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P70266 (F261_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1

Short name=6PF-2-K/Fru-2,6-P2ase 1
Short name=PFK/FBPase 1
Alternative name(s):
6PF-2-K/Fru-2,6-P2ase liver isozyme

Including the following 2 domains:

  1. 6-phosphofructo-2-kinase
    EC=2.7.1.105
  2. Fructose-2,6-bisphosphatase
    EC=3.1.3.46
Gene names
Name:Pfkfb1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length471 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Synthesis and degradation of fructose 2,6-bisphosphate.

Catalytic activity

Beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.

ATP + D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate.

Enzyme regulation

Phosphorylation at Ser-33 inhibits the kinase and activates the bisphosphatase By similarity.

Subunit structure

Homodimer By similarity.

Tissue specificity

Liver.

Sequence similarities

In the C-terminal section; belongs to the phosphoglycerate mutase family.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
Kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processdephosphorylation

Inferred from sequence or structural similarity. Source: GOC

fructose 2,6-bisphosphate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

fructose metabolic process

Inferred from electronic annotation. Source: InterPro

organ regeneration

Inferred from electronic annotation. Source: Ensembl

positive regulation of glucokinase activity

Inferred from electronic annotation. Source: Ensembl

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to glucagon

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from electronic annotation. Source: Ensembl

response to starvation

Inferred from electronic annotation. Source: Ensembl

   Cellular_component6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 1 complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_function6-phosphofructo-2-kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

fructose-2,6-bisphosphate 2-phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

fructose-6-phosphate binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P70266-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P70266-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2-33: SREMGELTQTRLQKIWIPHSSSSSLLQRRRGS → MEEKASKRAA
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 4714706-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1
PRO_0000179961

Regions

Nucleotide binding49 – 579ATP By similarity
Nucleotide binding170 – 1756ATP By similarity
Nucleotide binding350 – 3534ATP By similarity
Nucleotide binding394 – 3985ATP By similarity
Region2 – 2502496-phosphofructo-2-kinase By similarity
Region251 – 471221Fructose-2,6-bisphosphatase By similarity

Sites

Active site1311 Potential
Active site1611 Potential
Active site2591Tele-phosphohistidine intermediate By similarity
Active site3281Proton donor/acceptor By similarity
Active site3931Proton donor/acceptor By similarity
Binding site821Fructose 6-phosphate By similarity
Binding site1051Fructose 6-phosphate By similarity
Binding site1331Fructose 6-phosphate By similarity
Binding site1391Fructose 6-phosphate By similarity
Binding site1751Fructose 6-phosphate By similarity
Binding site1961Fructose 6-phosphate By similarity
Binding site2001Fructose 6-phosphate By similarity
Binding site2581Fructose 2,6-bisphosphate By similarity
Binding site2651Fructose 2,6-bisphosphate By similarity
Binding site2711Fructose 2,6-bisphosphate; via amide nitrogen By similarity
Binding site3081Fructose 2,6-bisphosphate By similarity
Binding site3391Fructose 2,6-bisphosphate By similarity
Binding site3531Fructose 2,6-bisphosphate By similarity
Binding site3571Fructose 2,6-bisphosphate By similarity
Binding site3681Fructose 2,6-bisphosphate By similarity
Binding site3941Fructose 2,6-bisphosphate By similarity
Binding site3981Fructose 2,6-bisphosphate By similarity
Binding site4301ATP By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue331Phosphoserine; by PKA By similarity

Natural variations

Alternative sequence2 – 3332SREMG…RRRGS → MEEKASKRAA in isoform 2.
VSP_022168

Experimental info

Sequence conflict4601P → A in CAA67353. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 9, 2007. Version 2.
Checksum: A8EA464FB4B2DA42

FASTA47154,849
        10         20         30         40         50         60 
MSREMGELTQ TRLQKIWIPH SSSSSLLQRR RGSSIPQFTN SPTMVIMVGL PARGKTYIST 

