P09467 (F16P1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Gene names

Name:	FBP1
Synonyms:	FBP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
Cofactor	Binds 3 magnesium ions per subunit By similarity. Ref.11 Ref.12
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.13 Ref.14 Ref.15
Pathway	Carbohydrate biosynthesis; gluconeogenesis.
Subunit structure	Homotetramer. Ref.12 Ref.13 Ref.14 Ref.15
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.16 Ref.17
Sequence similarities	Belongs to the FBPase class 1 family.
Sequence caution	The sequence AAC50207.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Gluconeogenesis
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
PTM	Acetylation
Technical term	3D-structure Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to drug Inferred from direct assay Ref.14Ref.15. Source: UniProtKB cellular response to magnesium ion Inferred from direct assay Ref.5. Source: UniProtKB fructose 6-phosphate metabolic process Inferred from direct assay Ref.14Ref.2. Source: UniProtKB fructose metabolic process Traceable author statement Ref.4. Source: ProtInc gluconeogenesis Inferred from mutant phenotype PubMed 19259699PubMed 20096900. Source: UniProtKB 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 glycolysis Inferred from direct assay PubMed 19881551. Source: UniProtKB protein homotetramerization Inferred from direct assay Ref.14Ref.15. Source: UniProtKB regulation of gluconeogenesis Inferred from mutant phenotype Ref.4. Source: UniProtKB small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	AMP binding Inferred from direct assay Ref.5Ref.15Ref.2. Source: UniProtKB fructose 1,6-bisphosphate 1-phosphatase activity Inferred from direct assay Ref.14Ref.15Ref.2. Source: UniProtKB metal ion binding Inferred from mutant phenotype Ref.2. Source: UniProtKB monosaccharide binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BIN1	O00499	4	EBI-712740,EBI-719094

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 338

337

Fructose-1,6-bisphosphatase 1

PRO_0000200498

Regions

Nucleotide binding

18 – 22

5

AMP

Nucleotide binding

28 – 32

5

AMP

Nucleotide binding

113 – 114

2

AMP

Region

122 – 125

4

Substrate binding

Region

213 – 216

4

Substrate binding

Region

244 – 249

6

Substrate binding

Region

275 – 277

3

Substrate binding

Sites

Metal binding

69

1

Magnesium 1 By similarity

Metal binding

98

1

Magnesium 1 By similarity

Metal binding

98

1

Magnesium 2

Metal binding

119

1

Magnesium 2

Metal binding

119

1

Magnesium 3

Metal binding

121

1

Magnesium 2; via carbonyl oxygen

Metal binding

122

1

Magnesium 3

Metal binding

281

1

Magnesium 3

Binding site

141

1

AMP

Binding site

265

1

Substrate

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Natural variations

Natural variant

164

1

G → S in FBPD. Ref.16

VAR_002380

Natural variant

177

1

A → D in FBPD. Ref.16

VAR_002381

Natural variant

194

1

F → S in FBPD. Ref.17

VAR_038812

Natural variant

218

1

R → K. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7
Corresponds to variant rs1769259 [ dbSNP | Ensembl ].

VAR_022212

Natural variant

233

1

F → I. Ref.7
Corresponds to variant rs2297085 [ dbSNP | Ensembl ].

VAR_022213

Natural variant

255

1

R → L. Ref.7
Corresponds to variant rs28369761 [ dbSNP | Ensembl ].

VAR_022214

Natural variant

284

1

P → R in FBPD. Ref.17

VAR_038813

Natural variant

325

1

V → A. Ref.16

VAR_002382

Experimental info

Mutagenesis

119

1

D → A: Reduced activity. Ref.2

Mutagenesis

122

1

D → A: Reduced activity. Ref.2

Sequence conflict

215

1

G → A in AAA35817. Ref.2

Sequence conflict

215

1

G → A in AAC25774. Ref.5

Sequence conflict

337

1

A → G in AAC25774. Ref.5

Secondary structure

1

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338

Helix Strand Turn

Details...

Helix

14 – 24

11

Helix

30 – 49

20

Turn

50 – 53

4

Helix

54 – 57

4

Turn

58 – 61

4

Helix

74 – 87

14

Turn

88 – 90

3

Beta strand

92 – 97

6

Helix

108 – 110

3

Beta strand

111 – 122

12

Helix

124 – 129

6

Beta strand

133 – 141

9

Beta strand

144 – 147

4

Helix

150 – 153

4

Helix

157 – 159

3

Beta strand

161 – 178

18

Beta strand

181 – 188

8

Turn

189 – 192

4

Beta strand

193 – 198

6

Beta strand

208 – 212

5

Helix

214 – 219

6

Helix

222 – 232

11

Beta strand

235 – 237

3

Helix

249 – 259

11

Beta strand

262 – 265

4

Beta strand

269 – 271

3

Beta strand

275 – 277

3

Turn

278 – 281

4

Helix

282 – 291

10

Beta strand

295 – 297

3

Beta strand

299 – 302

4

Helix

303 – 305

3

Beta strand

317 – 321

5

Helix

322 – 334

13

Sequences

	Sequence		Length	Mass (Da)
	P09467 [UniParc]. Last modified November 2, 2010. Version 5. Checksum: B3D270BCBB358B71	FASTA	338	36,842
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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

GeneReviews

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 , 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.

IPI

IPI00073772.

PIR

A46666.

RefSeq

NP_000498.2. NM_000507.3.
NP_001121100.1. NM_001127628.1.

UniGene

Hs.494496.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P09467.

SMR

P09467. Positions 10-336.

ModBase

Search...

Protein-protein interaction databases

IntAct

P09467. 11 interactions.

MINT

MINT-3006780.

STRING

9606.ENSP00000364475.

PTM databases

PhosphoSite

P09467.

Polymorphism databases

DMDM

311033495.

Proteomic databases

PaxDb

P09467.

PRIDE

P09467.

Protocols and materials databases

DNASU

2203.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000375326; ENSP00000364475; ENSG00000165140.
ENST00000415431; ENSP00000408025; ENSG00000165140.

GeneID

2203.

KEGG

hsa:2203.

UCSC

uc004auw.4. human.

Organism-specific databases

CTD

2203.

GeneCards

GC09M097365.

H-InvDB

HIX0008191.

HGNC

HGNC:3606. FBP1.

HPA

HPA005857.
HPA012513.

MIM

229700. phenotype.
611570. gene.

neXtProt

NX_P09467.

Orphanet

348. Fructose-1,6-bisphosphatase deficiency.

PharmGKB

PA28018.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0158.

HOGENOM

HOG000191265.

HOVERGEN

HBG005627.

InParanoid

P09467.

KO

K03841.

OMA

SSFTTCV.

OrthoDB

EOG4P8FJF.

PhylomeDB

P09467.

Enzyme and pathway databases

BioCyc

MetaCyc:HS09189-MONOMER.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P09467.

UniPathway

UPA00138.

Gene expression databases

ArrayExpress

P09467.

Bgee

P09467.

CleanEx

HS_FBP1.

Genevestigator

P09467.

GermOnline

ENSG00000165140. Homo sapiens.

Family and domain databases

InterPro

IPR000146. FBPase_class-1/SBPase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]

PANTHER

PTHR11556. PTHR11556. 1 hit.

Pfam

PF00316. FBPase. 1 hit.
[Graphical view]

PIRSF

PIRSF000904. FBPtase_SBPase. 1 hit.

PRINTS

PR00115. F16BPHPHTASE.

PROSITE

PS00124. FBPASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P09467.

ChEMBL

CHEMBL3975.

DrugBank

DB00131. Adenosine monophosphate.

EvolutionaryTrace

P09467.

GenomeRNAi

2203.

NextBio

8907.

SOURCE

Search...

Entry information

Entry name

F16P1_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 150 of the entry and version 5 of the sequence. [Complete history]

Entry status

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.