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Protein

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

Gene

Pfkfb2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

The most important regulatory mechanism of these opposing activities is by phosphorylation and dephosphorylation of the enzyme.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei81Fructose 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 sitei259Fructose 2,6-bisphosphateBy similarity1
Sitei259Transition state stabilizerBy similarity1
Active sitei260Tele-phosphohistidine intermediateBy similarity1
Binding sitei266Fructose 2,6-bisphosphateBy similarity1
Sitei266Transition state stabilizerBy similarity1
Binding sitei272Fructose 2,6-bisphosphate; via amide nitrogenBy similarity1
Active sitei329Proton donor/acceptorBy similarity1
Binding sitei340Fructose 2,6-bisphosphateBy similarity1
Binding sitei354Fructose 2,6-bisphosphateBy similarity1
Binding sitei358Fructose 2,6-bisphosphateBy similarity1
Binding sitei369Fructose 2,6-bisphosphateBy similarity1
Sitei394Transition state stabilizerBy similarity1
Binding sitei395Fructose 2,6-bisphosphateBy similarity1
Binding sitei399Fructose 2,6-bisphosphateBy similarity1
Binding sitei431ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi48 – 56ATPBy similarity9
Nucleotide bindingi170 – 175ATPBy similarity6
Nucleotide bindingi351 – 354ATPBy similarity4
Nucleotide bindingi395 – 399ATPBy similarity5

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.105. 3474.
3.1.3.46. 3474.

Names & Taxonomyi

Protein namesi
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:
Fructose-2,6-bisphosphatase (EC:3.1.3.46)
Gene namesi
Name:Pfkfb2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:107815. Pfkfb2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001799652 – 5196-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2Add BLAST518

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei32Phosphoserine; by PKABy similarity1
Modified residuei469PhosphoserineCombined sources1
Modified residuei471PhosphothreonineBy similarity1
Modified residuei478Phosphothreonine; by PKCBy similarity1
Modified residuei486PhosphoserineCombined sources1
Modified residuei496PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylation by AMPK stimulates activity.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP70265.
MaxQBiP70265.
PaxDbiP70265.
PeptideAtlasiP70265.
PRIDEiP70265.

PTM databases

iPTMnetiP70265.
PhosphoSitePlusiP70265.

Expressioni

Tissue specificityi

Highest levels in kidney; also found in heart, brain, spleen, lung, liver, skeletal muscle and testis.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202123. 1 interactor.
IntActiP70265. 2 interactors.
STRINGi10090.ENSMUSP00000066426.

Structurei

3D structure databases

ProteinModelPortaliP70265.
SMRiP70265.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 2516-phosphofructo-2-kinaseAdd BLAST250
Regioni252 – 519Fructose-2,6-bisphosphataseAdd BLAST268

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0234. Eukaryota.
COG0406. LUCA.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiP70265.
KOiK19029.
PhylomeDBiP70265.

