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Protein

6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1

Gene

PFKFB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Synthesis and degradation of fructose 2,6-bisphosphate.

Catalytic activityi

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 regulationi

Phosphorylation at Ser-33 inhibits the kinase and activates the bisphosphatase.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei82Fructose 6-phosphateBy similarity1
Binding sitei105Fructose 6-phosphateBy similarity1
Active sitei131Sequence analysis1
Binding sitei133Fructose 6-phosphateBy similarity1
Binding sitei139Fructose 6-phosphateBy similarity1
Active sitei161Sequence analysis1
Binding sitei175Fructose 6-phosphateBy similarity1
Binding sitei196Fructose 6-phosphateBy similarity1
Binding sitei200Fructose 6-phosphateBy similarity1
Binding sitei258Fructose 2,6-bisphosphateBy similarity1
Active sitei259Tele-phosphohistidine intermediateBy similarity1
Binding sitei265Fructose 2,6-bisphosphateBy similarity1
Binding sitei271Fructose 2,6-bisphosphate; via amide nitrogenBy similarity1
Binding sitei308Fructose 2,6-bisphosphateBy similarity1
Active sitei328Proton donor/acceptorBy similarity1
Binding sitei339Fructose 2,6-bisphosphateBy similarity1
Binding sitei353Fructose 2,6-bisphosphateBy similarity1
Binding sitei357Fructose 2,6-bisphosphateBy similarity1
Binding sitei368Fructose 2,6-bisphosphateBy similarity1
Sitei393Transition state stabilizerBy similarity1
Binding sitei394Fructose 2,6-bisphosphateBy similarity1
Binding sitei398Fructose 2,6-bisphosphateBy similarity1
Binding sitei430ATP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi49 – 57ATP1 Publication9
Nucleotide bindingi170 – 175ATP1 Publication6
Nucleotide bindingi350 – 353ATPBy similarity4
Nucleotide bindingi394 – 398ATPBy similarity5

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Kinase, Multifunctional enzyme, Transferase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS08310-MONOMER
BRENDAi2.7.1.105 2681
3.1.3.46 2681
ReactomeiR-HSA-163358 PKA-mediated phosphorylation of key metabolic factors
R-HSA-163767 PP2A-mediated dephosphorylation of key metabolic factors
R-HSA-70171 Glycolysis
SABIO-RKP16118

Names & Taxonomyi

Protein namesi
Recommended name:
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1
Short name:
6PF-2-K/Fru-2,6-P2ase 1
Short name:
PFK/FBPase 1
Alternative name(s):
6PF-2-K/Fru-2,6-P2ase liver isozyme
Including the following 2 domains:
Fructose-2,6-bisphosphatase (EC:3.1.3.46)
Gene namesi
Name:PFKFB1
Synonyms:F6PK, PFRX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

EuPathDBiHostDB:ENSG00000158571.10
HGNCiHGNC:8872 PFKFB1
MIMi311790 gene
neXtProtiNX_P16118

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Pathology & Biotechi

Organism-specific databases

OpenTargetsiENSG00000158571
PharmGKBiPA33211

Chemistry databases

ChEMBLiCHEMBL3421524
DrugBankiDB02515 3-Phosphoglycerol
DB04493 Fructose-6-Phosphate
DB04137 Guanosine-5'-Triphosphate
DB02930 Phosphothiophosphoric Acid-Adenylate Ester

Polymorphism and mutation databases

DMDMi2507178

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001799602 – 4716-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1Add BLAST470

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei33Phosphoserine; by PKABy similarity1
Modified residuei141PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP16118
PeptideAtlasiP16118
PRIDEiP16118

PTM databases

DEPODiP16118
iPTMnetiP16118
PhosphoSitePlusiP16118

Expressioni

Tissue specificityi

Liver.

Gene expression databases

BgeeiENSG00000158571
CleanExiHS_PFKFB1
ExpressionAtlasiP16118 baseline and differential
GenevisibleiP16118 HS

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi111228, 7 interactors
IntActiP16118, 12 interactors
MINTiP16118
STRINGi9606.ENSP00000364145

Chemistry databases

BindingDBiP16118

Structurei

Secondary structure

1471
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi43 – 48Combined sources6
Helixi55 – 68Combined sources14
Beta strandi73 – 77Combined sources5
Helixi78 – 83Combined sources6
Helixi91 – 94Combined sources4
Helixi99 – 121Combined sources23
Beta strandi126 – 132Combined sources7
Helixi137 – 150Combined sources14
Beta strandi153 – 160Combined sources8
Helixi164 – 175Combined sources12
Helixi187 – 201Combined sources15
Turni209 – 214Combined sources6
Beta strandi217 – 221Combined sources5
Turni222 – 225Combined sources4
Beta strandi226 – 230Combined sources5
Helixi235 – 244Combined sources10
Beta strandi254 – 258Combined sources5
Helixi263 – 266Combined sources4
Helixi278 – 293Combined sources16
Beta strandi300 – 303Combined sources4
Helixi307 – 314Combined sources8
Helixi324 – 326Combined sources3
Helixi332 – 334Combined sources3
Helixi339 – 345Combined sources7
Helixi347 – 355Combined sources9
Turni357 – 359Combined sources3
Helixi368 – 384Combined sources17
Beta strandi386 – 392Combined sources7
Helixi394 – 405Combined sources12
Turni409 – 411Combined sources3
Helixi412 – 414Combined sources3
Beta strandi421 – 427Combined sources7
Beta strandi429 – 438Combined sources10
Helixi460 – 464Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K6MX-ray2.40A/B40-471[»]
ProteinModelPortaliP16118
SMRiP16118
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16118

