Difference between revisions of "YAL023C"

From SGD-Wiki
Jump to: navigation, search
(Automated import of articles)
(Automated import of articles)
 
(2 intermediate revisions by the same user not shown)
Line 4: Line 4:
 
{|{{Prettytable}} align = 'right' width = '200px'
 
{|{{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 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''PMT2 ''
Line 18: Line 18:
 
|}
 
|}
 
<br>
 
<br>
'''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 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>
 
  {{SGDpaper|S000049666}} PMID 7852348</ref>
 
<br>
 
<br>

Latest revision as of 14:05, 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]




</protect>

Community Commentary

About Community Commentary. Please share your knowledge!




<protect>

References

See Help:References on how to add references

  1. 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
  2. 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
  3. 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
  4. 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
  5. 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

See Help:Categories on how to add the wiki page for this gene to a Category </protect>