AGGF1 is largely expressed during early embryonic vein specification, and expression is increased when endothelial cells are activated. While AGGF1 is predominantly functional in endothelial, vascular smooth muscle cells, and osteoblasts, it also has activity in mast cells, cardiac cells, Kupffer cells and hematopoietic stem cells. AGGF1 mRNA has been detected in the heart, kidneys and limbs which indicates that the protein likely also functions in these organs. The proliferation of vascular smooth muscle cells is inhibited when AGGF1 is expressed. It has been found that AGGF1 is highly expressed in some malignant tumours which has implicated AGGF1 in cancer. In vitro models have shown that AGGF1 localizes to cell periphery and directly outside of the cell. Depending on the mutation type, AGGF1 mutations can be lethal in either the heterozygous or homozygous genotype due to its haploinsufficiency. Mice models have shown that heterozygous mutations can cause fatality due to hemorrhaging while homozygous mutations can prevent proper stem cell differentiation. Aggf1 is not unique to humans. This gene is conserved across many species, such as chimpanzees, Rhesus monkeys, dogs, cows, mice, rats, chickens, and frogs. There are 212 organisms that have genes which are orthologs to AGGF1. Within the human chromosome, there are pseudogenes related to AGGF1 are located on chromosomes 3, 4, 10 and 16 that have likely arisen due to translocation events. AGGF1 functions to regulate angiogenesis and vascular development. Gene ontology has also implicated AGGF1 in cell adhesion, positive regulation of angiogenesis and endothelial cell proliferation. Additionally, AGGF1 has been shown to protect against inflammation and ischemic injuries. During embryongenesis, AGGF1 is required for hematopoietic stem cell specification and the differentiation of hematopoietic and endothelial cell lineages. Specifically, it regulates vascular endothelial cadherin (VE-cadherin) by inhibiting the phosphorylation of the cadherin and increasing its presence in the plasma membrane of endothelial cells. AGGF1 is critical to the specification of veins and multipotent hemanigioblasts, anti-inflammation, tumour angiogenesis, and inhibition of vascular permeability. Additionally, it activates autophagy in specific cell types, such as endothelial cells, cardiac HL1 and H9C2 cells, and vascular smooth muscle cells.