Fructose-bisphosphatase 2

FBP2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3IFA, 3IFC, 4HE0, 4HE1, 4HE2, 5ET7, 5ET5, 5ET6
Identifiers
Aliases	FBP2, fructose-bisphosphatase 2, CORLK
External IDs	OMIM: 603027 MGI: 95491 HomoloGene: 55784 GeneCards: FBP2
Gene location (Human) Chr. Chromosome 9 (human) Band 9q22.32 Start 94,558,720 bp End 94,593,824 bp
Gene location (Mouse) Chr. Chromosome 13 (mouse) Band 13|13 B3 Start 62,984,691 bp End 63,006,236 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in biceps brachii vastus lateralis muscle triceps brachii muscle gastrocnemius muscle thoracic diaphragm body of tongue deltoid muscle body of stomach secondary oocyte fundus Top expressed in ileum duodenum jejunum morula blastocyst intestinal epithelium intestinal villus Paneth cell left colon crypt of lieberkuhn of small intestine More reference expression data BioGPS n/a
Gene ontology Molecular function phosphoric ester hydrolase activity catalytic activity hydrolase activity protein binding metal ion binding phosphatase activity fructose 1,6-bisphosphate 1-phosphatase activity identical protein binding Cellular component cytoplasm cell junction Z disc extracellular exosome nucleus nucleoplasm cytosol plasma membrane Biological process fructose metabolic process metabolism dephosphorylation sucrose biosynthetic process fructose 6-phosphate metabolic process gluconeogenesis fructose 1,6-bisphosphate metabolic process carbohydrate metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8789 14120 Ensembl ENSG00000130957 ENSMUSG00000021456 UniProt O00757 P70695 RefSeq (mRNA) NM_003837 NM_007994 RefSeq (protein) NP_003828 NP_032020 Location (UCSC) Chr 9: 94.56 – 94.59 Mb Chr 13: 62.98 – 63.01 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Fructose-bisphosphatase 2 is an enzyme that in humans is encoded by the FBP2 gene.

Function

This gene encodes a gluconeogenesis regulatory enzyme which catalyzes the hydrolysis of fructose 2,6-bisphosphate to fructose 6-phosphate and inorganic phosphate.

Further reading

• Rakus D, Maciaszczyk E, Wawrzycka D, Ułaszewski S, Eschrich K, Dzugaj A (October 2005). "The origin of the high sensitivity of muscle fructose 1,6-bisphosphatase towards AMP". FEBS Letters. 579 (25): 5577–5581. doi:10.1016/j.febslet.2005.09.021. PMID 16213487. S2CID 6931830.
• Gizak A, Maciaszczyk E, Dzugaj A, Eschrich K, Rakus D (July 2008). "Evolutionary conserved N-terminal region of human muscle fructose 1,6-bisphosphatase regulates its activity and the interaction with aldolase". Proteins. 72 (1): 209–216. doi:10.1002/prot.21909. PMID 18214967. S2CID 21403418.
• Flachsbart F, Franke A, Kleindorp R, Caliebe A, Blanché H, Schreiber S, Nebel A (December 2010). "Investigation of genetic susceptibility factors for human longevity - a targeted nonsynonymous SNP study". Mutation Research. 694 (1–2): 13–19. doi:10.1016/j.mrfmmm.2010.08.006. PMID 20800603.
• Li H, Wang J, Xu H, Xing R, Pan Y, Li W, et al. (September 2013). "Decreased fructose-1,6-bisphosphatase-2 expression promotes glycolysis and growth in gastric cancer cells". Molecular Cancer. 12 (1): 110. doi:10.1186/1476-4598-12-110. PMC 3849177. PMID 24063558.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.