Reviewed, UniProtKB/Swiss-Prot O00757 (F16P2_HUMAN)

Names and originHide

Protein names

Recommended name:
Fructose-1,6-bisphosphatase isozyme 2
Short name=FBPase 2
EC=3.1.3.11

Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase 2

Gene names

Name:

FBP2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributesHide

Sequence length	339 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)Hide

Catalytic activity	D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
Cofactor	Binds 3 magnesium ions per subunit By similarity. Ref.5
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. Fructose-2,6-biphosphate acts as competitive inhibitor. Ref.5
Pathway	Carbohydrate biosynthesis; gluconeogenesis.
Subunit structure	Homotetramer By similarity.
Sequence similarities	Belongs to the FBPase class 1 family.
Biophysicochemical properties	Kinetic parameters: KM=1.3 µM for fructose-1,6-biphosphate

OntologiesHide

Keywords
Biological process	Carbohydrate metabolism Gluconeogenesis
Coding sequence diversity	Polymorphism
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Allosteric enzyme Complete proteome
Gene Ontology (GO)
Biological process	fructose metabolic process Traceable author statement. Source: ProtInc gluconeogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	fructose 1,6-bisphosphate 1-phosphatase activity Inferred from electronic annotation. Source: EC fructose-2,6-bisphosphate 2-phosphatase activity Traceable author statement. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)Hide

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 339	339	Fructose-1,6-bisphosphatase isozyme 2		PRO_0000200504
Regions
	Nucleotide binding	18 – 22	5	AMP By similarity
	Nucleotide binding	28 – 32	5	AMP By similarity
	Nucleotide binding	113 – 114	2	AMP By similarity
	Region	122 – 125	4	Substrate binding By similarity
	Region	213 – 216	4	Substrate binding By similarity
	Region	244 – 249	6	Substrate binding By similarity
	Region	275 – 277	3	Substrate binding By similarity
Sites
	Metal binding	69	1	Magnesium 1 By similarity
	Metal binding	98	1	Magnesium 1 By similarity
	Metal binding	98	1	Magnesium 2 By similarity
	Metal binding	119	1	Magnesium 2 By similarity
	Metal binding	119	1	Magnesium 3 By similarity
	Metal binding	121	1	Magnesium 2; via carbonyl oxygen By similarity
	Metal binding	122	1	Magnesium 3 By similarity
	Metal binding	281	1	Magnesium 3 By similarity
	Binding site	141	1	AMP By similarity
	Binding site	265	1	Substrate By similarity
Amino acid modifications
	Modified residue	216	1	Phosphotyrosine Ref.6
Natural variations
	Natural variant	86	1	V → L. [dbSNP:rs573212] Ref.1 Ref.4		VAR_024448
Experimental info
	Mutagenesis	21	1	K → E: Reduces sensitivity to AMP; when associated with M-178 and C-180. Ref.5
	Mutagenesis	178	1	T → M: Reduces sensitivity to AMP; when associated with E-21 and C-180. Ref.5
	Mutagenesis	180	1	Q → C: Reduces sensitivity to AMP; when associated with E-21 and M-178. Ref.5

SequencesHide

	Sequence		Length	Mass (Da)
	O00757-1 [UniParc]. Last modified September 27, 2005. Version 2. Checksum: 196B06D744710BC4	FASTA	339	36,743
	10 20 30 40 50 60 MTDRSPFETD MLTLTRYVME KGRQAKGTGE LTQLLNSMLT AIKAISSAVR KAGLAHLYGI 70 80 90 100 110 120 AGSVNVTGDE VKKLDVLSNS LVINMVQSSY STCVLVSEEN KDAIITAKEK RGKYVVCFDP 130 140 150 160 170 180 LDGSSNIDCL ASIGTIFAIY RKTSEDEPSE KDALQCGRNI VAAGYALYGS ATLVALSTGQ 190 200 210 220 230 240 GVDLFMLDPA LGEFVLVEKD VKIKKKGKIY SLNEGYAKYF DAATTEYVQK KKFPEDGSAP 250 260 270 280 290 300 YGARYVGSMV ADVHRTLVYG GIFLYPANQK SPKGKLRLLY ECNPVAYIIE QAGGLATTGT 310 320 330 QPVLDVKPEA IHQRVPLILG SPEDVQEYLT CVQKNQAGS

