Q9UBI6 · GBG12_HUMAN
- ProteinGuanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12
- GeneGNG12
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular exosome | |
Cellular Component | heterotrimeric G-protein complex | |
Cellular Component | plasma membrane | |
Molecular Function | G-protein beta-subunit binding | |
Molecular Function | PDZ domain binding | |
Biological Process | G protein-coupled receptor signaling pathway | |
Biological Process | signal transduction |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGuanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9UBI6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 59 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, modified residue (large scale data), chain, lipidation, propeptide.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Chain | PRO_0000012667 | 2-69 | UniProt | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12 | |||
Sequence: SSKTASTNNIAQARRTVQQLRLEASIERIKVSKASADLMSYCEEHARSDPLLIGIPTSENPFKDKKTC | |||||||
Modified residue (large scale data) | 3 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 5 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 7 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 26 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 26 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 41 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 42 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 49 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 49 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 59 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 69 | UniProt | Cysteine methyl ester | ||||
Sequence: C | |||||||
Lipidation | 69 | UniProt | S-geranylgeranyl cysteine | ||||
Sequence: C | |||||||
Propeptide | PRO_0000012668 | 70-72 | UniProt | Removed in mature form | |||
Sequence: IIL |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
G proteins are composed of 3 units, alpha, beta and gamma.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9UBI6 | FHL2 Q14192 | 11 | EBI-358636, EBI-701903 | |
BINARY | Q9UBI6 | HDAC7 Q8WUI4-6 | 3 | EBI-358636, EBI-12094670 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length72
- Mass (Da)8,006
- Last updated2007-01-23 v3
- ChecksumA4C489A61697FAA9
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 29 | in Ref. 9; AAH05940 | ||||
Sequence: R → G |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF188181 EMBL· GenBank· DDBJ | AAF04571.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF123766 EMBL· GenBank· DDBJ | AAP97245.1 EMBL· GenBank· DDBJ | mRNA | ||
AF119663 EMBL· GenBank· DDBJ | AAF17220.1 EMBL· GenBank· DDBJ | mRNA | ||
AF365871 EMBL· GenBank· DDBJ | AAK53385.1 EMBL· GenBank· DDBJ | mRNA | ||
AF493879 EMBL· GenBank· DDBJ | AAM12593.1 EMBL· GenBank· DDBJ | mRNA | ||
AK293101 EMBL· GenBank· DDBJ | BAF85790.1 EMBL· GenBank· DDBJ | mRNA | ||
AL832431 EMBL· GenBank· DDBJ | CAH10645.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471059 EMBL· GenBank· DDBJ | EAX06484.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471059 EMBL· GenBank· DDBJ | EAX06485.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471059 EMBL· GenBank· DDBJ | EAX06486.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC005940 EMBL· GenBank· DDBJ | AAH05940.1 EMBL· GenBank· DDBJ | mRNA |