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The splicing mutation was found to decrease GPAA1 mRNA.
the lumenal domain of GAA1/GPAA1 has a 3D structure similar to that of an M28-type aminopeptidase. GAA1/GPAA1 is a candidate for the enzyme that catalyzes the peptide bond formation between the omega-site and a phosphoethanolamine group of GPI lipid anchor.
a conserved proline in the last transmembrane segment of Gaa1 is required for glycosylphosphatidylinositol recognition by GPI transamidase
passively retained in the ER by a signalless mechanism
Increased expression of glycosyl-phosphatidylinositol anchor attachment protein 1 is associated with gene amplification in hepatocellular carcinoma
Results show an increased expression level and elevated copy number for GAA1 in head and neck squamous carcinoma, suggesting a role for this GPI anchor subunit in HNSCC.
Posttranslational glycosylphosphatidylinositol (GPI) anchor attachment serves as a general mechanism for linking proteins to the cell surface membrane. The protein encoded by this gene presumably functions in GPI anchoring at the GPI transfer step. The mRNA transcript is ubiquitously expressed in both fetal and adult tissues. The anchor attachment protein 1 contains an N-terminal signal sequence, 1 cAMP- and cGMP-dependent protein kinase phosphorylation site, 1 leucine zipper pattern, 2 potential N-glycosylation sites, and 8 putative transmembrane domains.
GAA1 protein homolog
, GPAA1P anchor attachment protein 1 homolog
, GPI anchor attachment protein 1
, GPI transamidase subunit
, anchor attachment protein 1 (Gaa1p, yeast) homolog
, glycophosphatidylinositol anchor attachment 1
, glycosylphosphatidylinositol anchor attachment 1 protein
, glycosylphosphatidylinositol anchor attachment protein 1 homolog
, anchor attachment protein 1
, glycosylphosphatidylinositol anchor attachment 1 (GPAA1)