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P09467 (F16P1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fructose-1,6-bisphosphatase 1

Short name=FBPase 1
EC=3.1.3.11
Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase 1
Liver FBPase
Gene names
Name:FBP1
Synonyms:FBP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11 Ref.13 Ref.14

Catalytic activity

D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate. HAMAP-Rule MF_01855

Cofactor

Binds 3 magnesium ions per subunit By similarity. Ref.15 Ref.16

Enzyme 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 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. Ref.12 Ref.16 Ref.17 Ref.18 Ref.19

Pathway

Carbohydrate biosynthesis; gluconeogenesis. HAMAP-Rule MF_01855

Subunit structure

Homotetramer. Ref.16 Ref.17 Ref.18 Ref.19

Tissue specificity

Expressed in pancreatic islets. Ref.13

Induction

Up-regulated in pancreatic islets of individuals with type 2 diabetes. Ref.12 Ref.13 Ref.16 Ref.17 Ref.18 Ref.19

Involvement in disease

Fructose-1,6-bisphosphatase deficiency (FBPD) [MIM:229700]: Inherited as an autosomal recessive disorder mainly in the liver and causes life-threatening episodes of hypoglycemia and metabolic acidosis (lactacidemia) in newborn infants or young children.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20 Ref.21

Sequence similarities

Belongs to the FBPase class 1 family.

Biophysicochemical properties

Kinetic parameters:

The kinetic constants are determined for the recombinant enzyme expressed in E.coli.

KM=2.7 µM for fructose 1,6-biphosphate Ref.12

Sequence caution

The sequence AAC50207.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Gluconeogenesis
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   PTMAcetylation
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

cellular response to drug

Inferred from direct assay Ref.18Ref.19. Source: UniProtKB

cellular response to magnesium ion

Inferred from direct assay Ref.5. Source: UniProtKB

dephosphorylation

Inferred from direct assay Ref.19Ref.2. Source: UniProtKB

fructose 6-phosphate metabolic process

Inferred from direct assay Ref.18Ref.2. Source: UniProtKB

fructose metabolic process

Traceable author statement Ref.4. Source: ProtInc

gluconeogenesis

Inferred from mutant phenotype PubMed 19259699PubMed 20096900. Source: UniProtKB

glucose metabolic process

Traceable author statement. Source: Reactome

negative regulation of Ras protein signal transduction

Inferred from direct assay PubMed 19881551. Source: UniProtKB

negative regulation of cell growth

Inferred from direct assay PubMed 19881551. Source: UniProtKB

negative regulation of glycolytic process

Inferred from direct assay PubMed 19881551. Source: UniProtKB

protein homotetramerization

Inferred from direct assay Ref.18Ref.19. Source: UniProtKB

regulation of gluconeogenesis

Inferred from mutant phenotype Ref.4. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 20096900. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

   Molecular_functionAMP binding

Inferred from direct assay Ref.5Ref.19Ref.2. Source: UniProtKB

fructose 1,6-bisphosphate 1-phosphatase activity

Inferred from direct assay Ref.18Ref.19Ref.2. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 16169070PubMed 16189514PubMed 21516116. Source: IntAct

metal ion binding

Inferred from mutant phenotype Ref.2. Source: UniProtKB

monosaccharide binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.5Ref.2. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-712740,EBI-712740
BIN1O004994EBI-712740,EBI-719094

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 338337Fructose-1,6-bisphosphatase 1 HAMAP-Rule MF_01855
PRO_0000200498

Regions

Nucleotide binding18 – 225AMP HAMAP-Rule MF_01855
Nucleotide binding28 – 325AMP HAMAP-Rule MF_01855
Nucleotide binding113 – 1142AMP HAMAP-Rule MF_01855
Region122 – 1254Substrate binding HAMAP-Rule MF_01855
Region213 – 2164Substrate binding HAMAP-Rule MF_01855
Region244 – 2496Substrate binding HAMAP-Rule MF_01855
Region275 – 2773Substrate binding HAMAP-Rule MF_01855

Sites

Metal binding691Magnesium 1 By similarity
Metal binding981Magnesium 1 By similarity
Metal binding981Magnesium 2
Metal binding1191Magnesium 2
Metal binding1191Magnesium 3
Metal binding1211Magnesium 2; via carbonyl oxygen
Metal binding1221Magnesium 3
Metal binding2811Magnesium 3
Binding site1411AMP
Binding site2651Substrate

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1511N6-succinyllysine By similarity

