YAL023C - Revision history

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-'''Description of YAL023C:''' Protein O-mannosyltransferase; transfers mannose residues from dolichyl phosphate-D-mannose to protein Ser/Thr residues; involved in ER quality control; acts in a complex with Pmt1p, can instead interact with Pmt5; antifungal drug target; PMT2 has a paralog, PMT3, that arose from the whole genome duplication<ref name='S000113653'>Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61 {{SGDpaper|S000113653}} PMID 16169922</ref><ref name='S000072926'>Girrbach V and Strahl S (2003) Members of the evolutionarily conserved PMT family of protein O-mannosyltransferases form distinct protein complexes among themselves. J Biol Chem 278(14):12554-62 {{SGDpaper|S000072926}} PMID 12551906</ref><ref name='S000142426'>Goder V and Melero A (2011) Protein O-mannosyltransferases participate in ER protein quality control. J Cell Sci 124(Pt 1):144-53 {{SGDpaper|S000142426}} PMID 21147851</ref><ref name='S000049666'>Lussier M, et al. (1995) Protein O-glycosylation in yeast. The PMT2 gene specifies a second protein O-mannosyltransferase that functions in addition to the PMT1-encoded activity. J Biol Chem 270(6):2770-5
+'''Description of YAL023C:''' Protein O-mannosyltransferase of the ER membrane; transfers mannose residues from dolichyl phosphate-D-mannose to protein serine/threonine residues; involved in ER quality control; acts in a complex with Pmt1p, can instead interact with Pmt5p; antifungal drug target; PMT2 has a paralog, PMT3, that arose from the whole genome duplication<ref name='S000113653'>Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61 {{SGDpaper|S000113653}} PMID 16169922</ref><ref name='S000055278'>Gentzsch M, et al. (1995) Protein O-glycosylation in Saccharomyces cerevisiae: the protein O-mannosyltransferases Pmt1p and Pmt2p function as heterodimer. FEBS Lett 377(2):128-30 {{SGDpaper|S000055278}} PMID 8543034</ref><ref name='S000072926'>Girrbach V and Strahl S (2003) Members of the evolutionarily conserved PMT family of protein O-mannosyltransferases form distinct protein complexes among themselves. J Biol Chem 278(14):12554-62 {{SGDpaper|S000072926}} PMID 12551906</ref><ref name='S000142426'>Goder V and Melero A (2011) Protein O-mannosyltransferases participate in ER protein quality control. J Cell Sci 124(Pt 1):144-53 {{SGDpaper|S000142426}} PMID 21147851</ref><ref name='S000049666'>Lussier M, et al. (1995) Protein O-glycosylation in yeast. The PMT2 gene specifies a second protein O-mannosyltransferase that functions in addition to the PMT1-encoded activity. J Biol Chem 270(6):2770-5
   {{SGDpaper|S000049666}} PMID 7852348</ref>
 <br>

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-'''Description of YAL023C:''' Protein O-mannosyltransferase, transfers mannose residues from dolichyl phosphate-D-mannose to protein Ser/Thr residues; involved in ER quality control; acts in a complex with Pmt1p, can instead interact with Pmt5; target for new antifungal<ref name='S000072926'>Girrbach V and Strahl S (2003) Members of the evolutionarily conserved PMT family of protein O-mannosyltransferases form distinct protein complexes among themselves. J Biol Chem 278(14):12554-62 {{SGDpaper|S000072926}} PMID 12551906</ref><ref name='S000142426'>Goder V and Melero A (2011) Protein O-mannosyltransferases participate in ER protein quality control. J Cell Sci 124(Pt 1):144-53 {{SGDpaper|S000142426}} PMID 21147851</ref><ref name='S000049666'>Lussier M, et al. (1995) Protein O-glycosylation in yeast. The PMT2 gene specifies a second protein O-mannosyltransferase that functions in addition to the PMT1-encoded activity. J Biol Chem 270(6):2770-5
+'''Description of YAL023C:''' Protein O-mannosyltransferase; transfers mannose residues from dolichyl phosphate-D-mannose to protein Ser/Thr residues; involved in ER quality control; acts in a complex with Pmt1p, can instead interact with Pmt5; antifungal drug target; PMT2 has a paralog, PMT3, that arose from the whole genome duplication<ref name='S000113653'>Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61 {{SGDpaper|S000113653}} PMID 16169922</ref><ref name='S000072926'>Girrbach V and Strahl S (2003) Members of the evolutionarily conserved PMT family of protein O-mannosyltransferases form distinct protein complexes among themselves. J Biol Chem 278(14):12554-62 {{SGDpaper|S000072926}} PMID 12551906</ref><ref name='S000142426'>Goder V and Melero A (2011) Protein O-mannosyltransferases participate in ER protein quality control. J Cell Sci 124(Pt 1):144-53 {{SGDpaper|S000142426}} PMID 21147851</ref><ref name='S000049666'>Lussier M, et al. (1995) Protein O-glycosylation in yeast. The PMT2 gene specifies a second protein O-mannosyltransferase that functions in addition to the PMT1-encoded activity. J Biol Chem 270(6):2770-5
   {{SGDpaper|S000049666}} PMID 7852348</ref>
 <br>

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 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000021 YAL023C]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000021 YAL023C]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''PMT2 ''

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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr I:108552..106273
+|nowrap| Chr I:108551..106272
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000000021

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YAL023C:''' Protein O-mannosyltransferase, transfers mannose residues from dolichyl phosphate-D-mannose to protein serine/threonine residues; acts in a complex with Pmt1p, can instead interact with Pmt5p in some conditions; target for new antifungals<ref name='S000072926'>Girrbach V and Strahl S (2003) Members of the evolutionarily conserved PMT family of protein O-mannosyltransferases form distinct protein complexes among themselves. J Biol Chem 278(14):12554-62 {{SGDpaper|S000072926}} PMID 12551906</ref><ref name='S000049666'>Lussier M, et al. (1995) Protein O-glycosylation in yeast. The PMT2 gene specifies a second protein O-mannosyltransferase that functions in addition to the PMT1-encoded activity. J Biol Chem 270(6):2770-5
+'''Description of YAL023C:''' Protein O-mannosyltransferase, transfers mannose residues from dolichyl phosphate-D-mannose to protein Ser/Thr residues; involved in ER quality control; acts in a complex with Pmt1p, can instead interact with Pmt5; target for new antifungal<ref name='S000072926'>Girrbach V and Strahl S (2003) Members of the evolutionarily conserved PMT family of protein O-mannosyltransferases form distinct protein complexes among themselves. J Biol Chem 278(14):12554-62 {{SGDpaper|S000072926}} PMID 12551906</ref><ref name='S000142426'>Goder V and Melero A (2011) Protein O-mannosyltransferases participate in ER protein quality control. J Cell Sci 124(Pt 1):144-53 {{SGDpaper|S000142426}} PMID 21147851</ref><ref name='S000049666'>Lussier M, et al. (1995) Protein O-glycosylation in yeast. The PMT2 gene specifies a second protein O-mannosyltransferase that functions in addition to the PMT1-encoded activity. J Biol Chem 270(6):2770-5
   {{SGDpaper|S000049666}} PMID 7852348</ref>
 <br>