Family and domain databases

CDDicd07067. HP_PGM_like. 1 hit.
Gene3Di3.40.50.1240. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003094. 6Pfruct_kin.
IPR013079. 6Phosfructo_kin.
IPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR027417. P-loop_NTPase.
IPR001345. PG/BPGM_mutase_AS.
[Graphical view]
PANTHERiPTHR10606. PTHR10606. 1 hit.
PfamiPF01591. 6PF2K. 1 hit.
PF00300. His_Phos_1. 1 hit.
[Graphical view]
PRINTSiPR00991. 6PFRUCTKNASE.
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF53254. SSF53254. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P70265-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSENSTFSTE DSCNSSYKPH ASNLRRAGKT CSWASYMTNS PTLIVMIGLP
60 70 80 90 100
ARGKTYVSKK LTRYLNWIGV PTKVFNLGVY RREAVKSYQS YDFFRHDNEE
110 120 130 140 150
AMKIRKQCAL VALEDVKAYF TEESGQIAVF DATNTTRERR DMILNFAKQN
160 170 180 190 200
AFKVFFVESV CDDPDVIAAN ILEVKVSSPD YPERNRENVM EDFLKRIECY
210 220 230 240 250
KVTYQPLDPD NYDKDLSFIK VMNVGQRFLV NRVQDYIQSK IVYYLMNIHV
260 270 280 290 300
HPRTIYLCRH GESEFNLLGK IGGDSGLSVR GKQFAHALKK FLEEQEIQDL
310 320 330 340 350
KVWTSQLKRT IQTAESLGVT YEQWKILNEI DAGVCEEMTY SEIEQRYPEE
360 370 380 390 400
FALRDQEKYL YRYPGGESYQ DLVQRLEPVI MELERQGNIL VISHQAVMRC
410 420 430 440 450
LLAYFLDKGA DELPYLRCPL HIIFKLTPVA YGCKVETITL NVDAVDTHRD
460 470 480 490 500
KPTHNFPKSQ TPVRMRRNSF TPLSSSNTIR RPRNYSVGSR PLKPLSPLRA
510
LDMQEGADQP KTQVSIPVV
Length:519
Mass (Da):59,925
Last modified:September 1, 2009 - v2
Checksum:iFD4CF41AEDF22F89
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti9T → P in AAH18418 (PubMed:15489334).Curated1
Sequence conflicti12Missing in AAH18418 (PubMed:15489334).Curated1
Sequence conflicti222M → I in AAH18418 (PubMed:15489334).Curated1
Sequence conflicti496S → K in CAA67352 (PubMed:8814283).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98847 mRNA. Translation: CAA67352.1.
BC018418 mRNA. Translation: AAH18418.1.
PIRiS74242.
RefSeqiNP_032851.2. NM_008825.4.
UniGeneiMm.249861.

Genome annotation databases

GeneIDi18640.
KEGGimmu:18640.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98847 mRNA. Translation: CAA67352.1.
BC018418 mRNA. Translation: AAH18418.1.
PIRiS74242.
RefSeqiNP_032851.2. NM_008825.4.
UniGeneiMm.249861.

3D structure databases

ProteinModelPortaliP70265.
SMRiP70265.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202123. 1 interactor.
IntActiP70265. 2 interactors.
STRINGi10090.ENSMUSP00000066426.

PTM databases

iPTMnetiP70265.
PhosphoSitePlusiP70265.

Proteomic databases

EPDiP70265.
MaxQBiP70265.
PaxDbiP70265.
PeptideAtlasiP70265.
PRIDEiP70265.

Protocols and materials databases

DNASUi18640.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi18640.
KEGGimmu:18640.

Organism-specific databases

CTDi5208.
MGIiMGI:107815. Pfkfb2.

Phylogenomic databases

eggNOGiKOG0234. Eukaryota.
COG0406. LUCA.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiP70265.
KOiK19029.
PhylomeDBiP70265.

Enzyme and pathway databases

BRENDAi2.7.1.105. 3474.
3.1.3.46. 3474.

Miscellaneous databases

PROiP70265.
SOURCEiSearch...

Family and domain databases

CDDicd07067. HP_PGM_like. 1 hit.
Gene3Di3.40.50.1240. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003094. 6Pfruct_kin.
IPR013079. 6Phosfructo_kin.
IPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR027417. P-loop_NTPase.
IPR001345. PG/BPGM_mutase_AS.
[Graphical view]
PANTHERiPTHR10606. PTHR10606. 1 hit.
PfamiPF01591. 6PF2K. 1 hit.
PF00300. His_Phos_1. 1 hit.
[Graphical view]
PRINTSiPR00991. 6PFRUCTKNASE.
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF53254. SSF53254. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiF262_MOUSE
AccessioniPrimary (citable) accession number: P70265
Secondary accession number(s): Q8VEI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 1, 2009
Last modified: November 2, 2016
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.