Literature summary for 3.1.3.11 extracted from

Pirog, M.; Gizak, A.; Rakus, D.
Changes in quaternary structure of muscle fructose-1,6-bisphosphatase regulate affinity of the enzyme to mitochondria (2014), Int. J. Biochem. Cell Biol., 48, 55-59.

Search for more literature for 3.1.3.11

Cloned(Commentary)

Cloned (Comment)	Organism
expression in HL-1 cardiomyocyte	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	deletion of first 7 N-terminal amino acids of isoform FBP2 markedly impairs colocalization of the enzyme with mitochondria in the presence of GSK3 inhibitor. Deletion of the next 3 residues further enhanced this effect	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O00757	isoform FBP2	-

Synonyms

Synonyms	Comment	Organism
FBP2	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	the quaternary structure of isoform FBP2 plays a crucial role in the binding binds to mitochondria where it interacts with proteins involved in regulation of energy homeostasis interaction. The AMP-driven transition of the FBP2 subunit arrangement from active to inactive precludes its association with the mitochondria. Truncation of the evolutionarily conserved N-terminal residues of FBP2 results in a loss of its mitochondria-protective functions	Homo sapiens

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Release 2023.1 (January 2023)