P68253 · 1433G_SHEEP
- Protein14-3-3 protein gamma
- GeneYWHAG
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids158 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Promotes inactivation of WDR24 component of the GATOR2 complex by binding to phosphorylated WDR24. Participates in the positive regulation of NMDA glutamate receptor activity by promoting the L-glutamate secretion through interaction with BEST1.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 34 | Interaction with phosphoserine on interacting protein | ||||
Sequence: R | ||||||
Site | 59 | Interaction with phosphoserine on interacting protein | ||||
Sequence: R |
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 | cytoplasm | |
Molecular Function | insulin-like growth factor receptor binding | |
Molecular Function | phosphorylation-dependent protein binding | |
Molecular Function | protein kinase C binding | |
Molecular Function | protein sequestering activity | |
Biological Process | positive regulation of cell-cell adhesion | |
Biological Process | regulation of neuron differentiation | |
Biological Process | regulation of protein localization | |
Biological Process | regulation of synaptic plasticity | |
Biological Process | signal transduction |
Names & Taxonomy
Protein names
- Recommended name14-3-3 protein gamma
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Caprinae > Ovis
Accessions
- Primary accessionP68253
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000058610 | 1-158 | 14-3-3 protein gamma | |||
Sequence: AAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTSFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALNYSVFYYEITAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDDDGG | ||||||
Modified residue | 48 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 60 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 72 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 130 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 149 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 150 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated by various PKC isozymes.
Keywords
- PTM
Interaction
Subunit
Homodimer (By similarity).
Interacts with SAMSN1 (By similarity).
Interacts with RAF1, SSH1 and CRTC2/TORC2 (By similarity).
Interacts with ABL1 (phosphorylated form); the interaction retains it in the cytoplasm (By similarity).
Interacts with GAB2 (By similarity).
Interacts with MDM4 (phosphorylated); negatively regulates MDM4 activity toward TP53 (By similarity).
Interacts with PKA-phosphorylated AANAT and SIRT2 (PubMed:11427721).
Interacts with the 'Thr-369' phosphorylated form of DAPK2 (By similarity).
Interacts with PI4KB, TBC1D22A and TBC1D22B (By similarity).
Interacts with SLITRK1 (By similarity).
Interacts with LRRK2; this interaction is dependent on LRRK2 phosphorylation (By similarity).
Interacts with MARK2 and MARK3 (By similarity).
Interacts with MEFV (By similarity).
Interacts with ENDOG, TSC2 and PIK3C3; interaction with ENDOG weakens its interaction with TSC2 and PIK3C3 (By similarity).
Interacts with (phosphorylated) WDR24 (By similarity).
Interacts with BEST1; this interaction promotes L-glutamate channel activity leading to the positive regulation of NMDA glutamate receptor activity through the L-glutamate secretion (By similarity).
Interacts with SAMSN1 (By similarity).
Interacts with RAF1, SSH1 and CRTC2/TORC2 (By similarity).
Interacts with ABL1 (phosphorylated form); the interaction retains it in the cytoplasm (By similarity).
Interacts with GAB2 (By similarity).
Interacts with MDM4 (phosphorylated); negatively regulates MDM4 activity toward TP53 (By similarity).
Interacts with PKA-phosphorylated AANAT and SIRT2 (PubMed:11427721).
Interacts with the 'Thr-369' phosphorylated form of DAPK2 (By similarity).
Interacts with PI4KB, TBC1D22A and TBC1D22B (By similarity).
Interacts with SLITRK1 (By similarity).
Interacts with LRRK2; this interaction is dependent on LRRK2 phosphorylation (By similarity).
Interacts with MARK2 and MARK3 (By similarity).
Interacts with MEFV (By similarity).
Interacts with ENDOG, TSC2 and PIK3C3; interaction with ENDOG weakens its interaction with TSC2 and PIK3C3 (By similarity).
Interacts with (phosphorylated) WDR24 (By similarity).
Interacts with BEST1; this interaction promotes L-glutamate channel activity leading to the positive regulation of NMDA glutamate receptor activity through the L-glutamate secretion (By similarity).
Structure
Sequence
- Sequence statusFragments
- Length158
- Mass (Da)18,000
- Last updated2004-10-25 v1
- Checksum69EC73EBA23B7B6F
Features
Showing features for non-terminal residue, non-adjacent residues.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: A | ||||||
Non-adjacent residues | 48-49 | |||||
Sequence: SF | ||||||
Non-adjacent residues | 113-114 | |||||
Sequence: IT | ||||||
Non-terminal residue | 158 | |||||
Sequence: G |
Keywords
- Technical term