Difference between revisions of "YNL007C"
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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=S000004952 YNL007C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''SIS1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''SIS1 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
|nowrap| Chr XIV:619567..618509 | |nowrap| Chr XIV:619567..618509 | ||
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000004952 | ||
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<br> | <br> | ||
| − | '''Description of | + | '''Description of YNL007C:''' Type II HSP40 co-chaperone that interacts with the HSP70 protein Ssa1p; not functionally redundant with Ydj1p due to due to substrate specificity; shares similarity with bacterial DnaJ proteins<ref name='S000077437'>Fan CY, et al. (2004) Exchangeable chaperone modules contribute to specification of type I and type II Hsp40 cellular function. Mol Biol Cell 15(2):761-73 {{SGDpaper|S000077437}} PMID 14657253</ref><ref name='S000065137'>Lu Z and Cyr DM (1998) Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1. J Biol Chem 273(43):27824-30 |
{{SGDpaper|S000065137}} PMID 9774392</ref> | {{SGDpaper|S000065137}} PMID 9774392</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 07:46, 27 February 2007
Share your knowledge...Edit this entry! <protect>
| Systematic name | YNL007C |
| Gene name | SIS1 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr XIV:619567..618509 |
| Primary SGDID | S000004952 |
Description of YNL007C: Type II HSP40 co-chaperone that interacts with the HSP70 protein Ssa1p; not functionally redundant with Ydj1p due to due to substrate specificity; shares similarity with bacterial DnaJ proteins[1][2]
</protect>
Contents
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References
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- ↑ Fan CY, et al. (2004) Exchangeable chaperone modules contribute to specification of type I and type II Hsp40 cellular function. Mol Biol Cell 15(2):761-73 SGD PMID 14657253
- ↑ Lu Z and Cyr DM (1998) Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1. J Biol Chem 273(43):27824-30 SGD PMID 9774392
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