Q16877 · F264_HUMAN
- Protein6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4
- GenePFKFB4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids469 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Synthesis and degradation of fructose 2,6-bisphosphate.
Catalytic activity
- beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Activity regulation
The most important regulatory mechanism of these opposing activities is by phosphorylation and dephosphorylation of the enzyme.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 46-54 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GLPARGKTY | ||||||
Binding site | 79 | beta-D-fructose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 103 | beta-D-fructose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 129 | |||||
Sequence: D | ||||||
Binding site | 131 | beta-D-fructose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 137 | beta-D-fructose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 159 | |||||
Sequence: C | ||||||
Binding site | 168-173 | ATP (UniProtKB | ChEBI) | ||||
Sequence: NIVQVK | ||||||
Binding site | 173 | beta-D-fructose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 194 | beta-D-fructose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 198 | beta-D-fructose 6-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 256 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 257 | Tele-phosphohistidine intermediate | ||||
Sequence: H | ||||||
Binding site | 263 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 269 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 306 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 326 | Proton donor/acceptor | ||||
Sequence: E | ||||||
Binding site | 337 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 348-351 | ATP (UniProtKB | ChEBI) | ||||
Sequence: FALR | ||||||
Binding site | 351 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 355 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 366 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Site | 391 | Transition state stabilizer | ||||
Sequence: H | ||||||
Binding site | 392 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 392-396 | ATP (UniProtKB | ChEBI) | ||||
Sequence: QAVMR | ||||||
Binding site | 396 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 428 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | 6-phosphofructo-2-kinase activity | |
Molecular Function | ATP binding | |
Molecular Function | fructose-2,6-bisphosphate 2-phosphatase activity | |
Biological Process | fructose 2,6-bisphosphate metabolic process | |
Biological Process | fructose metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4
- Short names6PF-2-K/Fru-2,6-P2ase 4; PFK/FBPase 4
- Alternative names
Including 2 domains:
- Recommended name6-phosphofructo-2-kinase
- EC number
- Recommended nameFructose-2,6-bisphosphatase
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ16877
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_036075 | 181 | in a breast cancer sample; somatic mutation | |||
Sequence: N → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 465 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000179970 | 1-469 | UniProt | 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4 | |||
Sequence: MASPRELTQNPLKKIWMPYSNGRPALHACQRGVCMTNCPTLIVMVGLPARGKTYISKKLTRYLNWIGVPTREFNVGQYRRDVVKTYKSFEFFLPDNEEGLKIRKQCALAALRDVRRFLSEEGGHVAVFDATNTTRERRATIFNFGEQNGYKTFFVESICVDPEVIAANIVQVKLGSPDYVNRDSDEATEDFMRRIECYENSYESLDEDLDRDLSYIKIMDVGQSYVVNRVADHIQSRIVYYLMNIHVTPRSIYLCRHGESELNLKGRIGGDPGLSPRGREFAKSLAQFISDQNIKDLKVWTSQMKRTIQTAEALGVPYEQWKVLNEIDAGVCEEMTYEEIQDNYPLEFALRDQDKYRYRYPKGESYEDLVQRLEPVIMELERQENVLVICHQAVMRCLLAYFLDKAAEQLPYLKCPLHTVLKLTPVAYGCKVESIFLNVAAVNTHRDRPQNVDISRPPEEALVTVPAHQ | |||||||
Modified residue (large scale data) | 3 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 176 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 444 | UniProt | Phosphothreonine; by PKC | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Homodimer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q16877 | CCDC102B Q68D86 | 3 | EBI-764534, EBI-10171570 | |
BINARY | Q16877 | CDC23 Q9UJX2 | 3 | EBI-764534, EBI-396137 | |
BINARY | Q16877 | LRR1 Q96L50 | 3 | EBI-764534, EBI-2510106 | |
BINARY | Q16877 | PFKFB1 P16118 | 6 | EBI-764534, EBI-709807 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-249 | 6-phosphofructo-2-kinase | ||||
Sequence: MASPRELTQNPLKKIWMPYSNGRPALHACQRGVCMTNCPTLIVMVGLPARGKTYISKKLTRYLNWIGVPTREFNVGQYRRDVVKTYKSFEFFLPDNEEGLKIRKQCALAALRDVRRFLSEEGGHVAVFDATNTTRERRATIFNFGEQNGYKTFFVESICVDPEVIAANIVQVKLGSPDYVNRDSDEATEDFMRRIECYENSYESLDEDLDRDLSYIKIMDVGQSYVVNRVADHIQSRIVYYLMNIHVTP | ||||||
Region | 250-469 | Fructose-2,6-bisphosphatase | ||||
Sequence: RSIYLCRHGESELNLKGRIGGDPGLSPRGREFAKSLAQFISDQNIKDLKVWTSQMKRTIQTAEALGVPYEQWKVLNEIDAGVCEEMTYEEIQDNYPLEFALRDQDKYRYRYPKGESYEDLVQRLEPVIMELERQENVLVICHQAVMRCLLAYFLDKAAEQLPYLKCPLHTVLKLTPVAYGCKVESIFLNVAAVNTHRDRPQNVDISRPPEEALVTVPAHQ |
Sequence similarities
In the C-terminal section; belongs to the phosphoglycerate mutase family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q16877-1
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.
- Name1
- Length469
- Mass (Da)54,040
- Last updated2007-01-23 v6
- Checksum7E190C3C0A197D9F
Q16877-2
- Name2
- Differences from canonical
- 330-364: Missing
Q16877-3
- Name3
- Differences from canonical
- 1-34: Missing
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY756062 EMBL· GenBank· DDBJ | AAV28717.1 EMBL· GenBank· DDBJ | mRNA | ||
AY756064 EMBL· GenBank· DDBJ | AAV28719.1 EMBL· GenBank· DDBJ | mRNA | ||
D49818 EMBL· GenBank· DDBJ | BAA18921.1 EMBL· GenBank· DDBJ | mRNA | ||
AY714243 EMBL· GenBank· DDBJ | AAU14998.1 EMBL· GenBank· DDBJ | mRNA | ||
AF108765 EMBL· GenBank· DDBJ | AAD09427.1 EMBL· GenBank· DDBJ | mRNA | ||
AY786551 EMBL· GenBank· DDBJ | AAV65753.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC134772 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471055 EMBL· GenBank· DDBJ | EAW64890.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC010269 EMBL· GenBank· DDBJ | AAH10269.1 EMBL· GenBank· DDBJ | mRNA |