Natural variations

Natural variant1641G → S in FBPD. Ref.20
VAR_002380
Natural variant1771A → D in FBPD. Ref.20
VAR_002381
Natural variant1941F → S in FBPD. Ref.21
VAR_038812
Natural variant2181R → K. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7
Corresponds to variant rs1769259 [ dbSNP | Ensembl ].
VAR_022212
Natural variant2331F → I. Ref.7
Corresponds to variant rs2297085 [ dbSNP | Ensembl ].
VAR_022213
Natural variant2551R → L. Ref.7
Corresponds to variant rs28369761 [ dbSNP | Ensembl ].
VAR_022214
Natural variant2841P → R in FBPD. Ref.21
VAR_038813
Natural variant3251V → A. Ref.20
VAR_002382

Experimental info

Mutagenesis701Q → E: Increased affinity towards Ca(2+) and Mg(2+). Ref.12
Mutagenesis1191D → A: Reduced activity. Ref.2
Mutagenesis1221D → A: Reduced activity. Ref.2
Sequence conflict2151G → A in AAA35817. Ref.2
Sequence conflict2151G → A in AAC25774. Ref.5
Sequence conflict3371A → G in AAC25774. Ref.5

Secondary structure

.......................................................... 338
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09467 [UniParc].

Last modified November 2, 2010. Version 5.
Checksum: B3D270BCBB358B71

FASTA33836,842
        10         20         30         40         50         60 
MADQAPFDTD VNTLTRFVME EGRKARGTGE LTQLLNSLCT AVKAISSAVR KAGIAHLYGI 

        70         80         90        100        110        120 
AGSTNVTGDQ VKKLDVLSND LVMNMLKSSF ATCVLVSEED KHAIIVEPEK RGKYVVCFDP 

       130        140        150        160        170        180 
LDGSSNIDCL VSVGTIFGIY RKKSTDEPSE KDALQPGRNL VAAGYALYGS ATMLVLAMDC 

       190        200        210        220        230        240 
GVNCFMLDPA IGEFILVDKD VKIKKKGKIY SLNEGYARDF DPAVTEYIQR KKFPPDNSAP 

       250        260        270        280        290        300 
YGARYVGSMV ADVHRTLVYG GIFLYPANKK SPNGKLRLLY ECNPMAYVME KAGGMATTGK 

