FBP2
entrez
8789
canonical
uniprot
O00757
canonical
ensembl
ENSG00000130957
resolver
ensp
ENSP00000364486
resolver
enst
ENST00000375337
resolver
genesymbol
FBP2
resolver
hgnc
HGNC:3607
resolver
uniprot
Q17R39
resolver
uniprot
Q6FI53
resolver
uniprot_entry
F16P2_HUMAN
resolver
uniprot_sec
Q17R39
resolver
uniprot_sec
Q6FI53
resolver
activity_regulation
ACTIVITY REGULATION: Subject to complex allosteric regulation. The enzyme can assume an active R-state, or an inactive T-state. Intermediate conformations may exist. AMP acts as an allosteric inhibitor (PubMed:33977262). Fructose 2,6-bisphosphate acts as a competitive inhibitor. Strongly inhibited by Ca(2+). {ECO:0000269|PubMed:16213487, ECO:0000269|PubMed:17350621, ECO:0000269|PubMed:18214967, ECO:0000269|PubMed:33977262}.
uniprot
proteins
amino_acid_sequence
MTDRSPFETDMLTLTRYVMEKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNSLVINMVQSSYSTCVLVSEENKDAIITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTSEDEPSEKDALQCGRNIVAAGYALYGSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIYSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYGARYVGSMVADVHRTLVYGGIFLYPANQKSPKGKLRLLYECNPVAYIIEQAGGLATTGTQPVLDVKPEAIHQRVPLILGSPEDVQEYLTCVQKNQAGS
uniprot
proteins
disease_involvement
DISEASE: Leukodystrophy, childhood-onset, remitting (CORLK) [MIM:619864]: An autosomal dominant disorder characterized by loss of developmental abilities, demyelination and leukodystrophy on brain imaging, triggered by fever or infection in the first year of life. Abnormalities almost completely resolve over a period of 1 to 2 years, and affected children regain normal development accompanied by remyelination. {ECO:0000269|PubMed:33977262}. Note=The disease may be caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.1.3.11
uniprot
proteins
function
FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations and probably participates in glycogen synthesis from carbohydrate precursors, such as lactate. {ECO:0000269|PubMed:17350621, ECO:0000269|PubMed:18214967, ECO:0000269|PubMed:33977262}.
uniprot
proteins
mass_dalton
36743
uniprot
proteins
mutagenesis
MUTAGEN 1..10; /note="Missing: Greatly reduces sensitivity to inhibition by AMP and Ca(2+) and activation by Mg(2+). Decreases binding to ALDOA."; /evidence="ECO:0000269|PubMed:18214967"; MUTAGEN 1..7; /note="Missing: Greatly reduces sensitivity to inhibition by AMP and Ca(2+) and activation by Mg(2+). Decreases binding to ALDOA."; MUTAGEN 1..6; /note="Missing: Reduces sensitivity to inhibition by AMP and Ca(2+) and activation by Mg(2+). Decreases binding to ALDOA."; MUTAGEN 1..5; /note="Missing: Reduces sensitivity to inhibition by AMP and Ca(2+) and activation by Mg(2+). Decreases binding to ALDOA."; MUTAGEN 1..4; /note="Missing: Slightly reduces sensitivity to inhibition by AMP and Ca(2+) and activation by Mg(2+). Decreases binding to ALDOA."; MUTAGEN 1..3; /note="Missing: No effect on kinetic properties but decreases binding to ALDOA."; MUTAGEN 1..2; /note="Missing: No effect on kinetic properties and interaction with ALDOA."; MUTAGEN 1; /note="Missing: No effect on kinetic properties and interaction with ALDOA."; MUTAGEN 21; /note="K->E: Reduces sensitivity to AMP; when associated with M-178 and C-180."; /evidence="ECO:0000269|PubMed:16213487"; MUTAGEN 33; /note="Q->R: Causes conformational change of N-terminal residues and decreased sensitivity towards AMP with lack of conversion to the inactive T-state in the presence of AMP."; MUTAGEN 70; /note="E->Q: Greatly reduces affinity towards Ca(2+) and slightly reduces affinity towards Mg(2+)."; /evidence="ECO:0000269|PubMed:17350621"; MUTAGEN 178; /note="T->M: Reduces sensitivity to AMP; when associated with E-21 and C-180."; /evidence="ECO:0000269|PubMed:16213487"; MUTAGEN 180; /note="Q->C: Reduces sensitivity to AMP; when associated with E-21 and M-178."; /evidence="ECO:0000269|PubMed:16213487"; MUTAGEN 204..208; /note="KKKGK->AAAGA,EEEGE: Almost completely abolishes nuclear localization."; /evidence="ECO:0000269|PubMed:19626708"; MUTAGEN 204; /note="K->E: Minor reduction in nuclear localization."; MUTAGEN 205; /note="K->E: Minor reduction in nuclear localization."; MUTAGEN 206; /note="K->E: Greatly reduces nuclear lozalization."; MUTAGEN 208; /note="K->E: Significantly reduces nuclear localization.
uniprot
proteins
pathway_participation
PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
uniprot
proteins
protein_family
FBPase class 1 family
uniprot
proteins
pubmed
12507293
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16213487
uniprot
proteins
pubmed
17350621
uniprot
proteins
pubmed
18214967
uniprot
proteins
pubmed
19626708
uniprot
proteins
pubmed
22120740
uniprot
proteins
pubmed
24086250
uniprot
proteins
pubmed
33977262
uniprot
proteins
pubmed
9678974
uniprot
proteins
sequence_length
339
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell junction {ECO:0000250}. Cytoplasm. Nucleus. Cytoplasm, myofibril, sarcomere, Z line. Note=In neonatal cardiomyocytes, distributed throughout the cytosol, accumulating in the intercalated disks which occur at the Z line of cardiomyocytes and connect adjacent cells, and also located in the nucleus; dissociates from the Z line following an increase in cytosolic Ca(2+) concentration (By similarity). In muscle precursor cells, localizes predominantly to the nucleus and to a lesser extent to the cytoplasm at the proliferative phase, while mainly localizing to the cytoplasm at the differentiation phase (By similarity). Colocalizes with ALDOA and alpha-actinin on both sides of the Z line of skeletal muscle; dissociates rapidly from the Z line following an increase in cytosolic Ca(2+) concentration. {ECO:0000250}.
uniprot
proteins