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 2506-phosphofructo-2-kinaseAdd BLAST249
Regioni251 – 471Fructose-2,6-bisphosphataseAdd BLAST221

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0234 Eukaryota
COG0406 LUCA
GeneTreeiENSGT00390000018751
HOGENOMiHOG000181112
HOVERGENiHBG005628
InParanoidiP16118
KOiK19028
OMAiHNYLSHE
OrthoDBiEOG091G0A43
PhylomeDBiP16118
TreeFamiTF313541

Family and domain databases

CDDicd07067 HP_PGM_like, 1 hit
Gene3Di3.40.50.1240, 1 hit
InterProiView protein in InterPro
IPR003094 6Pfruct_kin
IPR013079 6Phosfructo_kin
IPR013078 His_Pase_superF_clade-1
IPR029033 His_PPase_superfam
IPR027417 P-loop_NTPase
IPR001345 PG/BPGM_mutase_AS
PANTHERiPTHR10606 PTHR10606, 1 hit
PfamiView protein in Pfam
PF01591 6PF2K, 1 hit
PF00300 His_Phos_1, 1 hit
PRINTSiPR00991 6PFRUCTKNASE
SMARTiView protein in SMART
SM00855 PGAM, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
SSF53254 SSF53254, 1 hit
PROSITEiView protein in PROSITE
PS00175 PG_MUTASE, 1 hit

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P16118-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSPEMGELTQ TRLQKIWIPH SSGSSRLQRR RGSSIPQFTN SPTMVIMVGL
60 70 80 90 100
PARGKTYIST KLTRYLNWIG TPTKVFNLGQ YRREAVSYKN YEFFLPDNME
110 120 130 140 150
ALQIRKQCAL AALKDVHNYL SHEEGHVAVF DATNTTRERR SLILQFAKEH
160 170 180 190 200
GYKVFFIESI CNDPGIIAEN IRQVKLGSPD YIDCDREKVL EDFLKRIECY
210 220 230 240 250
EVNYQPLDEE LDSHLSYIKI FDVGTRYMVN RVQDHIQSRT VYYLMNIHVT
260 270 280 290 300
PRSIYLCRHG ESELNIRGRI GGDSGLSVRG KQYAYALANF IQSQGISSLK
310 320 330 340 350
VWTSHMKRTI QTAEALGVPY EQWKALNEID AGVCEEMTYE EIQEHYPEEF
360 370 380 390 400
ALRDQDKYRY RYPKGESYED LVQRLEPVIM ELERQENVLV ICHQAVMRCL
410 420 430 440 450
LAYFLDKSSD ELPYLKCPLH TVLKLTPVAY GCKVESIYLN VEAVNTHREK
460 470
PENVDITREP EEALDTVPAH Y
Length:471
Mass (Da):54,681
Last modified:November 1, 1997 - v3
Checksum:iC4FF081A295FB7D3
GO
Isoform 2 (identifier: P16118-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: MSPEMGELTQ...RYLNWIGTPT → MEEKTSRI

Show »
Length:406
Mass (Da):47,426
Checksum:i5D982E7DFBAC5CC1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti305H → R in CAA36861 (PubMed:2163524).Curated1
Sequence conflicti359R → H in AAA35818 (PubMed:2837207).Curated1
Sequence conflicti397 – 398MR → HA in AAA35818 (PubMed:2837207).Curated2

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0547951 – 73MSPEM…IGTPT → MEEKTSRI in isoform 2. 1 PublicationAdd BLAST73

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52638 mRNA Translation: CAA36861.1
AK314089 mRNA Translation: BAG36785.1
AK300724 mRNA Translation: BAG62397.1
AL049732 Genomic DNA No translation available.
AL020991 Genomic DNA No translation available.
BC096079 mRNA Translation: AAH96079.1
M19938 mRNA Translation: AAA35818.1
CCDSiCCDS14364.1 [P16118-1]
CCDS65273.1 [P16118-2]
PIRiS12732
RefSeqiNP_001258733.1, NM_001271804.1
NP_001258734.1, NM_001271805.1 [P16118-2]
NP_002616.2, NM_002625.3 [P16118-1]
UniGeneiHs.444304

Genome annotation databases

EnsembliENST00000375006; ENSP00000364145; ENSG00000158571 [P16118-1]
ENST00000545676; ENSP00000444074; ENSG00000158571 [P16118-2]
GeneIDi5207
KEGGihsa:5207
UCSCiuc004dty.3 human [P16118-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiF261_HUMAN
AccessioniPrimary (citable) accession number: P16118
Secondary accession number(s): B2RA88
, B4DUN5, Q5JXS5, Q99951
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1997
Last modified: May 23, 2018
This is version 192 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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