Product nameRecombinant Human GGA3 protein
See all GGA3 proteins and peptides
Protein lengthProtein fragment
Amino Acid Sequence
Amino acids246 to 345
Tagsproprietary tag N-Terminus
Our Abpromise guarantee covers the use of ab161554 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Additional notesProtein concentration is above or equal to 0.05 mg/ml.
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Preparation and Storage
Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
Constituents: 0.31% Glutathione, 0.79% Tris HCl
- ADP ribosylation factor binding protein 3
- ADP ribosylation factor binding protein GGA 3
- ADP ribosylation factor binding protein GGA3
FunctionPlays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (AC-LL) motif.
Tissue specificityUbiquitously expressed.
Sequence similaritiesBelongs to the GGA protein family.
Contains 1 GAE domain.
Contains 1 GAT domain.
Contains 1 VHS domain.
DomainThe VHS domain functions as a recognition module for sorting signals composed of an acidic cluster followed by two leucines (AC-LL motif).
The GAT domain is responsible for interaction with ARF-GTP, UBC and RABEP1. Required for recruitment to the TGN it prevents ARF-GTP hydrolysis.
The unstructured hinge region contains clathrin-binding and an autoinhibitory (AC-LL) motifs.
The GAE domain binds accessory proteins regulating GGAs function.
modificationsPhosphorylated by CK2 and dephosphorylated by PP2A (By similarity). Phosphorylation of GGA3 allows the internal AC-LL motif to bind the VHS domain and to inhibit the recognition of cargo signals.
Cellular localizationGolgi apparatus > trans-Golgi network membrane. Endosome membrane.
- Information by UniProt
ab161554 has not yet been referenced specifically in any publications.