ReferencesHide

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of an allelic cDNA for human muscle fructose-1,6-bisphosphatase." Tillman H., Eschrich K. Gene 212:295-304(1998) [PubMed: 9678974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-86. Tissue: Skeletal muscle.
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"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: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LEU-86. Tissue: Colon.
[5]	"The origin of the high sensitivity of muscle fructose 1,6-bisphosphatase towards AMP." Rakus D., Maciaszczyk E., Wawrzycka D., Ulaszewski S., Eschrich K., Dzugaj A. FEBS Lett. 579:5577-5581(2005) [PubMed: 16213487] [Abstract] Cited for: ENZYME REGULATION, COFACTOR, MUTAGENESIS OF LYS-21; THR-178 AND GLN-180, BIOPHYSICOCHEMICAL PROPERTIES.
[6]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, MASS SPECTROMETRY. Tissue: Lung carcinoma.
+	Additional computationally mapped references.

Cross-referencesHide

Sequence databases
EMBL GenBank DDBJ	Y10812 mRNA. Translation: CAA71772.1. CR536483 mRNA. Translation: CAG38722.1. AL161728 Genomic DNA. Translation: CAH72694.1. BC113632 mRNA. Translation: AAI13633.1. BC117477 mRNA. Translation: AAI17478.1.
IPI	IPI00299456.
RefSeq	NP_003828.2.
UniGene	Hs.61255
3D structure databases
SMR	O00757. Positions 7-337.
ModBase	Search...
Protein-protein interaction databases
IntAct	O00757. 1 interaction.
MINT	MINT-1374932.
STRING	O00757.
PTM databases
PhosphoSite	O00757.
Proteomic databases
PRIDE	O00757.
Genome annotation databases
Ensembl	ENST00000375337; ENSP00000364486; ENSG00000130957; Homo sapiens. [Genome view]
GeneID	8789.
KEGG	hsa:8789.
NMPDR	fig|9606.3.peg.31580.
UCSC	uc004auv.1. human.
Organism-specific databases
CTD	8789.
GeneCards	GC09M096360.
H-InvDB	HIX0034872.
HGNC	HGNC:3607. FBP2.
HPA	HPA012513.
MIM	603027. gene.
PharmGKB	PA28019.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG10983.
HOGENOM	HBG731261.
HOVERGEN	HBG005627.
InParanoid	O00757.
OMA	ITAKEKR.
OrthoDB	EOG9Z3905.
PhylomeDB	O00757.
Enzyme and pathway databases
BRENDA	3.1.3.11. 247.
Reactome	REACT_474. Metabolism of carbohydrates.
Gene expression databases
ArrayExpress	O00757.
Bgee	O00757.
CleanEx	HS_FBP2.
Genevestigator	O00757.
GermOnline	ENSG00000130957. Homo sapiens.
Family and domain databases
InterPro	IPR000146. Fructose_bisphosphatase. IPR020548. Fructose_bisphosphatase_AS. [Graphical view]
PANTHER	PTHR11556. In_FB_phphtase. 1 hit.
Pfam	PF00316. FBPase. 1 hit. [Graphical view]
PRINTS	PR00115. F16BPHPHTASE.
PROSITE	PS00124. FBPASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	32964.
SOURCE	Search...

Entry informationHide

Entry name

F16P2_HUMAN

Accession

Primary (citable) accession number: O00757
Secondary accession number(s): Q17R39, Q6FI53

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	September 27, 2005
Last modified:	July 13, 2010
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.