. Author manuscript; available in PMC: 2008 Aug 30.

Published in final edited form as: Biochemistry. 2007 Jun 9;46(26):7665–7677. doi: 10.1021/bi700338m

Table 1.

Sites of G protein lipid modifications. The N-terminal sequences of several Gα and the C-terminal sequences of two Gγ are shown. Myristate links through an amide bond to an N-terminal glycine after removal of the initiating methionine as indicated by G. Palmitate attaches via a thioester bond to cysteine (in bold italics) residues near the N-terminus of Gα. γ₁ and γ₂ are isoprenylated through a thioether bond to a cysteine, indicated by C. After isoprenylation the C-terminal three amino acids are removed (↓), and the new C-terminus is carboxyl methylated. This is a representative listing of G protein subunits. In humans, 16 genes encode Gα (plus additional splice variants), 5 genes encode Gβ (Gβ proteins are not known to be lipid-modified), and 12 genes encode Gγ.

Gαsubunits	N-termini of αsubunits	Lipid modification
α_i1	MGCTLSAEDKAAVERSKMID-	Myristoylation,Palmitoylation
α_o1	MGCTLSAEERAALERSKAIE-	Myristoylation,Palmitoylation
α_Z	MGCRQSSEEKEAARRSRRID-	Myristoylation,Palmitoylation
α_t	MGAGASAEEKHSREL-	Myristoylation
α_s	MGCLGNSKTEDQRNEEDAQR-	Palmitoylation
α_q	MTLESIMACCLSEEAKEARR-	Palmitoylation
α₁₄	MAGCCCLSAEEKESQRISAE-	Palmitoylation
α₁₆	MARSLRWRCCPWCLTEDEKA-	Palmitoylation
α₁₂	MSGVVRTLSRCLLPAEAGAR-	Palmitoylation
α₁₃	MADFLPSRSVLSVCFPGCVL-	Palmitoylation
Gγsubunits	C-termini of γsubunits	Lipid modification
γ₁	-KGIPEDKNPFKELKGGC^↓VIS	Farnesylation
γ₂	-TPVPASENPFREKKFFC^↓AIL	Geranylgeranylation