UniProtKB - P09467 (F16P1_HUMAN)
Protein
Fructose-1,6-bisphosphatase 1
Gene
FBP1
Organism
Homo sapiens (Human)
Status
Functioni
Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liver. Important regulator of appetite and adiposity; increased expression of the protein in liver after nutrient excess increases circulating satiety hormones and reduces appetite-stimulating neuropeptides and thus seems to provide a feedback mechanism to limit weight gain.3 Publications
Catalytic activityi
- EC:3.1.3.112 Publications
Cofactori
Mg2+1 PublicationNote: Binds 3 Mg2+ ions per subunit.By similarity
Activity regulationi
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 allosteric inhibitor. AMP binding affects the turnover of bound substrate and not the affinity for substrate. Fructose 2,6-bisphosphate acts as competitive inhibitor. Fructose 2,6-bisphosphate and AMP have synergistic effects.5 Publications
Kineticsi
The kinetic constants are determined for the recombinant enzyme expressed in E.coli.
- KM=2.7 µM for fructose 1,6-biphosphate1 Publication
: gluconeogenesis Pathwayi
This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 69 | Magnesium 1By similarity | 1 | |
Metal bindingi | 98 | Magnesium 1By similarity | 1 | |
Metal bindingi | 98 | Magnesium 2By similarity | 1 | |
Metal bindingi | 119 | Magnesium 2By similarity | 1 | |
Metal bindingi | 119 | Magnesium 3Combined sources | 1 | |
Metal bindingi | 121 | Magnesium 2; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 122 | Magnesium 3Combined sources | 1 | |
Binding sitei | 141 | AMPCombined sources1 Publication | 1 | |
Binding sitei | 265 | SubstrateBy similarity | 1 | |
Metal bindingi | 281 | Magnesium 3Combined sources | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 18 – 22 | AMPCombined sources1 Publication | 5 | |
Nucleotide bindingi | 28 – 32 | AMPCombined sources1 Publication | 5 | |
Nucleotide bindingi | 113 – 114 | AMPCombined sources1 Publication | 2 |
GO - Molecular functioni
- AMP binding Source: UniProtKB
- fructose 1,6-bisphosphate 1-phosphatase activity Source: UniProtKB
- identical protein binding Source: UniProtKB
- metal ion binding Source: UniProtKB
- monosaccharide binding Source: UniProtKB
- RNA polymerase II transcription factor binding Source: CAFA
GO - Biological processi
- cellular response to drug Source: UniProtKB
- cellular response to magnesium ion Source: UniProtKB
- dephosphorylation Source: UniProtKB
- fructose 1,6-bisphosphate metabolic process Source: GO_Central
- fructose 6-phosphate metabolic process Source: UniProtKB
- fructose metabolic process Source: GO_Central
- gluconeogenesis Source: UniProtKB
- negative regulation of cell growth Source: UniProtKB
- negative regulation of glycolytic process Source: UniProtKB
- negative regulation of Ras protein signal transduction Source: UniProtKB
- negative regulation of transcription by RNA polymerase II Source: CAFA
- regulation of gluconeogenesis Source: UniProtKB
- sucrose biosynthetic process Source: GO_Central
Keywordsi
Molecular function | Allosteric enzyme, Hydrolase |
Biological process | Carbohydrate metabolism, Gluconeogenesis |
Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
BioCyci | MetaCyc:HS09189-MONOMER |
BRENDAi | 3.1.3.11, 2681 |
PathwayCommonsi | P09467 |
Reactomei | R-HSA-70263, Gluconeogenesis |
SABIO-RKi | P09467 |
UniPathwayi | UPA00138 |
Protein family/group databases
MoonProti | P09467 |
Names & Taxonomyi
Protein namesi | Recommended name: Fructose-1,6-bisphosphatase 1 (EC:3.1.3.112 Publications)Short name: FBPase 1 Alternative name(s): D-fructose-1,6-bisphosphate 1-phosphohydrolase 1 Liver FBPase |
Gene namesi | Name:FBP1 Synonyms:FBP |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000165140.9 |
HGNCi | HGNC:3606, FBP1 |
MIMi | 611570, gene |
neXtProti | NX_P09467 |
Subcellular locationi
Cytosol
- cytosol Source: UniProtKB
Extracellular region or secreted
- extracellular exosome Source: UniProtKB
Nucleus
- nucleus Source: CAFA
Other locations
- cytoplasm Source: UniProtKB
Pathology & Biotechi
Involvement in diseasei
Fructose-1,6-bisphosphatase deficiency (FBP1D)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive metabolic disorder characterized by impaired gluconeogenesis, and episodes of hypoglycemia and metabolic acidosis that can be lethal in newborn infants or young children.
Related information in OMIMFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_075492 | 158 | R → W in FBP1D; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs766005419EnsemblClinVar. | 1 | |
Natural variantiVAR_002380 | 164 | G → S in FBP1D. 1 PublicationCorresponds to variant dbSNP:rs121918188EnsemblClinVar. | 1 | |
Natural variantiVAR_002381 | 177 | A → D in FBP1D. 1 PublicationCorresponds to variant dbSNP:rs121918189EnsemblClinVar. | 1 | |
Natural variantiVAR_038812 | 194 | F → S in FBP1D. 1 PublicationCorresponds to variant dbSNP:rs121918191EnsemblClinVar. | 1 | |
Natural variantiVAR_038813 | 284 | P → R in FBP1D. 1 PublicationCorresponds to variant dbSNP:rs121918192EnsemblClinVar. | 1 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 70 | Q → E: Increased affinity towards Ca(2+) and Mg(2+). 1 Publication | 1 | |
Mutagenesisi | 119 | D → A: Reduced activity. 1 Publication | 1 | |
Mutagenesisi | 122 | D → A: Reduced activity. 1 Publication | 1 |
Keywords - Diseasei
Disease mutationOrganism-specific databases
DisGeNETi | 2203 |
MalaCardsi | FBP1 |
MIMi | 229700, phenotype |
OpenTargetsi | ENSG00000165140 |
Orphaneti | 348, Fructose-1,6-bisphosphatase deficiency |
PharmGKBi | PA28018 |
Miscellaneous databases
Pharosi | P09467, Tchem |
Chemistry databases
ChEMBLi | CHEMBL3975 |
DrugBanki | DB02778, 2,5-Anhydroglucitol-1,6-Biphosphate DB07312, 2,5-DICHLORO-N-(5-CHLORO-1,3-BENZOXAZOL-2-YL)BENZENESULFONAMIDE DB07321, 2,5-DICHLORO-N-[5-METHOXY-7-(6-METHOXYPYRIDIN-3-YL)-1,3-BENZOXAZOL-2-YL]BENZENESULFONAMIDE DB08484, 4-AMINO-N-[(2-SULFANYLETHYL)CARBAMOYL]BENZENESULFONAMIDE DB00131, Adenosine phosphate DB04493, Fructose-6-phosphate DB05518, Managlinat dialanetil DB05053, MB-07803 DB04175, Mdl-29951 DB07270, N-[7-(3-AMINOPHENYL)-5-METHOXY-1,3-BENZOXAZOL-2-YL]-2,5-DICHLOROBENZENESULFONAMIDE DB02848, {4-[3-(6,7-Diethoxy-Quinazolin-4-Ylamino)-Phenyl]-Thiazol-2-Yl}-Methanol |
DrugCentrali | P09467 |
Polymorphism and mutation databases
BioMutai | FBP1 |
DMDMi | 311033495 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedBy similarity1 Publication | |||
ChainiPRO_0000200498 | 2 – 338 | Fructose-1,6-bisphosphatase 1Add BLAST | 337 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanineBy similarity | 1 | |
Modified residuei | 151 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 216 | PhosphotyrosineBy similarity | 1 | |
Modified residuei | 245 | PhosphotyrosineBy similarity | 1 | |
Modified residuei | 265 | PhosphotyrosineCombined sources | 1 |
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
CPTACi | CPTAC-200 CPTAC-201 |
EPDi | P09467 |
jPOSTi | P09467 |
MassIVEi | P09467 |
MaxQBi | P09467 |
PaxDbi | P09467 |
PeptideAtlasi | P09467 |
PRIDEi | P09467 |
ProteomicsDBi | 52223 |
PTM databases
DEPODi | FBP1 |
iPTMneti | P09467 |
PhosphoSitePlusi | P09467 |
Expressioni
Tissue specificityi
Expressed in pancreatic islets.1 Publication
Inductioni
Up-regulated in pancreatic islets of individuals with type 2 diabetes.1 Publication
Gene expression databases
Bgeei | ENSG00000165140, Expressed in right lobe of liver and 169 other tissues |
ExpressionAtlasi | P09467, baseline and differential |
Genevisiblei | P09467, HS |
Organism-specific databases
HPAi | ENSG00000165140, Tissue enhanced (liver, lung) |
Interactioni
Subunit structurei
Homotetramer.
4 PublicationsBinary interactionsi
Hide detailsP09467
GO - Molecular functioni
- identical protein binding Source: UniProtKB
- RNA polymerase II transcription factor binding Source: CAFA
Protein-protein interaction databases
BioGRIDi | 108497, 36 interactors |
DIPi | DIP-46677N |
IntActi | P09467, 48 interactors |
MINTi | P09467 |
STRINGi | 9606.ENSP00000408025 |
Chemistry databases
BindingDBi | P09467 |
Miscellaneous databases
RNActi | P09467, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P09467 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P09467 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 122 – 125 | Substrate bindingBy similarity | 4 | |
Regioni | 213 – 216 | Substrate bindingBy similarity | 4 | |
Regioni | 244 – 249 | Substrate bindingBy similarity | 6 | |
Regioni | 275 – 277 | Substrate bindingBy similarity | 3 |
Sequence similaritiesi
Belongs to the FBPase class 1 family.Curated
Phylogenomic databases
eggNOGi | KOG1458, Eukaryota |
GeneTreei | ENSGT00390000015513 |
HOGENOMi | CLU_039977_1_0_1 |
InParanoidi | P09467 |
OMAi | QSGLVCR |
OrthoDBi | 1381522at2759 |
PhylomeDBi | P09467 |
TreeFami | TF314824 |
Family and domain databases
CDDi | cd00354, FBPase, 1 hit |
HAMAPi | MF_01855, FBPase_class1, 1 hit |
InterProi | View protein in InterPro IPR044015, FBPase_C_dom IPR000146, FBPase_class-1 IPR033391, FBPase_N IPR028343, FBPtase IPR020548, Fructose_bisphosphatase_AS |
PANTHERi | PTHR11556, PTHR11556, 1 hit |
Pfami | View protein in Pfam PF00316, FBPase, 1 hit PF18913, FBPase_C, 1 hit |
PIRSFi | PIRSF500210, FBPtase, 1 hit PIRSF000904, FBPtase_SBPase, 1 hit |
PRINTSi | PR00115, F16BPHPHTASE |
PROSITEi | View protein in PROSITE PS00124, FBPASE, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All
P09467-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MADQAPFDTD VNTLTRFVME EGRKARGTGE LTQLLNSLCT AVKAISSAVR
60 70 80 90 100
KAGIAHLYGI AGSTNVTGDQ VKKLDVLSND LVMNMLKSSF ATCVLVSEED
110 120 130 140 150
KHAIIVEPEK RGKYVVCFDP LDGSSNIDCL VSVGTIFGIY RKKSTDEPSE
160 170 180 190 200
KDALQPGRNL VAAGYALYGS ATMLVLAMDC GVNCFMLDPA IGEFILVDKD
210 220 230 240 250
VKIKKKGKIY SLNEGYARDF DPAVTEYIQR KKFPPDNSAP YGARYVGSMV
260 270 280 290 300
ADVHRTLVYG GIFLYPANKK SPNGKLRLLY ECNPMAYVME KAGGMATTGK
310 320 330
EAVLDVIPTD IHQRAPVILG SPDDVLEFLK VYEKHSAQ
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A3B3IUC7 | A0A3B3IUC7_HUMAN | Fructose-bisphosphatase | FBP1 | 273 | Annotation score: | ||
Q5VZC3 | Q5VZC3_HUMAN | Fructose-bisphosphatase | FBP1 | 151 | Annotation score: |
Sequence cautioni
The sequence AAC50207 differs from that shown. Reason: Erroneous gene model prediction.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 215 | G → A in AAA35817 (PubMed:8387495).Curated | 1 | |
Sequence conflicti | 215 | G → A in AAC25774 (PubMed:10222032).Curated | 1 | |
Sequence conflicti | 337 | A → G in AAC25774 (PubMed:10222032).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_075492 | 158 | R → W in FBP1D; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs766005419EnsemblClinVar. | 1 | |