       310        320        330 
EAVLDVIPTD IHQRAPVILG SPDDVLEFLK VYEKHSAQ 

« Hide

References

« Hide 'large scale' references
[1]"Activation of the fructose 1,6-bisphosphatase gene by 1,25-dihydroxyvitamin D3 during monocytic differentiation."
Solomon D.H., Raynal M.-C., Tejwani G.A., Cayre Y.E.
Proc. Natl. Acad. Sci. U.S.A. 85:6904-6908(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LYS-218.
[2]"Isolation of a human liver fructose-1,6-bisphosphatase cDNA and expression of the protein in Escherichia coli. Role of Asp-118 and Asp-121 in catalysis."
El-Maghrabi M.R., Gidh-Jain M., Austin L.R., Pilkis S.J.
J. Biol. Chem. 268:9466-9472(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-11, MUTAGENESIS OF ASP-119 AND ASP-122, VARIANT LYS-218.
Tissue: Liver.
[3]"cDNA sequences encoding human fructose 1,6-bisphosphatase from monocytes, liver and kidney: application of monocytes to molecular analysis of human fructose 1,6-bisphosphatase deficiency."
Kikawa Y., Inuzuka M., Takano T., Shigematsu Y., Nakai A., Yamamoto Y., Jin B.Y., Koga J., Taketo A., Sudo M.
Biochem. Biophys. Res. Commun. 199:687-693(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LYS-218.
Tissue: Kidney, Liver and Monocyte.
[4]"Human fructose-1,6-bisphosphatase gene (FBP1): exon-intron organization, localization to chromosome bands 9q22.2-q22.3, and mutation screening in subjects with fructose-1,6-bisphosphatase deficiency."
El-Maghrabi M.R., Lang A.J., Jiang W., Yamagata K., Stoffel M., Takeda J., Fernald A.A., le Beau M.M., Bell G.I., Baker L., Pilkis S.J.
Genomics 27:520-525(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-218.
Tissue: Liver.
[5]"cDNA sequence and kinetic properties of human lung fructose(1, 6)bisphosphatase."
Skalecki K., Rakus D., Wisniewski J.R., Kolodziej J., Dzugaj A.
Arch. Biochem. Biophys. 365:1-9(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, VARIANT LYS-218.
Tissue: Lung.
[6]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LYS-218.
Tissue: Thymus.
[7]NIEHS SNPs program
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-218; ILE-233 AND LEU-255.
[8]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Urinary bladder.
[10]"Liver fructose-1,6-bisphosphatase cDNA: trans-complementation of fission yeast and characterization of two human transcripts."
Bertolotti R., Armbruster-Hilbert L., Okayama H.
Differentiation 59:51-60(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 320-338.
Tissue: Liver.
[11]"Expression of human fructose-1,6-bisphosphatase in the liver of transgenic mice results in increased glycerol gluconeogenesis."
Lamont B.J., Visinoni S., Fam B.C., Kebede M., Weinrich B., Papapostolou S., Massinet H., Proietto J., Favaloro J., Andrikopoulos S.
Endocrinology 147:2764-2772(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Glu 69 is essential for the high sensitivity of muscle fructose-1,6-bisphosphatase inhibition by calcium ions."
Zarzycki M., Maciaszczyk E., Dzugaj A.
FEBS Lett. 581:1347-1350(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLN-70.
[13]"Fructose-1,6-bisphosphatase overexpression in pancreatic beta-cells results in reduced insulin secretion: a new mechanism for fat-induced impairment of beta-cell function."
Kebede M., Favaloro J., Gunton J.E., Laybutt D.R., Shaw M., Wong N., Fam B.C., Aston-Mourney K., Rantzau C., Zulli A., Proietto J., Andrikopoulos S.
Diabetes 57:1887-1895(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
[14]"The role of liver fructose-1,6-bisphosphatase in regulating appetite and adiposity."
Visinoni S., Khalid N.F., Joannides C.N., Shulkes A., Yim M., Whitehead J., Tiganis T., Lamont B.J., Favaloro J.M., Proietto J., Andrikopoulos S., Fam B.C.
Diabetes 61:1122-1132(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"Crystallographic studies of the catalytic mechanism of the neutral form of fructose-1,6-bisphosphatase."
Zhang Y., Liang J.-Y., Huang S., Ke H., Lipscomb W.N.
Biochemistry 32:1844-1857(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM IONS AND SUBSTRATE ANALOGS, COFACTOR.
[16]"Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 2,6-bisphosphate, AMP, and Zn2+ at 2.0-A resolution: aspects of synergism between inhibitors."
Xue Y., Huang S., Liang J.-Y., Zhang Y., Lipscomb W.N.
Proc. Natl. Acad. Sci. U.S.A. 91:12482-12486(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-2,6-BISPHOSPHATE; AMP AND ZINC, SUBUNIT, COFACTOR, ENZYME REGULATION.
[17]"Benzoxazole benzenesulfonamides as allosteric inhibitors of fructose-1,6-bisphosphatase."
Lai C., Gum R.J., Daly M., Fry E.H., Hutchins C., Abad-Zapatero C., von Geldern T.W.
Bioorg. Med. Chem. Lett. 16:1807-1810(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) IN COMPLEX WITH BENZOXAZOLE BENZENESULFONAMIDES, SUBUNIT, ENZYME REGULATION.
[18]"Benzoxazole benzenesulfonamides are novel allosteric inhibitors of fructose-1,6-bisphosphatase with a distinct binding mode."
von Geldern T.W., Lai C., Gum R.J., Daly M., Sun C., Fry E.H., Abad-Zapatero C.
Bioorg. Med. Chem. Lett. 16:1811-1815(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH BENZOXAZOLE BENZENESULFONAMIDES, SUBUNIT, ENZYME REGULATION.
[19]"Allosteric FBPase inhibitors gain 10(5) times in potency when simultaneously binding two neighboring AMP sites."
Hebeisen P., Kuhn B., Kohler P., Gubler M., Huber W., Kitas E., Schott B., Benz J., Joseph C., Ruf A.
Bioorg. Med. Chem. Lett. 18:4708-4712(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH AROMATIC SULFONYLUREA AMP ANALOGS, SUBUNIT, ENZYME REGULATION.
[20]"Identification of genetic mutations in Japanese patients with fructose-1,6-bisphosphatase deficiency."
Kikawa Y., Inuzuka M., Jin B.Y., Kaji S., Koga J., Yamamoto Y., Fujisawa K., Hata I., Nakai A., Shigematsu Y., Mizunuma H., Taketo A., Mayumi M., Sudo M.
Am. J. Hum. Genet. 61:852-861(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FBPD SER-164 AND ASP-177, VARIANT ALA-325.
[21]"Two newly identified genomic mutations in a Japanese female patient with fructose-1,6-bisphosphatase (FBPase) deficiency."
Matsuura T., Chinen Y., Arashiro R., Katsuren K., Tamura T., Hyakuna N., Ohta T.
Mol. Genet. Metab. 76:207-210(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FBPD SER-194 AND ARG-284.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs
Wikipedia

