Skip Header

Contribute Send feedback
Read comments (?) or add your own

P26285 (F262_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length531 AA.
Sequence statusComplete.
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

Phosphorylation results in the activation of the kinase activity.

Subunit structure

Homodimer.

Tissue specificity

Heart.

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

Chain1 – 5315316-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2
PRO_0000179963

Regions

Nucleotide binding46 – 538ATP By similarity
Region1 – 2492496-phosphofructo-2-kinase
Region250 – 531282Fructose-2,6-bisphosphatase

Sites

Active site1291 Potential
Active site1591 Potential
Active site2581Tele-phosphohistidine intermediate
Active site3271 Potential
Active site3921Proton donor By similarity
Binding site1031Fructose-6-phosphate By similarity
Binding site1941Fructose-6-phosphate By similarity

Amino acid modifications

Modified residue4671Phosphoserine; by PKA Ref.3
Modified residue4691Phosphothreonine By similarity
Modified residue4761Phosphothreonine; by AMPK and PKC Ref.3
Modified residue4841Phosphoserine By similarity
Modified residue4941Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P26285 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: E5090BBFD10BC594

FASTA53160,811
        10         20         30         40         50         60 
MSGNPASSSE QNNNSYETKA SLRISEKKCS WASYMTNSPT LIVMIGLPAR GKTYVSKKLT 

        70         80         90        100        110        120 
RYLNWIGVPT KVFNLGVYRR QAVKSYKSYD FFRHDNEEAM KIRKQCALVA LKDVKAYLTE 

       130        140        150        160        170        180 
ESGQIAVFDA TNTTRERRDL ILNFAEENSF KVFFVESVCD DPDVIAANIL EVKVSSPDYP 

       190        200        210        220        230        240 
ERNRENVMDD FLKRIECYKV TYQPLDPDSH DKDLSFIKVI NVGQRFLVNK VQDYIQSKIV 

       250        260        270        280        290        300 
YYLMNIHVHP RTIYLCRHGE SEFNLLGKIG GDSGLSVRGK QFAQALRKFL EEQEIADLKV 

       310        320        330        340        350        360 
WTSQLKRTIQ TAESLGVTYE QWKILNEIDA GVCEEMTYAE IQEQYPDEFA LRDEEKYLYR 

       370        380        390        400        410        420 
YPGGESYQDL VQRLEPVIME LERQGNVLVI SHQAVMRCLL AYFLDKGADE LPYLRCPLHT 

       430        440        450        460        470        480 
IFKLTPVAYG CKVETIKLNV EAVNTHRDKP TNNFPKSQTP VRMRRNSFTP LSSSNTIRRP 

       490        500        510        520        530 
RNYSVGSRPL QPLSPLRALD TQEGADQPKT QAETSRAAHR LPSPAPPTSP S

« Hide

References

[1]"Bovine heart fructose-6-phosphate 2-kinase/fructose-2,6-bisphosphatase: complete amino acid sequence and localization of phosphorylation sites."
Sakata J., Uyeda K.
Proc. Natl. Acad. Sci. U.S.A. 87:4951-4955(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[2]"Bovine heart fructose 6-P,2-kinase:fructose 2,6-bisphosphatase mRNA and gene structure."
Tsuchiya Y., Uyeda K.
Arch. Biochem. Biophys. 310:467-474(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[3]"Phosphorylation of myocardial fructose-6-phosphate,2-kinase: fructose-2,6-bisphosphatase by cAMP-dependent protein kinase and protein kinase C. Activation by phosphorylation and amino acid sequences of the phosphorylation sites."
Kitamura K., Kangawa K., Matsuo H., Uyeda K.
J. Biol. Chem. 263:16796-16801(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 464-480, PHOSPHORYLATION AT SER-467 AND THR-476.
Tissue: Heart.
[4]"Catalytic site of rat liver and bovine heart fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase. Identification of fructose 6-phosphate binding site."
Kitamura K., Uyeda K., Hartman F.C., Kangawa K., Matsuo H.
J. Biol. Chem. 264:6344-6348(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 104-112; 189-204 AND 416-432.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M34241 mRNA. Translation: AAA30523.1.
S70453 mRNA. Translation: AAB30689.2.
IPIIPI00709752.
PIRA31780. S44388.
RefSeqNP_777237.3. NM_174812.4.
UniGeneBt.3949.

3D structure databases

ProteinModelPortalP26285.
SMRP26285. Positions 37-449.
ModBaseSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000002753.

Proteomic databases

PRIDEP26285.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000002753; ENSBTAP00000002753; ENSBTAG00000002126.
GeneID287019.
KEGGbta:287019.

Organism-specific databases

CTD5208.

Phylogenomic databases

eggNOGCOG0406.
GeneTreeENSGT00390000018751.
HOGENOMHOG000181112.
HOVERGENHBG005628.
InParanoidP26285.
KOK01103.
OMAALDMQEG.
OrthoDBEOG408N7S.

Enzyme and pathway databases

BRENDA3.1.3.46. 908.
SABIO-RKP26285.

Gene expression databases

ArrayExpressP26285.

Family and domain databases

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

Other

NextBio20806542.

Entry information

Entry nameF262_BOVIN
AccessionPrimary (citable) accession number: P26285
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 108 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents