FBP1

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.2 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.

K_M=
2.7 µM for fructose 1,6-biphosphate
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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: CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLN-70.

Pathwayⁱ: gluconeogenesis

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	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	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

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cellular response to drug
Source: UniProtKB
Inferred from direct assayⁱ
- 16442285
- 18650089
cellular response to magnesium ion
Source: UniProtKB
Inferred from direct assayⁱ
- 10222032
dephosphorylation
Source: UniProtKB
Inferred from direct assayⁱ
- 18650089
- 8387495
fructose 1,6-bisphosphate metabolic process
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
fructose 6-phosphate metabolic process
Source: UniProtKB
Inferred from direct assayⁱ
- 16442285
- 8387495
fructose metabolic process
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
gluconeogenesis
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 19259699
- 20096900
negative regulation of cell growth
Source: UniProtKB
Inferred from direct assayⁱ
- 19881551
negative regulation of glycolytic process
Source: UniProtKB
Inferred from direct assayⁱ
- 19881551
negative regulation of Ras protein signal transduction
Source: UniProtKB
Inferred from direct assayⁱ
- 19881551
negative regulation of transcription by RNA polymerase II
Source: CAFA
Inferred from mutant phenotypeⁱ
- 25043030
protein homotetramerization
Source: UniProtKB
Inferred from direct assayⁱ
- 16442285
- 18650089
regulation of gluconeogenesis
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 7558035
sucrose biosynthetic process
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

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
Reactomeⁱ	R-HSA-70263 Gluconeogenesis
SABIO-RKⁱ	P09467
UniPathwayⁱ	UPA00138

Protein family/group databases

MoonProtⁱ	P09467

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	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 9

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000165140.9
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:3606 FBP1
MIMⁱ	611570 gene
neXtProtⁱ	NX_P09467

Subcellular locationⁱ

GO - Cellular component

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.

Mutagenesis

Feature key	Position(s)	DescriptionActions	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 mutation

Organism-specific databases

DisGeNET More...DisGeNETⁱ	2203
MalaCards human disease database More...MalaCardsⁱ	FBP1
MIMⁱ	229700 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000165140
Orphanetⁱ	348 Fructose-1,6-bisphosphatase deficiency
PharmGKBⁱ	PA28018

Chemistry databases

ChEMBLⁱ	CHEMBL3975
Drug and drug target database More...DrugBankⁱ	DB08484 4-AMINO-N-[(2-SULFANYLETHYL)CARBAMOYL]BENZENESULFONAMIDE DB00131 Adenosine monophosphate DB04493 Fructose-6-Phosphate DB05053 MB07803 DB04175 Mdl-29951

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	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, Phosphoprotein

Proteomic databases

EPDⁱ	P09467
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P09467
PaxDbⁱ	P09467
PeptideAtlas More...PeptideAtlasⁱ	P09467
PRIDEⁱ	P09467
ProteomicsDBⁱ	52223

PTM databases

DEPODⁱ	P09467
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 153 organ(s), highest expression level in right lobe of liver
CleanExⁱ	HS_FBP1
ExpressionAtlasⁱ	P09467 baseline and differential
Genevisibleⁱ	P09467 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB033869 HPA005857 HPA012513

HPAⁱ

CAB033869
HPA005857
HPA012513

Interactionⁱ

Subunit structureⁱ

Homotetramer.4 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
itself		12	EBI-712740,EBI-712740
BIN1	O00499	4	EBI-712740,EBI-719094
EPAS1	Q99814	4	EBI-712740,EBI-447470
FBP2	O00757	14	EBI-712740,EBI-719781
HIF1A	Q16665	5	EBI-712740,EBI-447269

GO - Molecular functionⁱ

identical protein binding
Source: IntAct
Inferred from physical interactionⁱ

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	108497, 31 interactors
Database of interacting proteins More...DIPⁱ	DIP-46677N
IntActⁱ	P09467, 39 interactors
Molecular INTeraction database More...MINTⁱ	P09467
STRINGⁱ	9606.ENSP00000364475

Chemistry databases

BindingDBⁱ

P09467

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	14 – 24	Combined sources	11
Helixⁱ	30 – 49	Combined sources	20
Turnⁱ	50 – 53	Combined sources	4
Helixⁱ	54 – 57	Combined sources	4
Turnⁱ	58 – 61	Combined sources	4
Helixⁱ	74 – 87	Combined sources	14
Turnⁱ	88 – 90	Combined sources	3
Beta strandⁱ	92 – 97	Combined sources	6
Helixⁱ	108 – 110	Combined sources	3
Beta strandⁱ	111 – 122	Combined sources	12
Helixⁱ	124 – 129	Combined sources	6
Beta strandⁱ	133 – 141	Combined sources	9
Beta strandⁱ	144 – 147	Combined sources	4
Helixⁱ	150 – 153	Combined sources	4
Helixⁱ	157 – 159	Combined sources	3
Beta strandⁱ	161 – 178	Combined sources	18
Beta strandⁱ	181 – 188	Combined sources	8
Turnⁱ	189 – 192	Combined sources	4
Beta strandⁱ	193 – 198	Combined sources	6
Beta strandⁱ	208 – 212	Combined sources	5
Helixⁱ	214 – 219	Combined sources	6
Helixⁱ	222 – 232	Combined sources	11
Beta strandⁱ	235 – 237	Combined sources	3
Helixⁱ	249 – 259	Combined sources	11
Beta strandⁱ	262 – 265	Combined sources	4
Beta strandⁱ	269 – 271	Combined sources	3
Beta strandⁱ	275 – 277	Combined sources	3
Turnⁱ	278 – 281	Combined sources	4
Helixⁱ	282 – 291	Combined sources	10
Beta strandⁱ	295 – 297	Combined sources	3
Beta strandⁱ	299 – 302	Combined sources	4
Helixⁱ	303 – 305	Combined sources	3
Beta strandⁱ	317 – 321	Combined sources	5
Helixⁱ	322 – 334	Combined sources	13

Show more details

3D structure databases

ProteinModelPortalⁱ	P09467
SMRⁱ	P09467
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P09467

EvolutionaryTraceⁱ

P09467

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	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 COG0158 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000015513
HOGENOMⁱ	HOG000191265
HOVERGENⁱ	HBG005627
InParanoidⁱ	P09467
KEGG Orthology (KO) More...KOⁱ	K03841
OMAⁱ	QSGLVCR
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0AZP
PhylomeDBⁱ	P09467
TreeFamⁱ	TF314824

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00354 FBPase, 1 hit
HAMAPⁱ	MF_01855 FBPase_class1, 1 hit
InterProⁱ	View protein in InterPro IPR000146 FBPase_class-1 IPR033391 FBPase_N IPR028343 FBPtase IPR020548 Fructose_bisphosphatase_AS
PANTHERⁱ	PTHR11556 PTHR11556, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00316 FBPase, 1 hit
PIRSFⁱ	PIRSF500210 FBPtase, 1 hit PIRSF000904 FBPtase_SBPase, 1 hit
PRINTSⁱ	PR00115 F16BPHPHTASE
PROSITEⁱ	View protein in PROSITE PS00124 FBPASE, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

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

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show all Align All

P09467-1 [UniParc]FASTA Add 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

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	Q5VZC3	Q5VZC3_HUMAN		Fructose-1,6-bisphosphatase 1 Fructose-1,6-bisphosphatase 1	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	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	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 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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS6712.1
PIRⁱ	A46666
NCBI Reference Sequences More...RefSeqⁱ	NP_000498.2, NM_000507.3 NP_001121100.1, NM_001127628.1
UniGeneⁱ	Hs.494496

Genome annotation databases

Ensemblⁱ	ENST00000375326; ENSP00000364475; ENSG00000165140 ENST00000415431; ENSP00000408025; ENSG00000165140
GeneIDⁱ	2203
KEGGⁱ	hsa:2203
UCSC genome browser More...UCSCⁱ	uc004auw.5 human

Keywords - Coding sequence diversityⁱ

Polymorphism

Protein	Similar proteins		Species	Score	Length	Source
P09467	Fructose-1,6-bisphosphatase 1 (Fragment)		HUMAN		151	UniRef100_P09467
UPI0003EAE7B0		HUMAN		256

Protein	Similar proteins		Species	Score	Length	Source
P09467	Fructose-1,6-bisphosphatase 1	)	PIG		338	UniRef90_P09467
Fructose-1,6-bisphosphatase 1	)	RABIT		338
Fructose-1,6-bisphosphatase 1 (Fragment)		HUMAN		151
Uncharacterized protein		RHIRO		409
FBP1 isoform 2 (Fragment)		PONAB		151
+106

Protein	Similar proteins		Species	Score	Length	Source
P09467	Fructose-1,6-bisphosphatase 1	)	RABIT		338	UniRef50_P09467
Fructose-1,6-bisphosphatase 1	)	PIG		338
Fructose-1,6-bisphosphatase 1		RAT		363
Fructose-1,6-bisphosphatase 1		MOUSE		338
Fructose-1,6-bisphosphatase isozyme 2	)	HUMAN		339
+852

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 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
UniGeneⁱ	Hs.494496

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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	[»]
ProteinModelPortalⁱ	P09467
SMRⁱ	P09467
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	108497, 31 interactors
DIPⁱ	DIP-46677N
IntActⁱ	P09467, 39 interactors
MINTⁱ	P09467
STRINGⁱ	9606.ENSP00000364475

Chemistry databases

BindingDBⁱ	P09467
ChEMBLⁱ	CHEMBL3975
DrugBankⁱ	DB08484 4-AMINO-N-[(2-SULFANYLETHYL)CARBAMOYL]BENZENESULFONAMIDE DB00131 Adenosine monophosphate DB04493 Fructose-6-Phosphate DB05053 MB07803 DB04175 Mdl-29951

Protein family/group databases

MoonProtⁱ	P09467

MoonProtⁱ

P09467

PTM databases

DEPODⁱ	P09467
iPTMnetⁱ	P09467
PhosphoSitePlusⁱ	P09467

Polymorphism and mutation databases

BioMutaⁱ	FBP1
DMDMⁱ	311033495

Proteomic databases

EPDⁱ	P09467
MaxQBⁱ	P09467
PaxDbⁱ	P09467
PeptideAtlasⁱ	P09467
PRIDEⁱ	P09467
ProteomicsDBⁱ	52223

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	2203
Structural Biology Knowledgebase	Search...

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
H-InvDBⁱ	HIX0008191
HGNCⁱ	HGNC:3606 FBP1
HPAⁱ	CAB033869 HPA005857 HPA012513
MalaCardsⁱ	FBP1
MIMⁱ	229700 phenotype 611570 gene
neXtProtⁱ	NX_P09467
OpenTargetsⁱ	ENSG00000165140
Orphanetⁱ	348 Fructose-1,6-bisphosphatase deficiency
PharmGKBⁱ	PA28018
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG1458 Eukaryota COG0158 LUCA
GeneTreeⁱ	ENSGT00390000015513
HOGENOMⁱ	HOG000191265
HOVERGENⁱ	HBG005627
InParanoidⁱ	P09467
KOⁱ	K03841
OMAⁱ	QSGLVCR
OrthoDBⁱ	EOG091G0AZP
PhylomeDBⁱ	P09467
TreeFamⁱ	TF314824

Enzyme and pathway databases

UniPathwayⁱ	UPA00138
BioCycⁱ	MetaCyc:HS09189-MONOMER
BRENDAⁱ	3.1.3.11 2681
Reactomeⁱ	R-HSA-70263 Gluconeogenesis
SABIO-RKⁱ	P09467

Miscellaneous databases

ChiTaRSⁱ	FBP1 human
EvolutionaryTraceⁱ	P09467
GenomeRNAiⁱ	2203
Protein Ontology More...PROⁱ	PR:P09467
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000165140 Expressed in 153 organ(s), highest expression level in right lobe of liver
CleanExⁱ	HS_FBP1
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 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
PIRSFⁱ	PIRSF500210 FBPtase, 1 hit PIRSF000904 FBPtase_SBPase, 1 hit
PRINTSⁱ	PR00115 F16BPHPHTASE
PROSITEⁱ	View protein in PROSITE PS00124 FBPASE, 1 hit
ProtoNetⁱ	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:	November 7, 2018
	This is version 203 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
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
Human chromosome 9
Human chromosome 9: entries, gene names and cross-references to MIM

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UniProtKB - P09467 (F16P1_HUMAN)

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Fructose-1,6-bisphosphatase 1

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: gluconeogenesis

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GO - Biological processi

Enzyme and pathway databases

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<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytosol

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<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

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<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

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Amino acid modifications

Keywords - PTMi

Proteomic databases

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<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

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<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

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<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

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Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

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Sequence databases

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Functionⁱ

Kineticsⁱ

Pathwayⁱ: gluconeogenesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