095W D2390
Description from SGD	YDL095W PMT1 SGDID:S000002253, Chr IV from 287059-289512, Genome Release 64-3-1, Verified ORF, "Protein O-mannosyltransferase of the ER membrane; transfers mannose from dolichyl phosphate-D-mannose to protein serine and threonine residues; 1 of 7 related proteins involved in O-glycosylation which is essential for cell wall rigidity; functions as a heterodimer with Pmt2p but can also pair with Pmt3p; involved in ER quality control; amino terminus faces cytoplasm, carboxyl terminus faces ER lumen"
Protein length	817
Download	sequence (fasta, from Uniprot), modifications (csv format)
Database links	Uniprot, SGD, TheCellVision.org, FungiDB

MSEEKTYKRV EQDDPVPELD IKQGPVRPFI VTDPSAELAS LRTMVTLKEK
LLVACLAVFT AVIRLHGLAW PDSVVFDEVH FGGFASQYIR GTYFMDVHPP
LAKMLYAGVA SLGGFQGDFD FENIGDSFPS TTPYVLMRFF SASLGALTVI
LMYMTLRYSG VRMWVALMSA ICFAVENSYV TISRYILLDA PLMFFIAAAV
YSFKKYEMYP ANSLNAYKSL LATGIALGMA SSSKWVGLFT VTWVGLLCIW
RLWFMIGDLT KSSKSIFKVA FAKLAFLLGV PFALYLVFFY IHFQSLTLDG
DGASFFSPEF RSTLKNNKIP QNVVADVGIG SIISLRHLST MGGYLHSHSH
NYPAGSEQQQ STLYPHMDAN NDWLLELYNA PGESLTTFQN LTDGTKVRLF
HTVTRCRLHS HDHKPPVSES SDWQKEVSCY GYSGFDGDAN DDWVVEIDKK
NSAPGVAQER VIALDTKFRL RHAMTGCYLF SHEVKLPAWG FEQQEVTCAS
SGRHDLTLWY VENNSNPLLP EDTKRISYKP ASFISKFIES HKKMWHINKN
LVEPHVYESQ PTSWPFLLRG ISYWGENNRN VYLLGNAIVW WAVTAFIGIF
GLIVITELFS WQLGKPILKD SKVVNFHVQV IHYLLGFAVH YAPSFLMQRQ
MFLHHYLPAY YFGILALGHA LDIIVSYVFR SKRQMGYAVV ITFLAASVYF
FKSFSPIIYG TPWTQELCQK SQWLSGWDYN CNTYFSSLEE YKNQTLTKRE
SQPAATSTVE EITIEGDGPS YEDLMNEDGK KIFKDTEGNE LDPEVVKKML
EEEGANILKV EKRAVLE

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[390, Glyc]	Zatorska, E.,  Gal, L.,  Schmitt, J.,  Bausewein, D.,  Schuldiner, M.,  Strahl, S. (2017). Cellular Consequences of Diminished Protein O-Mannosyltransferase Activity in Baker's Yeast. Int J Mol Sci 18: 1226. (Publication) (All modifications)
[414, 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)
[467, 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)
[513, Glyc]	Zatorska, E.,  Gal, L.,  Schmitt, J.,  Bausewein, D.,  Schuldiner, M.,  Strahl, S. (2017). Cellular Consequences of Diminished Protein O-Mannosyltransferase Activity in Baker's Yeast. Int J Mol Sci 18: 1226. (Publication) (All modifications)
[513, 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)
[536, 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)
[743, Glyc]	Zatorska, E.,  Gal, L.,  Schmitt, J.,  Bausewein, D.,  Schuldiner, M.,  Strahl, S. (2017). Cellular Consequences of Diminished Protein O-Mannosyltransferase Activity in Baker's Yeast. Int J Mol Sci 18: 1226. (Publication) (All modifications)
[743, 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)