Difference between revisions of "YDL181W"
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| − | '''Description of YDL181W:''' Protein that inhibits ATP hydrolysis by the F1F0-ATP synthase; inhibitory function is enhanced by stabilizing proteins Stf1p and Stf2p; has similarity to Stf1p; has a calmodulin-binding motif and binds calmodulin in vitro<ref name=' | + | '''Description of YDL181W:''' Protein that inhibits ATP hydrolysis by the F1F0-ATP synthase; inhibitory function is enhanced by stabilizing proteins Stf1p and Stf2p; has similarity to Stf1p; has a calmodulin-binding motif and binds calmodulin in vitro<ref name='S000071876'>Dienhart M, et al. (2002) Formation of the yeast F1F0-ATP synthase dimeric complex does not require the ATPase inhibitor protein, Inh1. J Biol Chem 277(42):39289-95 {{SGDpaper|S000071876}} PMID 12167646</ref><ref name='S000114019'>Contessi S, et al. (2005) Identification of a conserved calmodulin-binding motif in the sequence of F0F1 ATPsynthase inhibitor protein. J Bioenerg Biomembr 37(5):317-26 |
| − | {{SGDpaper| | + | {{SGDpaper|S000114019}} PMID 16341776</ref> |
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Revision as of 04:15, 19 December 2008
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| Systematic name | YDL181W |
| Gene name | INH1 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr IV:135180..135437 |
| Primary SGDID | S000002340 |
Description of YDL181W: Protein that inhibits ATP hydrolysis by the F1F0-ATP synthase; inhibitory function is enhanced by stabilizing proteins Stf1p and Stf2p; has similarity to Stf1p; has a calmodulin-binding motif and binds calmodulin in vitro[1][2]
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References
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- ↑ Dienhart M, et al. (2002) Formation of the yeast F1F0-ATP synthase dimeric complex does not require the ATPase inhibitor protein, Inh1. J Biol Chem 277(42):39289-95 SGD PMID 12167646
- ↑ Contessi S, et al. (2005) Identification of a conserved calmodulin-binding motif in the sequence of F0F1 ATPsynthase inhibitor protein. J Bioenerg Biomembr 37(5):317-26 SGD PMID 16341776
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