Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01450
Entry Name
UniProt Accession
Theoretical PI
9.14
Molecular Weight
8006.22
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12
Protein Synonyms/Alias
Gene Name
GNG12
Gene Synonyms/Alias
Created Date
01-DEC-2000
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
69
Canonical
PFKDKKTCIIL****
[1][2]
S-Geranylgeranylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Morishita R, Nakayama H, Isobe T, Matsuda T, Hashimoto Y, Okano T, Fukada Y,Mizuno K, Ohno S, Kozawa O, et al. Primary structure of a gamma subunit of Gprotein, gamma 12, and its phosphorylation by protein kinase C. J Biol Chem. 1995Dec 8;270(49):29469-75.[PMID:7493986]
[2] Catherman AD, Durbin KR, Ahlf DR, Early BP, Fellers RT, Tran JC, Thomas PM,Kelleher NL. Large-scale top-down proteomics of the human proteome: membraneproteins, mitochondria, and senescence. Mol Cell Proteomics. 2013Dec;12(12):3465-73. doi: 10.1074/mcp.M113.030114. Epub 2013 Sep 10.[PMID:24023390]
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-acetylserine.
Modified residue: 26 26 Phosphoserine.
Modified residue: 69 69 Cysteine methyl ester.
Protein Length
72 AA.
Protein Sequence
(Canonical)
MSSKTASTNN IAQARRTVQQ LRLEASIERI KVSKASADLM SYCEEHARSD PLLIGIPTSE  60
NPFKDKKTCI IL                                                      72
FASTA
(Canonical)
>LipidDB-9606-01450|Q9UBI6
MSSKTASTNNIAQARRTVQQLRLEASIERIKVSKASADLMSYCEEHARSDPLLIGIPTSE
NPFKDKKTCIIL
Gene Ontology
GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB
GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0030165; F:PDZ domain binding; IDA:MGI
GO:0042301; F:phosphate ion binding; IEA:Ensembl
GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW
GO:0071377; P:cellular response to glucagon stimulus; TAS:Reactome
GO:0021987; P:cerebral cortex development; IEA:Ensembl
GO:0006112; P:energy reserve metabolic process; TAS:Reactome
GO:0007186; P:G-protein coupled receptor signaling pathway; IEA:InterPro
GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl
GO:0007165; P:signal transduction; TAS:ProtInc
GO:0044281; P:small molecule metabolic process; TAS:Reactome
GO:0007268; P:synaptic transmission; TAS:Reactome
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;