Natural variantiVAR_002380 | 164 | G → S in FBP1D. 1 PublicationCorresponds to variant dbSNP:rs121918188EnsemblClinVar. | 1 | |
Natural variantiVAR_002381 | 177 | A → D in FBP1D. 1 PublicationCorresponds to variant dbSNP:rs121918189EnsemblClinVar. | 1 | |
Natural variantiVAR_038812 | 194 | F → S in FBP1D. 1 PublicationCorresponds to variant dbSNP:rs121918191EnsemblClinVar. | 1 | |
Natural variantiVAR_022212 | 218 | R → K7 PublicationsCorresponds to variant dbSNP:rs1769259EnsemblClinVar. | 1 | |
Natural variantiVAR_022213 | 233 | F → I1 PublicationCorresponds to variant dbSNP:rs2297085EnsemblClinVar. | 1 | |
Natural variantiVAR_022214 | 255 | R → L1 PublicationCorresponds to variant dbSNP:rs28369761Ensembl. | 1 | |
Natural variantiVAR_038813 | 284 | P → R in FBP1D. 1 PublicationCorresponds to variant dbSNP:rs121918192EnsemblClinVar. | 1 | |
Natural variantiVAR_002382 | 325 | V → A1 Publication | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M19922 mRNA Translation: AAA35517.1 L10320 mRNA Translation: AAA35817.1 D26054 mRNA Translation: BAA05051.1 D26055 mRNA Translation: BAA05052.1 D26056 mRNA Translation: BAA05053.1 U21931 , U21925, U21926, U21927, U21929, U21930 Genomic DNA Translation: AAC50207.1 Sequence problems. AF073475 mRNA Translation: AAC25774.1 AK223395 mRNA Translation: BAD97115.1 AY866483 Genomic DNA Translation: AAW34363.1 AL161728 Genomic DNA No translation available. BC012927 mRNA Translation: AAH12927.1 U47919 mRNA Translation: AAA89098.1 U47918 mRNA Translation: AAA89097.1 |
CCDSi | CCDS6712.1 |
PIRi | A46666 |
RefSeqi | NP_000498.2, NM_000507.3 NP_001121100.1, NM_001127628.1 |
Genome annotation databases
Ensembli | ENST00000375326; ENSP00000364475; ENSG00000165140 ENST00000415431; ENSP00000408025; ENSG00000165140 |
GeneIDi | 2203 |
KEGGi | hsa:2203 |
UCSCi | uc004auw.5, human |
Keywords - Coding sequence diversityi
PolymorphismSimilar proteinsi
Cross-referencesi
Web resourcesi
NIEHS-SNPs |
Wikipedia Fructose bisphosphatase entry |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M19922 mRNA Translation: AAA35517.1 L10320 mRNA Translation: AAA35817.1 D26054 mRNA Translation: BAA05051.1 D26055 mRNA Translation: BAA05052.1 D26056 mRNA Translation: BAA05053.1 U21931 , U21925, U21926, U21927, U21929, U21930 Genomic DNA Translation: AAC50207.1 Sequence problems. AF073475 mRNA Translation: AAC25774.1 AK223395 mRNA Translation: BAD97115.1 AY866483 Genomic DNA Translation: AAW34363.1 AL161728 Genomic DNA No translation available. BC012927 mRNA Translation: AAH12927.1 U47919 mRNA Translation: AAA89098.1 U47918 mRNA Translation: AAA89097.1 |
CCDSi | CCDS6712.1 |
PIRi | A46666 |
RefSeqi | NP_000498.2, NM_000507.3 NP_001121100.1, NM_001127628.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1FTA | X-ray | 2.30 | A/B/C/D | 2-338 | [»] | |
2FHY | X-ray | 2.95 | A/D/H/L | 1-338 | [»] | |
2FIE | X-ray | 2.81 | A/D/H/L | 1-338 | [»] | |
2FIX | X-ray | 3.50 | A/D/H/L | 1-338 | [»] | |
2JJK | X-ray | 2.00 | A/B/C/D | 1-338 | [»] | |
2VT5 | X-ray | 2.20 | A/B/C/D/E/F/G/H | 1-338 | [»] | |
2WBB | X-ray | 2.22 | A/B/C/D/E/F/G/H | 1-338 | [»] | |
2WBD | X-ray | 2.40 | A/B/C/D/E/F/G/H | 1-338 | [»] | |
2Y5K | X-ray | 2.10 | A/B/C/D | 1-338 | [»] | |
2Y5L | X-ray | 2.20 | A/B/C/D/E/F/G/H | 1-338 | [»] | |
3A29 | X-ray | 2.60 | A/B/C/D | 2-338 | [»] | |
3KBZ | X-ray | 2.45 | A/B/C/D | 2-338 | [»] | |
3KC0 | X-ray | 2.80 | A/B/C/D | 2-338 | [»] | |
3KC1 | X-ray | 2.25 | A/B/C/D | 2-338 | [»] | |
4MJO | X-ray | 2.40 | A/B/C/D/E/F/G/H | 1-338 | [»] | |
5LDZ | X-ray | 2.20 | A/B/C/D/E/F | 1-338 | [»] | |
5PZQ | X-ray | 2.70 | A/B/C/D | 1-338 | [»] | |
5PZR | X-ray | 1.90 | A/B/C/D | 1-338 | [»] | |
5PZS | X-ray | 2.37 | A/B/C/D | 1-338 | [»] | |
5PZT | X-ray | 2.80 | A/B/C/D/E/F/G/H | 1-338 | [»] | |
5PZU | X-ray | 1.90 | A/B/C/D | 1-338 | [»] | |
5PZV | X-ray | 2.00 | A/B/C/D | 1-338 | [»] | |
5PZW | X-ray | 2.00 | A/B/C/D | 1-338 | [»] | |
5PZX | X-ray | 2.75 | A/B/C/D/E/F/G/H | 1-338 | [»] | |
5PZY | X-ray | 2.21 | A/B/C/D/E/F/G/H | 1-338 | [»] | |
5PZZ | X-ray | 2.50 | A/B/C/D/E/F/G/H | 1-338 | [»] | |
5Q00 | X-ray | 2.60 | A/B/C/D/E/F/G/H | 1-338 | [»] | |
5Q01 | X-ray | 2.60 | A/B/C/D/E/F/G/H | 1-338 | [»] | |
5Q02 | X-ray | 2.10 | A/B/C/D | 1-338 | [»] | |
5Q03 | X-ray | 2.31 | A/B/C/D/E/F/G/H | 1-338 | [»] | |
5Q04 | X-ray | 2.50 | A/B/C/D/E/F/G/H | 1-338 | [»] | |
5Q05 | X-ray | 2.20 | A/B/C/D/E/F/G/H | 1-338 | [»] | |
5Q06 | X-ray | 2.40 | A/B/C/D | 1-338 | [»] | |
5Q07 | X-ray | 2.42 | A/B/C/D/E/F/G/H | 1-338 | [»] | |
5Q08 | X-ray | 2.20 | A/B/C/D/E/F/G/H | 1-338 | [»] | |
5Q09 | X-ray | 1.90 | A/B/C/D/E/F/G/H | 1-338 | [»] | |
5Q0A | X-ray | 2.30 | A/B/C/D | 1-338 | [»] | |
5Q0B | X-ray | 2.30 | A/B/C/D | 1-338 | [»] | |
6LS5 | X-ray | 2.03 | A/B/C/D | 1-338 | [»] | |
6LW2 | X-ray | 2.40 | A/B/C/D | 1-338 | [»] | |
SMRi | P09467 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 108497, 36 interactors |
DIPi | DIP-46677N |
IntActi | P09467, 48 interactors |
MINTi | P09467 |
STRINGi | 9606.ENSP00000408025 |
Chemistry databases
BindingDBi | P09467 |
ChEMBLi | CHEMBL3975 |
DrugBanki | DB02778, 2,5-Anhydroglucitol-1,6-Biphosphate DB07312, 2,5-DICHLORO-N-(5-CHLORO-1,3-BENZOXAZOL-2-YL)BENZENESULFONAMIDE DB07321, 2,5-DICHLORO-N-[5-METHOXY-7-(6-METHOXYPYRIDIN-3-YL)-1,3-BENZOXAZOL-2-YL]BENZENESULFONAMIDE DB08484, 4-AMINO-N-[(2-SULFANYLETHYL)CARBAMOYL]BENZENESULFONAMIDE DB00131, Adenosine phosphate DB04493, Fructose-6-phosphate DB05518, Managlinat dialanetil DB05053, MB-07803 DB04175, Mdl-29951 DB07270, N-[7-(3-AMINOPHENYL)-5-METHOXY-1,3-BENZOXAZOL-2-YL]-2,5-DICHLOROBENZENESULFONAMIDE DB02848, {4-[3-(6,7-Diethoxy-Quinazolin-4-Ylamino)-Phenyl]-Thiazol-2-Yl}-Methanol |
DrugCentrali | P09467 |
Protein family/group databases
MoonProti | P09467 |
PTM databases
DEPODi | FBP1 |
iPTMneti | P09467 |
PhosphoSitePlusi | P09467 |
Polymorphism and mutation databases
BioMutai | FBP1 |
DMDMi | 311033495 |
Proteomic databases
CPTACi | CPTAC-200 CPTAC-201 |
EPDi | P09467 |
jPOSTi | P09467 |
MassIVEi | P09467 |
MaxQBi | P09467 |
PaxDbi | P09467 |
PeptideAtlasi | P09467 |
PRIDEi | P09467 |
ProteomicsDBi | 52223 |
Protocols and materials databases
Antibodypediai | 1620, 267 antibodies |
DNASUi | 2203 |
Genome annotation databases
Ensembli | ENST00000375326; ENSP00000364475; ENSG00000165140 ENST00000415431; ENSP00000408025; ENSG00000165140 |
GeneIDi | 2203 |
KEGGi | hsa:2203 |
UCSCi | uc004auw.5, human |
Organism-specific databases
CTDi | 2203 |
DisGeNETi | 2203 |
EuPathDBi | HostDB:ENSG00000165140.9 |
GeneCardsi | FBP1 |
HGNCi | HGNC:3606, FBP1 |
HPAi | ENSG00000165140, Tissue enhanced (liver, lung) |
MalaCardsi | FBP1 |
MIMi | 229700, phenotype 611570, gene |
neXtProti | NX_P09467 |
OpenTargetsi | ENSG00000165140 |
Orphaneti | 348, Fructose-1,6-bisphosphatase deficiency |
PharmGKBi | PA28018 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG1458, Eukaryota |
GeneTreei | ENSGT00390000015513 |
HOGENOMi | CLU_039977_1_0_1 |
InParanoidi | P09467 |
OMAi | QSGLVCR |
OrthoDBi | 1381522at2759 |
PhylomeDBi | P09467 |
TreeFami | TF314824 |
Enzyme and pathway databases
UniPathwayi | UPA00138 |
BioCyci | MetaCyc:HS09189-MONOMER |
BRENDAi | 3.1.3.11, 2681 |
PathwayCommonsi | P09467 |
Reactomei | R-HSA-70263, Gluconeogenesis |
SABIO-RKi | P09467 |
Miscellaneous databases
BioGRID-ORCSi | 2203, 17 hits in 851 CRISPR screens |
ChiTaRSi | FBP1, human |
EvolutionaryTracei | P09467 |
GenomeRNAii | 2203 |
Pharosi | P09467, Tchem |
PROi | PR:P09467 |
RNActi | P09467, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000165140, Expressed in right lobe of liver and 169 other tissues |
ExpressionAtlasi | P09467, baseline and differential |
Genevisiblei | P09467, HS |
Family and domain databases
CDDi | cd00354, FBPase, 1 hit |
HAMAPi | MF_01855, FBPase_class1, 1 hit |
InterProi | View protein in InterPro IPR044015, FBPase_C_dom IPR000146, FBPase_class-1 IPR033391, FBPase_N IPR028343, FBPtase IPR020548, Fructose_bisphosphatase_AS |
PANTHERi | PTHR11556, PTHR11556, 1 hit |
Pfami | View protein in Pfam PF00316, FBPase, 1 hit PF18913, FBPase_C, 1 hit |
PIRSFi | PIRSF500210, FBPtase, 1 hit PIRSF000904, FBPtase_SBPase, 1 hit |
PRINTSi | PR00115, F16BPHPHTASE |
PROSITEi | View protein in PROSITE PS00124, FBPASE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | F16P1_HUMAN | |
Accessioni | P09467Primary (citable) accession number: P09467 Secondary accession number(s): O75571, Q53F94, Q96E46 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
Last sequence update: | November 2, 2010 | |
Last modified: | December 2, 2020 | |
This is version 217 of the entry and version 5 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 9
Human chromosome 9: entries, gene names and cross-references to MIM - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations