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UniProtKB/Swiss-Prot entry O00757


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name F16P2_HUMAN
Primary accession number O00757
Secondary accession numbers Q17R39 Q6FI53
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on September 27, 2005 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 67)
Name and origin of the protein
Protein name Fructose-1,6-bisphosphatase isozyme 2
Synonyms FBPase 2
EC 3.1.3.11
D-fructose-1,6-bisphosphate 1-phosphohydrolase 2
Gene name
Name: FBP2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-86.
TISSUE=Skeletal muscle;
DOI=10.1016/S0378-1119(98)00181-4; PubMed=9678974 [NCBI, ExPASy, EBI, Israel, Japan]
Tillman H., Eschrich K.;
"Isolation and characterization of an allelic cDNA for human muscle fructose-1,6-bisphosphatase.";
Gene 212:295-304(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02465; PubMed=15164053 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-86.
TISSUE=Colon;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y10812; CAA71772.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR536483; CAG38722.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161728; CAH72694.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC113632; AAI13633.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC117477; AAI17478.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_003828.2; -.
UniGene Hs.61255
3D structure databases
HSSP P09467; 1FTA. [HSSP ENTRY / PDB]
SMR O00757; 9-335.
ModBase O00757.
Protein-protein interaction databases
IntAct O00757; 1.
PTM databases
PhosphoSite O00757; -.
Enzyme and pathway databases
Reactome REACT_1709; Metabolism of small molecules.
Organism-specific databases
H-InvDB HIX0034872; -.
HGNC HGNC:3607; FBP2.
GenAtlas FBP2.
HPA HPA012513; -.
MIM 603027; gene. [NCBI / EBI]
PharmGKB PA28019; -.
GeneCards O00757.
Gene expression databases
ArrayExpress O00757; -.
CleanEx HS_FBP2; -.
GermOnline ENSG00000130957; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0042132; Molecular function: fructose 1,6-bisphosphate 1-phosphatase activity (inferred from electronic annotation from EC).
GO:0004331; Molecular function: fructose-2,6-bisphosphate 2-phosphatase activity (traceable author statement from ProtInc).
GO:0006000; Biological process: fructose metabolic process (traceable author statement from ProtInc).
GO:0006094; Biological process: gluconeogenesis (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000146; In_FB_phphtase.
Graphical view of domain structure.
PANTHER PTHR11556; In_FB_phphtase; 1.
Pfam PF00316; FBPase; 1.
Pfam graphical view of domain structure.
PRINTS PR00115; FBPHPHTASE.
PR00377; INFBPHPHTASE.
ProDom PD001491; In_FB_phphtase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00124; FBPASE; 1.
Proteomics databases
PRIDE O00757; -.
Genome annotation databases
Ensembl ENSG00000130957; Homo sapiens. [Contig view]
GeneID 8789; -.
KEGG hsa:8789; -.
NMPDR fig|9606.3.peg.31580; -.
Phylogenomic databases
HOGENOM O00757; -.
HOVERGEN O00757; -.
Other
LinkHub O00757; -.
NextBio 32964; -.
SOURCE FBP2; Homo sapiens.
ProtoNet O00757.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Carbohydrate metabolism; Gluconeogenesis; Hydrolase; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   339  339     Fructose-1,6-bisphosphatase isozyme 2. PRO_0000200504
ACT_SITE   275   275        By similarity. 
MOD_RES   216   216        Phosphotyrosine. 
VARIANT   86    86  1     V -> L (in dbSNP:rs573212 [NCBI]). VAR_024448 [3D]
Sequence information
Length: 339 AA [This is the length of the unprocessed precursor] Molecular weight: 36743 Da [This is the MW of the unprocessed precursor] CRC64: 196B06D744710BC4 [This is a checksum on the sequence]
        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 

O00757 in FASTA format

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