DHHC domain: Difference between revisions
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Revision as of 10:35, 23 August 2010
| DHHC domain | |||||||||
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| Identifiers | |||||||||
| Symbol | DHHC | ||||||||
| Pfam | PF01529 | ||||||||
| InterPro | IPR001594 | ||||||||
| PROSITE | PDOC50216 | ||||||||
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In molecular biology the DHHC domain is a protein domain that acts as a palmitoyltransferase enzyme. The DHHC domain was discovered in 1999 and named after a conserved sequence motif found in its protein sequence.[1] Roth and colleagues showed that the yeast Akr1p protein could palmitoylate Yck2p in vitro and inferred that the DHHC domain defined a large family of palmitoyltransferases.[2] In mammals 23 members of this family have been identified and their substrate specificities investigated.[3] Some members of the family such as ZDHHC3 and ZDHHC7 enhance palmitoylation of PSD-95, SNAP25, GAP43, Gαs. Others such as ZDHHC9 showed specificity only toward H-Ras.[3]
References
- ^ Putilina T, Wong P, Gentleman S (1999). "The DHHC domain: a new highly conserved cysteine-rich motif". Mol. Cell. Biochem. 195 (1–2): 219–26. PMID 10395086.
{{cite journal}}: Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link) - ^ Roth AF, Feng Y, Chen L, Davis NG (2002). "The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl transferase". J. Cell Biol. 159 (1): 23–8. doi:10.1083/jcb.200206120. PMC 2173492. PMID 12370247.
{{cite journal}}: Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link) - ^ a b Fukata Y, Iwanaga T, Fukata M (2006). "Systematic screening for palmitoyl transferase activity of the DHHC protein family in mammalian cells". Methods. 40 (2): 177–82. doi:10.1016/j.ymeth.2006.05.015. PMID 17012030.
{{cite journal}}: Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link)