P70265 (F262_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 119.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended 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:
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| Gene names |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 519 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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. |
Ontologies
| Keywords | |
|---|---|
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Hydrolase Kinase Transferase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Multifunctional enzyme Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | fructose 2,6-bisphosphate metabolic process Inferred from electronic annotation. Source: InterPro fructose metabolic processInferred from electronic annotation. Source: InterPro glycolysisInferred from sequence or structural similarity. Source: UniProtKB |
| Molecular_function | 6-phosphofructo-2-kinase activity Inferred from sequence or structural similarity. Source: UniProtKB ATP bindingInferred from electronic annotation. Source: UniProtKB-KW fructose-2,6-bisphosphate 2-phosphatase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 519 | 519 | 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2 | PRO_0000179965 | |||||
Regions | |||||||||
| Nucleotide binding | 48 – 55 | 8 | ATP Potential | ||||||
| Region | 1 – 251 | 251 | 6-phosphofructo-2-kinase | ||||||
| Region | 252 – 519 | 268 | Fructose-2,6-bisphosphatase | ||||||
Sites | |||||||||
| Active site | 131 | 1 | Potential | ||||||
| Active site | 161 | 1 | Potential | ||||||
| Active site | 260 | 1 | Tele-phosphohistidine intermediate By similarity | ||||||
| Active site | 329 | 1 | Potential | ||||||
| Active site | 394 | 1 | Proton donor By similarity | ||||||
| Binding site | 105 | 1 | Fructose-6-phosphate By similarity | ||||||
| Binding site | 196 | 1 | Fructose-6-phosphate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 32 | 1 | Phosphoserine; by PKA By similarity | ||||||
| Modified residue | 469 | 1 | Phosphoserine; by AMPK and PKA Ref.3 | ||||||
| Modified residue | 471 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 478 | 1 | Phosphothreonine; by PKC By similarity | ||||||
| Modified residue | 486 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 496 | 1 | Phosphoserine Ref.3 | ||||||
Experimental info | |||||||||
| Sequence conflict | 9 | 1 | T → P in AAH18418. Ref.2 | ||||||
| Sequence conflict | 12 | 1 | Missing in AAH18418. Ref.2 | ||||||
| Sequence conflict | 222 | 1 | M → I in AAH18418. Ref.2 | ||||||
| Sequence conflict | 496 | 1 | S → K in CAA67352. Ref.1 | ||||||
Sequences
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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]. |
| [3] | "Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469 AND SER-496, MASS SPECTROMETRY. Tissue: Melanoma. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X98847 mRNA. Translation: CAA67352.1. BC018418 mRNA. Translation: AAH18418.1. |
| IPI | IPI00137533. |
| PIR | S74242. |
| RefSeq | NP_032851.2. NM_008825.4. |
| UniGene | Mm.249861. |
3D structure databases | |
| ProteinModelPortal | P70265. |
| SMR | P70265. Positions 40-451. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P70265. 2 interactions. |
| STRING | 10090.ENSMUSP00000066426. |
PTM databases | |
| PhosphoSite | P70265. |
Proteomic databases | |
| PaxDb | P70265. |
| PRIDE | P70265. |
Protocols and materials databases | |
| DNASU | 18640. |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 18640. |
| KEGG | mmu:18640. |
Organism-specific databases | |
| CTD | 5208. |
| MGI | MGI:107815. Pfkfb2. |
Phylogenomic databases | |
| eggNOG | COG0406. |
| HOGENOM | HOG000181112. |
| HOVERGEN | HBG005628. |
| InParanoid | P70265. |
| KO | K01103. |
| OrthoDB | EOG408N7S. |
Enzyme and pathway databases | |
| BRENDA | 3.1.3.46. 3474. |
Gene expression databases | |
| Genevestigator | P70265. |
| GermOnline | ENSMUSG00000026409. Mus musculus. |
Family and domain databases | |
| InterPro | IPR003094. 6Pfruct_kin. IPR013079. 6Phosfructo_kin. IPR016260. Bifunct_6PFK/fruc_bisP_Ptase. IPR013078. His_Pase_superF_clade-1. IPR001345. PG/BPGM_mutase_AS. [Graphical view] |
| PANTHER | PTHR10606. PTHR10606. 1 hit. |
| Pfam | PF01591. 6PF2K. 1 hit. PF00300. His_Phos_1. 1 hit. [Graphical view] |
| PIRSF | PIRSF000709. 6PFK_2-Ptase. 1 hit. |
| PRINTS | PR00991. 6PFRUCTKNASE. |
| SMART | SM00855. PGAM. 1 hit. [Graphical view] |
| PROSITE | PS00175. PG_MUTASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 294622. |
| SOURCE | Search... |
Entry information
| Entry name | F262_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P70265 Secondary accession number(s): Q8VEI9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
