Skip to main content
. Author manuscript; available in PMC: 2018 May 5.
Published in final edited form as: Subcell Biochem. 2012;63:193–223. doi: 10.1007/978-94-007-4765-4_11

Table 11.1.

Sites of G protein lipid modifications

Gα subunits N-termini of α subunits Lipid modification
αi1 MGCTLSAEDKAAVERSKMID- Myristoylation, Palmitoylation
αo1 MGCTLSAEERAALERSKAIE- Myristoylation, Palmitoylation
αZ MGCRQSSEEKEAARRSRRID- Myristoylation, Palmitoylation
αt MGAGASAEEKHSREL- Myristoylation
αs MGCLGNSKTEDQRNEEDAQR- Palmitoylation
αq MTLESIMACCLSEEAKEARR- Palmitoylation
α14 MAGCCCLSAEEKESQRISAE- Palmitoylation
α16 MARSLRWRCCPWCLTEDEKA- Palmitoylation
α12 MSGVVRTLSRCLLPAEAGAR- Palmitoylation
α13 MADFLPSRSVLSVCFPGCVL- Palmitoylation

Gγ subunits C-termini of γ subunits Lipid modification

γ1 -KGIPEDKNPFKELKGGC VIS Farnesylation
γ2 -TPVPASENPFREKKFFC AIL Geranylgeranylation

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. Reprinted with permission from Marrari et al. (2007). Copyright 2007 American Chemical Society