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Protein

Fructose-1,6-bisphosphatase 1

Gene

FBP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

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

Cofactori

Mg2+By similarityNote: Binds 3 Mg2+ ions per subunit.By similarity

Enzyme 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.

  1. KM=2.7 µM for fructose 1,6-biphosphate1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi69 – 691Magnesium 1By similarity
Metal bindingi98 – 981Magnesium 1By similarity
Metal bindingi98 – 981Magnesium 2
Metal bindingi119 – 1191Magnesium 2
Metal bindingi119 – 1191Magnesium 3
Metal bindingi121 – 1211Magnesium 2; via carbonyl oxygen
Metal bindingi122 – 1221Magnesium 3
Binding sitei141 – 1411AMP1 Publication
Binding sitei265 – 2651Substrate
Metal bindingi281 – 2811Magnesium 3

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 225AMP1 Publication
Nucleotide bindingi28 – 325AMP1 Publication
Nucleotide bindingi113 – 1142AMP1 Publication

GO - Molecular functioni

  1. AMP binding Source: UniProtKB
  2. fructose 1,6-bisphosphate 1-phosphatase activity Source: UniProtKB
  3. identical protein binding Source: IntAct
  4. metal ion binding Source: UniProtKB
  5. monosaccharide binding Source: UniProtKB

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. cellular response to drug Source: UniProtKB
  3. cellular response to magnesium ion Source: UniProtKB
  4. dephosphorylation Source: UniProtKB
  5. fructose 6-phosphate metabolic process Source: UniProtKB
  6. fructose metabolic process Source: ProtInc
  7. gluconeogenesis Source: UniProtKB
  8. glucose metabolic process Source: Reactome
  9. negative regulation of cell growth Source: UniProtKB
  10. negative regulation of glycolytic process Source: UniProtKB
  11. negative regulation of Ras protein signal transduction Source: UniProtKB
  12. pathogenesis Source: Reactome
  13. protein homotetramerization Source: UniProtKB
  14. regulation of gluconeogenesis Source: UniProtKB
  15. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Gluconeogenesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS09189-MONOMER.
ReactomeiREACT_1520. Gluconeogenesis.
SABIO-RKP09467.
UniPathwayiUPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-1,6-bisphosphatase 1 (EC:3.1.3.11)
Short name:
FBPase 1
Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase 1
Liver FBPase
Gene namesi
Name:FBP1
Synonyms:FBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:3606. FBP1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Fructose-1,6-bisphosphatase deficiency2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionInherited 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.

See also OMIM:229700
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti164 – 1641G → S in FBPD. 1 Publication
VAR_002380
Natural varianti177 – 1771A → D in FBPD. 1 Publication
VAR_002381
Natural varianti194 – 1941F → S in FBPD. 1 Publication
VAR_038812
Natural varianti284 – 2841P → R in FBPD. 1 Publication
VAR_038813

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi70 – 701Q → E: Increased affinity towards Ca(2+) and Mg(2+). 1 Publication
Mutagenesisi119 – 1191D → A: Reduced activity. 1 Publication
Mutagenesisi122 – 1221D → A: Reduced activity. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi229700. phenotype.
Orphaneti348. Fructose-1,6-bisphosphatase deficiency.
PharmGKBiPA28018.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity1 Publication
Chaini2 – 338337Fructose-1,6-bisphosphatase 1PRO_0000200498Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei151 – 1511N6-succinyllysineBy similarity
Modified residuei216 – 2161PhosphotyrosineBy similarity
Modified residuei265 – 2651Phosphotyrosine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP09467.
PaxDbiP09467.
PRIDEiP09467.

PTM databases

DEPODiP09467.
PhosphoSiteiP09467.

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

BgeeiP09467.
CleanExiHS_FBP1.
ExpressionAtlasiP09467. baseline and differential.
GenevestigatoriP09467.

Organism-specific databases

HPAiCAB033869.
HPA005857.
HPA012513.

Interactioni

Subunit structurei

Homotetramer.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-712740,EBI-712740
BIN1O004994EBI-712740,EBI-719094

Protein-protein interaction databases

BioGridi108497. 24 interactions.
DIPiDIP-46677N.
IntActiP09467. 34 interactions.
MINTiMINT-3006780.
STRINGi9606.ENSP00000364475.

Structurei

Secondary structure

1
338
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 2411Combined sources
Helixi30 – 4920Combined sources
Turni50 – 534Combined sources
Helixi54 – 574Combined sources
Turni58 – 614Combined sources
Helixi74 – 8714Combined sources
Turni88 – 903Combined sources
Beta strandi92 – 976Combined sources
Helixi108 – 1103Combined sources
Beta strandi111 – 12212Combined sources
Helixi124 – 1296Combined sources
Beta strandi133 – 1419Combined sources
Beta strandi144 – 1474Combined sources
Helixi150 – 1534Combined sources
Helixi157 – 1593Combined sources
Beta strandi161 – 17818Combined sources
Beta strandi181 – 1888Combined sources
Turni189 – 1924Combined sources
Beta strandi193 – 1986Combined sources
Beta strandi208 – 2125Combined sources
Helixi214 – 2196Combined sources
Helixi222 – 23211Combined sources
Beta strandi235 – 2373Combined sources
Helixi249 – 25911Combined sources
Beta strandi262 – 2654Combined sources
Beta strandi269 – 2713Combined sources
Beta strandi275 – 2773Combined sources
Turni278 – 2814Combined sources
Helixi282 – 29110Combined sources
Beta strandi295 – 2973Combined sources
Beta strandi299 – 3024Combined sources
Helixi303 – 3053Combined sources
Beta strandi317 – 3215Combined sources
Helixi322 – 33413Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP09467.
SMRiP09467. Positions 10-336.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09467.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni122 – 1254Substrate binding
Regioni213 – 2164Substrate binding
Regioni244 – 2496Substrate binding
Regioni275 – 2773Substrate binding

Sequence similaritiesi

Belongs to the FBPase class 1 family.Curated

Phylogenomic databases

eggNOGiCOG0158.
GeneTreeiENSGT00390000015513.
HOGENOMiHOG000191265.
HOVERGENiHBG005627.
InParanoidiP09467.
KOiK03841.
OMAiNGVNCFM.
OrthoDBiEOG7GJ6D9.
PhylomeDBiP09467.
TreeFamiTF314824.

Family and domain databases

HAMAPiMF_01855. FBPase_class1.
InterProiIPR000146. FBPase_class-1/SBPase.
IPR028343. FBPtase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
PANTHERiPTHR11556. PTHR11556. 1 hit.
PfamiPF00316. FBPase. 1 hit.
[Graphical view]
PIRSFiPIRSF500210. FBPtase. 1 hit.
PIRSF000904. FBPtase_SBPase. 1 hit.
PRINTSiPR00115. F16BPHPHTASE.
PROSITEiPS00124. FBPASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09467-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:338
Mass (Da):36,842
Last modified:November 2, 2010 - v5
Checksum:iB3D270BCBB358B71
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti215 – 2151G → A in AAA35817 (PubMed:8387495).Curated
Sequence conflicti215 – 2151G → A in AAC25774 (PubMed:10222032).Curated
Sequence conflicti337 – 3371A → G in AAC25774 (PubMed:10222032).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti164 – 1641G → S in FBPD. 1 Publication
VAR_002380
Natural varianti177 – 1771A → D in FBPD. 1 Publication
VAR_002381
Natural varianti194 – 1941F → S in FBPD. 1 Publication
VAR_038812
Natural varianti218 – 2181R → K.7 Publications
Corresponds to variant rs1769259 [ dbSNP | Ensembl ].
VAR_022212
Natural varianti233 – 2331F → I.1 Publication
Corresponds to variant rs2297085 [ dbSNP | Ensembl ].
VAR_022213
Natural varianti255 – 2551R → L.1 Publication
Corresponds to variant rs28369761 [ dbSNP | Ensembl ].
VAR_022214
Natural varianti284 – 2841P → R in FBPD. 1 Publication
VAR_038813
Natural varianti325 – 3251V → A.1 Publication
VAR_002382

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. Translation: CAH72692.1.
BC012927 mRNA. Translation: AAH12927.1.
U47919 mRNA. Translation: AAA89098.1.
U47918 mRNA. Translation: AAA89097.1.
CCDSiCCDS6712.1.
PIRiA46666.
RefSeqiNP_000498.2. NM_000507.3.
NP_001121100.1. NM_001127628.1.
UniGeneiHs.494496.

Genome annotation databases

EnsembliENST00000375326; ENSP00000364475; ENSG00000165140.
ENST00000415431; ENSP00000408025; ENSG00000165140.
GeneIDi2203.
KEGGihsa:2203.
UCSCiuc004auw.4. human.

Polymorphism databases

DMDMi311033495.

Keywords - Coding sequence diversityi

Polymorphism

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. Translation: CAH72692.1.
BC012927 mRNA. Translation: AAH12927.1.
U47919 mRNA. Translation: AAA89098.1.
U47918 mRNA. Translation: AAA89097.1.
CCDSiCCDS6712.1.
PIRiA46666.
RefSeqiNP_000498.2. NM_000507.3.
NP_001121100.1. NM_001127628.1.
UniGeneiHs.494496.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP09467.
SMRiP09467. Positions 10-336.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108497. 24 interactions.
DIPiDIP-46677N.
IntActiP09467. 34 interactions.
MINTiMINT-3006780.
STRINGi9606.ENSP00000364475.

Chemistry

BindingDBiP09467.
ChEMBLiCHEMBL3975.
DrugBankiDB00131. Adenosine monophosphate.

PTM databases

DEPODiP09467.
PhosphoSiteiP09467.

Polymorphism databases

DMDMi311033495.

Proteomic databases

MaxQBiP09467.
PaxDbiP09467.
PRIDEiP09467.

Protocols and materials databases

DNASUi2203.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375326; ENSP00000364475; ENSG00000165140.
ENST00000415431; ENSP00000408025; ENSG00000165140.
GeneIDi2203.
KEGGihsa:2203.
UCSCiuc004auw.4. human.

Organism-specific databases

CTDi2203.
GeneCardsiGC09M097365.
H-InvDBHIX0008191.
HGNCiHGNC:3606. FBP1.
HPAiCAB033869.
HPA005857.
HPA012513.
MIMi229700. phenotype.
611570. gene.
neXtProtiNX_P09467.
Orphaneti348. Fructose-1,6-bisphosphatase deficiency.
PharmGKBiPA28018.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0158.
GeneTreeiENSGT00390000015513.
HOGENOMiHOG000191265.
HOVERGENiHBG005627.
InParanoidiP09467.
KOiK03841.
OMAiNGVNCFM.
OrthoDBiEOG7GJ6D9.
PhylomeDBiP09467.
TreeFamiTF314824.

Enzyme and pathway databases

UniPathwayiUPA00138.
BioCyciMetaCyc:HS09189-MONOMER.
ReactomeiREACT_1520. Gluconeogenesis.
SABIO-RKP09467.

Miscellaneous databases

ChiTaRSiFBP1. human.
EvolutionaryTraceiP09467.
GenomeRNAii2203.
NextBioi8907.
PROiP09467.
SOURCEiSearch...

Gene expression databases

BgeeiP09467.
CleanExiHS_FBP1.
ExpressionAtlasiP09467. baseline and differential.
GenevestigatoriP09467.

Family and domain databases

HAMAPiMF_01855. FBPase_class1.
InterProiIPR000146. FBPase_class-1/SBPase.
IPR028343. FBPtase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
PANTHERiPTHR11556. PTHR11556. 1 hit.
PfamiPF00316. FBPase. 1 hit.
[Graphical view]
PIRSFiPIRSF500210. FBPtase. 1 hit.
PIRSF000904. FBPtase_SBPase. 1 hit.
PRINTSiPR00115. F16BPHPHTASE.
PROSITEiPS00124. FBPASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: FUNCTION.
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-265, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "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.
  17. "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.
  18. "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.
  19. "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.
  20. "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.
  21. "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.
  22. "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.

Entry informationi

Entry nameiF16P1_HUMAN
AccessioniPrimary (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: March 4, 2015
This is version 168 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.