Difference between revisions of "YCR032W"
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl? | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000628 YCR032W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''BPH1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''BPH1 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
|nowrap| Chr III:179516..186019 | |nowrap| Chr III:179516..186019 | ||
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000000628 | ||
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| − | '''Description of | + | '''Description of YCR032W:''' PProtein homologous to human Chediak-Higashi syndrome and murine Beige proteins, which are implicated in disease syndromes due to defective lysosomal trafficking; mutant phenotype and genetic interactions suggest a role in protein sorting<ref name='S000077194'>Shiflett SL, et al. (2004) Bph1p, the Saccharomyces cerevisiae homologue of CHS1/beige, functions in cell wall formation and protein sorting. Traffic 5(9):700-10 {{SGDpaper|S000077194}} PMID 15296494</ref><ref name='S000057863'>Perou CM, et al. (1996) Complementation of the beige mutation in cultured cells by episomally replicating murine yeast artificial chromosomes. Proc Natl Acad Sci U S A 93(12):5905-9 |
{{SGDpaper|S000057863}} PMID 8650191</ref> | {{SGDpaper|S000057863}} PMID 8650191</ref> | ||
<br> | <br> | ||
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J Biol Chem 278(5):3265-74</ref> | J Biol Chem 278(5):3265-74</ref> | ||
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Revision as of 07:45, 27 February 2007
Share your knowledge...Edit this entry! <protect>
| Systematic name | YCR032W |
| Gene name | BPH1 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr III:179516..186019 |
| Primary SGDID | S000000628 |
Description of YCR032W: PProtein homologous to human Chediak-Higashi syndrome and murine Beige proteins, which are implicated in disease syndromes due to defective lysosomal trafficking; mutant phenotype and genetic interactions suggest a role in protein sorting[1][2]
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References
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- ↑ Shiflett SL, et al. (2004) Bph1p, the Saccharomyces cerevisiae homologue of CHS1/beige, functions in cell wall formation and protein sorting. Traffic 5(9):700-10 SGD PMID 15296494
- ↑ Perou CM, et al. (1996) Complementation of the beige mutation in cultured cells by episomally replicating murine yeast artificial chromosomes. Proc Natl Acad Sci U S A 93(12):5905-9 SGD PMID 8650191
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