Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9913-00755
Entry Name
UniProt Accession
Theoretical PI
7.78
Molecular Weight
7850.14
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
Protein Synonyms/Alias
G gamma-I;
Gene Name
GNG2
Gene Synonyms/Alias
Created Date
27-SEP-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
68
Canonical
FREKKFFCAIL****
[1][2]
S-Geranylgeranylation
Organism
Bos taurus (Bovine)
NCBI Taxa ID
9913
Reference
[1] Sanford J, Codina J, Birnbaumer L. Gamma-subunits of G proteins, but not theiralpha- or beta-subunits, are polyisoprenylated. Studies on post-translationalmodifications using in vitro translation with rabbit reticulocyte lysates. J BiolChem. 1991 May 25;266(15):9570-9.[PMID:1903391]
[2] Wilcox MD, Schey KL, Busman M, Hildebrandt JD. Determination of the completecovalent structure of the gamma 2 subunit of bovine brain G proteins by massspectrometry. Biochem Biophys Res Commun. 1995 Jul 17;212(2):367-74.[PMID:7626050]
Functional Description
Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction.
Sequence Annotation
Modified residue: 2 2 N-acetylalanine.
Modified residue: 68 68 Cysteine methyl ester.
Protein Length
71 AA.
Protein Sequence
(Canonical)
MASNNTASIA QARKLVEQLK MEANIDRIKV SKAAADLMAY CEAHAKEDPL LTPVPASENP  60
FREKKFFCAI L                                                       71
FASTA
(Canonical)
>LipidDB-9913-00755|P63212
MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP
FREKKFFCAIL
Gene Ontology
GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl
GO:0005834; C:heterotrimeric G-protein complex; IDA:BHF-UCL
GO:0016020; C:membrane; IDA:BHF-UCL
GO:0031681; F:G-protein beta-subunit binding; ISS:UniProt
GO:0003924; F:GTPase activity; IDA:MGI
GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW
GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IDA:BHF-UCL
GO:0008283; P:cell proliferation; IEA:Ensembl
GO:0071870; P:cellular response to catecholamine stimulus; IDA:BHF-UCL
GO:0071380; P:cellular response to prostaglandin E stimulus; IDA:BHF-UCL
GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:MGI
GO:0006184; P:GTP catabolic process; IDA:GOC
Interpro
InterPro; IPR015898; G-protein_gamma-like_dom
InterPro; IPR001770; Gprotein-gamma
Pfam
Pfam; PF00631; G-gamma;
SMART
SMART; SM00224; GGL;
PROSITE
PROSITE; PS50058; G_PROTEIN_GAMMA;
PRINTS
PRINTS; PR00321; GPROTEING;