Difference between revisions of "YAL023C"
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000021 YAL023C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''PMT2 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''PMT2 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr I: | + | |nowrap| Chr I:108551..106272 |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000000021 | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000000021 | ||
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| − | '''Description of YAL023C:''' Protein O-mannosyltransferase | + | '''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| | + | {{SGDpaper|S000049666}} PMID 7852348</ref> |
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Latest revision as of 13:05, 24 August 2012
Share your knowledge...Edit this entry! <protect>
| Systematic name | YAL023C |
| Gene name | PMT2 |
| Aliases | FUN25 |
| Feature type | ORF, Verified |
| Coordinates | Chr I:108551..106272 |
| Primary SGDID | S000000021 |
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[1][2][3][4][5]
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References
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- ↑ 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 SGD PMID 16169922
- ↑ 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 SGD PMID 8543034
- ↑ 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 SGD PMID 12551906
- ↑ Goder V and Melero A (2011) Protein O-mannosyltransferases participate in ER protein quality control. J Cell Sci 124(Pt 1):144-53 SGD PMID 21147851
- ↑ 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 SGD PMID 7852348
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