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P70265 (F262_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Short name=6PF-2-K/Fru-2,6-P2ase 2
Short name=PFK/FBPase 2
Alternative name(s):
6PF-2-K/Fru-2,6-P2ase heart-type 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:Pfkfb2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length519 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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

The most important regulatory mechanism of these opposing activities is by phosphorylation and dephosphorylation of the enzyme By similarity.

Subunit structure

Homodimer By similarity.

Tissue specificity

Highest levels in kidney; also found in heart, brain, spleen, lung, liver, skeletal muscle and testis.

Post-translational modification

Phosphorylation by AMPK stimulates activity By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 5195186-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2
PRO_0000179965

Regions

Nucleotide binding48 – 569ATP By similarity
Nucleotide binding170 – 1756ATP By similarity
Nucleotide binding351 – 3544ATP By similarity
Nucleotide binding395 – 3995ATP By similarity
Region2 – 2512506-phosphofructo-2-kinase
Region252 – 519268Fructose-2,6-bisphosphatase

Sites

Active site1311 Potential
Active site1611 Potential
Active site2601Tele-phosphohistidine intermediate By similarity
Active site3291Proton donor/acceptor By similarity
Active site3941Proton donor/acceptor By similarity
Binding site811Fructose 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 site2591Fructose 2,6-bisphosphate By similarity
Binding site2661Fructose 2,6-bisphosphate By similarity
Binding site2721Fructose 2,6-bisphosphate; via amide nitrogen By similarity
Binding site3091Fructose 2,6-bisphosphate By similarity
Binding site3401Fructose 2,6-bisphosphate By similarity
Binding site3541Fructose 2,6-bisphosphate By similarity
Binding site3581Fructose 2,6-bisphosphate By similarity
Binding site3691Fructose 2,6-bisphosphate By similarity
Binding site3951Fructose 2,6-bisphosphate By similarity
Binding site3991Fructose 2,6-bisphosphate By similarity
Binding site4311ATP By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue321Phosphoserine; by PKA By similarity
Modified residue4691Phosphoserine; by AMPK and PKA
Modified residue4711Phosphothreonine By similarity
Modified residue4781Phosphothreonine; by PKC By similarity
Modified residue4861Phosphoserine By similarity
Modified residue4961Phosphoserine By similarity

Experimental info

Sequence conflict91T → P in AAH18418. Ref.2
Sequence conflict121Missing in AAH18418. Ref.2
Sequence conflict2221M → I in AAH18418. Ref.2
Sequence conflict4961S → K in CAA67352. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P70265 [UniParc].

Last modified September 1, 2009. Version 2.
Checksum: FD4CF41AEDF22F89

FASTA51959,925
        10         20         30         40         50         60 
MSENSTFSTE DSCNSSYKPH ASNLRRAGKT CSWASYMTNS PTLIVMIGLP ARGKTYVSKK 

        70         80         90        100        110        120 
LTRYLNWIGV PTKVFNLGVY RREAVKSYQS YDFFRHDNEE AMKIRKQCAL VALEDVKAYF 

       130        140        150        160        170        180 
TEESGQIAVF DATNTTRERR DMILNFAKQN AFKVFFVESV CDDPDVIAAN ILEVKVSSPD 

       190        200        210        220        230        240 
YPERNRENVM EDFLKRIECY KVTYQPLDPD NYDKDLSFIK VMNVGQRFLV NRVQDYIQSK 

       250        260        270        280        290        300 
IVYYLMNIHV HPRTIYLCRH GESEFNLLGK IGGDSGLSVR GKQFAHALKK FLEEQEIQDL 

       310        320        330        340        350        360 
KVWTSQLKRT IQTAESLGVT YEQWKILNEI DAGVCEEMTY SEIEQRYPEE FALRDQEKYL 

       370        380        390        400        410        420 
YRYPGGESYQ DLVQRLEPVI MELERQGNIL VISHQAVMRC LLAYFLDKGA DELPYLRCPL 

       430        440        450        460        470        480 
HIIFKLTPVA YGCKVETITL NVDAVDTHRD KPTHNFPKSQ TPVRMRRNSF TPLSSSNTIR 

       490        500        510 
RPRNYSVGSR PLKPLSPLRA LDMQEGADQP KTQVSIPVV 

« Hide

References

« Hide 'large scale' references
[1]"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].
Strain: BALB/c.
Tissue: Kidney.
[2]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X98847 mRNA. Translation: CAA67352.1.
BC018418 mRNA. Translation: AAH18418.1.
PIRS74242.
RefSeqNP_032851.2. NM_008825.4.
UniGeneMm.249861.

3D structure databases

ProteinModelPortalP70265.
SMRP70265. Positions 40-451.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202123. 1 interaction.
IntActP70265. 2 interactions.
STRING10090.ENSMUSP00000066426.

PTM databases

PhosphoSiteP70265.

Proteomic databases

PaxDbP70265.
PRIDEP70265.

Protocols and materials databases

DNASU18640.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID18640.
KEGGmmu:18640.

Organism-specific databases

CTD5208.
MGIMGI:107815. Pfkfb2.

Phylogenomic databases

eggNOGCOG0406.
HOGENOMHOG000181112.
HOVERGENHBG005628.
InParanoidP70265.
KOK01103.
PhylomeDBP70265.

Enzyme and pathway databases

BRENDA3.1.3.46. 3474.

Gene expression databases

GenevestigatorP70265.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003094. 6Pfruct_kin.
IPR013079. 6Phosfructo_kin.
IPR016260. Bifunct_6PFK/fruc_bisP_Ptase.
IPR013078. His_Pase_superF_clade-1.
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.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio294622.
PROP70265.
SOURCESearch...

Entry information

Entry nameF262_MOUSE
AccessionPrimary (citable) accession number: P70265
Secondary accession number(s): Q8VEI9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 1, 2009
Last modified: April 16, 2014
This is version 127 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