        70         80         90        100        110        120 
KLTRYLNWIG TPTKVFNLGQ YRREAVSYRN YEFFRPDNME AQLIRKQCAL AALKDVHKYL 

       130        140        150        160        170        180 
SREEGHVAVF DATNTTRERR SLILQFAKEH GYKVFFIESI CNDPDIIAEN IKQVKLGSPD 

       190        200        210        220        230        240 
YIDCDQEKVL EDFLKRIECY EINYQPLDEE LDSHLSYIKI FDVGTRYMVN RVQDHVQSRT 

       250        260        270        280        290        300 
AYYLMNIHVT PRSIYLCRHG ESELNLRGRI GGDSGLSARG KQYAYALANF IRSQSISSLK 

       310        320        330        340        350        360 
VWTSHMKRTI QTAEALGVPY EQWKALNEID AGVCEEMTYE EIQEHYPEEF ALRDQDKYRY 

       370        380        390        400        410        420 
RYPKGESYED LVQRLEPVIM ELERQENVLV ICHQAVMRCL LAYFLDKSSD ELPYLKCPLH 

       430        440        450        460        470 
TVLKLTPVAY GCRVESIYLN VEAVNTHRDK PENVDITREP EEALDTVPAH Y 

« Hide

Isoform 2 [UniParc].

Checksum: E1BCE0322914BC2F
Show »

FASTA44952,244

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Head.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"Molecular cloning and tissue-specific expression of mouse kidney 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."
Batra R.S., Brown R.M., Brown G.K., Craig I.W.
FEBS Lett. 393:167-173(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 402-471 (ISOFORM 1).
Strain: BALB/c.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK132629 mRNA. Translation: BAE21271.1.
AL672150 Genomic DNA. Translation: CAM21428.1.
X98848 mRNA. Translation: CAA67353.1.
CCDSCCDS30464.1. [P70266-2]
PIRS74243.
RefSeqNP_032850.1. NM_008824.3.
XP_006528818.1. XM_006528755.1. [P70266-1]
UniGeneMm.249131.

3D structure databases

ProteinModelPortalP70266.
SMRP70266. Positions 7-471.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP70266.

Proteomic databases

MaxQBP70266.
PaxDbP70266.
PRIDEP70266.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000112713; ENSMUSP00000108333; ENSMUSG00000025271. [P70266-1]
GeneID18639.
KEGGmmu:18639.

Organism-specific databases

CTD5207.
MGIMGI:107816. Pfkfb1.

Phylogenomic databases

eggNOGCOG0406.
GeneTreeENSGT00390000018751.
HOGENOMHOG000181112.
HOVERGENHBG005628.
InParanoidP70266.
KOK01103.
OMANIRGRIG.
PhylomeDBP70266.
TreeFamTF313541.

Gene expression databases

BgeeP70266.
GenevestigatorP70266.

Family and domain databases

Gene3D3.40.50.1240. 1 hit.
3.40.50.300. 1 hit.
InterProIPR003094. 6Pfruct_kin.
IPR013079. 6Phosfructo_kin.
IPR016260. Bifunct_6PFK/fruc_bisP_Ptase.
IPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR027417. P-loop_NTPase.
IPR001345. PG/BPGM_mutase_AS.
[Graphical view]
PANTHERPTHR10606. PTHR10606. 1 hit.
PfamPF01591. 6PF2K. 1 hit.
PF00300. His_Phos_1. 1 hit.
[Graphical view]
PIRSFPIRSF000709. 6PFK_2-Ptase. 1 hit.
PRINTSPR00991. 6PFRUCTKNASE.
SMARTSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
SSF53254. SSF53254. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio294618.
PROP70266.
SOURCESearch...

Entry information

Entry nameF261_MOUSE
AccessionPrimary (citable) accession number: P70266
Secondary accession number(s): A2AFN0, Q3V180
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 9, 2007
Last modified: July 9, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot