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Primary Information | |
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| BoMiProt ID | Bomi3569 |
| Protein Name | 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2/6PF-2-K/Fru-2,6-P2ase heart-type isozyme |
| Organism | Bos taurus |
| Uniprot ID | P26285 |
| Milk Fraction | Exosomes |
| Ref Sequence ID | NP_777237.3 |
| Aminoacid Length | 531 |
| Molecular Weight | 60811 |
| FASTA Sequence | Download |
| Gene Name | PFKFB2 |
| Gene ID | 287019 |
| Protein Existence Status | Reviewed |
Secondary Information | |
| Presence in other biological fluids/tissue/cells | retina |
| Protein Function | It is a homodimeric bifunctional enzyme that catalyses the synthesis and degradation of Fru-2,6-P2. |
| Biochemical Properties | The FBPase-2 domain of the enzyme subunit bears sequence, mechanistic and structural similarity to the histidine phosphatase family of enzymes. |
| PTMs | N-Acetylation at Ser, Phosphorylation at ser/Thr |
| Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | >sp|P26285|F262_BOVIN 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2 OS=Bos taurus OX=9913 GN=PFKFB2 PE=1 SV=2 MSGNPASSSEQNNNSYETKASLRISEKKCSWASYMTNSPTLIVMIGLPARGKTYVSKKLT RYLNWIGVPTKVFNLGVYRRQAVKSYKSYDFFRHDNEEAMKIRKQCALVALKDVKAYLTE ESGQIAVFDATNTTRERRDLILNFAEENSFKVFFVESVCDDPDVIAANILEVKVSSPDYP ERNRENVMDDFLKRIECYKVTYQPLDPDSHDKDLSFIKVINVGQRFLVNKVQDYIQSKIV YYLMNIHVHPRTIYLCRHGESEFNLLGKIGGDSGLSVRGKQFAQALRKFLEEQEIADLKV WTSQLKRTIQTAESLGVTYEQWKILNEIDAGVCEEMTYAEIQEQYPDEFALRDEEKYLYR YPGGESYQDLVQRLEPVIMELERQGNVLVISHQAVMRCLLAYFLDKGADELPYLRCPLHT IFKLTPVAYGCKVETIKLNVEAVNTHRDKPTNNFPKSQTPVRMRRNS*467FT*469PLSSSNT*476IRRP RNYS*484VGSRPLQPLS*494PLRALDTQEGADQPKTQAETSRAAHRLPSPAPPTSPS |
| CATH | Matched CATH superfamily 3.40.50.1240 3.40.50.300 |
| Predicted Disorder Regions | 1-20, 446-486, 501-531 |
| DisProt Annotation | |
| TM Helix Prediction | No TM helices |
| Significance of PTMs | Phosphorylation by AMPK stimulates activity. |
| PDB ID | 5HR5, |
| Bibliography | 1.Rider MH, Bertrand L, Vertommen D, Michels PA, Rousseau GG, Hue L. 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: head-to-head with a bifunctional enzyme that controls glycolysis. Biochem J. 2004 Aug 1;381(Pt 3):561-79. doi: 10.1042/BJ20040752. PMID: 15170386; PMCID: PMC1133864. |