Fructose bisphosphatase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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 expand/collapse EMBL AC list , 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. Translation: CAH72692.1.
BC012927 mRNA. Translation: AAH12927.1.
U47919 mRNA. Translation: AAA89098.1.
U47918 mRNA. Translation: AAA89097.1.
CCDSCCDS6712.1.
PIRA46666.
RefSeqNP_000498.2. NM_000507.3.
NP_001121100.1. NM_001127628.1.
UniGeneHs.494496.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FTAX-ray2.30A/B/C/D2-338[»]
2FHYX-ray2.95A/D/H/L1-338[»]
2FIEX-ray2.81A/D/H/L1-338[»]
2FIXX-ray3.50A/D/H/L1-338[»]
2JJKX-ray2.00A/B/C/D1-338[»]
2VT5X-ray2.20A/B/C/D/E/F/G/H1-338[»]
2WBBX-ray2.22A/B/C/D/E/F/G/H1-338[»]
2WBDX-ray2.40A/B/C/D/E/F/G/H1-338[»]
2Y5KX-ray2.10A/B/C/D1-338[»]
2Y5LX-ray2.20A/B/C/D/E/F/G/H1-338[»]
3A29X-ray2.60A/B/C/D2-338[»]
3KBZX-ray2.45A/B/C/D2-338[»]
3KC0X-ray2.80A/B/C/D2-338[»]
3KC1X-ray2.25A/B/C/D2-338[»]
4MJOX-ray2.40A/B/C/D/E/F/G/H1-338[»]
ProteinModelPortalP09467.
SMRP09467. Positions 10-336.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108497. 20 interactions.
IntActP09467. 17 interactions.
MINTMINT-3006780.
STRING9606.ENSP00000364475.

Chemistry

BindingDBP09467.
ChEMBLCHEMBL3975.
DrugBankDB00131. Adenosine monophosphate.

PTM databases

PhosphoSiteP09467.

Polymorphism databases

DMDM311033495.

Proteomic databases

MaxQBP09467.
PaxDbP09467.
PRIDEP09467.

Protocols and materials databases

DNASU2203.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375326; ENSP00000364475; ENSG00000165140.
ENST00000415431; ENSP00000408025; ENSG00000165140.
GeneID2203.
KEGGhsa:2203.
UCSCuc004auw.4. human.

Organism-specific databases

CTD2203.
GeneCardsGC09M097365.
H-InvDBHIX0008191.
HGNCHGNC:3606. FBP1.
HPAHPA005857.
HPA012513.
MIM229700. phenotype.
611570. gene.
neXtProtNX_P09467.
Orphanet348. Fructose-1,6-bisphosphatase deficiency.
PharmGKBPA28018.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0158.
HOGENOMHOG000191265.
HOVERGENHBG005627.
InParanoidP09467.
KOK03841.
OMASSFTTCV.
OrthoDBEOG7GJ6D9.
PhylomeDBP09467.
TreeFamTF314824.

Enzyme and pathway databases

BioCycMetaCyc:HS09189-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKP09467.
UniPathwayUPA00138.

Gene expression databases

ArrayExpressP09467.
BgeeP09467.
CleanExHS_FBP1.
GenevestigatorP09467.

Family and domain databases

HAMAPMF_01855. FBPase_class1.
InterProIPR000146. FBPase_class-1/SBPase.
IPR028343. FBPtase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
PANTHERPTHR11556. PTHR11556. 1 hit.
PfamPF00316. FBPase. 1 hit.
[Graphical view]
PIRSFPIRSF500210. FBPtase. 1 hit.
PIRSF000904. FBPtase_SBPase. 1 hit.
PRINTSPR00115. F16BPHPHTASE.
PROSITEPS00124. FBPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP09467.
GenomeRNAi2203.
NextBio8907.
PROP09467.
SOURCESearch...

Entry information

Entry nameF16P1_HUMAN
AccessionPrimary (citable) accession number: P09467
Secondary accession number(s): O75571, Q53F94, Q96E46
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 2, 2010
Last modified: July 9, 2014
This is version 161 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM