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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 transcript 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei81 – 811Fructose 6-phosphateBy similarity
Binding sitei105 – 1051Fructose 6-phosphateBy similarity
Active sitei131 – 1311Sequence Analysis
Binding sitei133 – 1331Fructose 6-phosphateBy similarity
Binding sitei139 – 1391Fructose 6-phosphateBy similarity
Active sitei161 – 1611Sequence Analysis
Binding sitei175 – 1751Fructose 6-phosphateBy similarity
Binding sitei196 – 1961Fructose 6-phosphateBy similarity
Binding sitei200 – 2001Fructose 6-phosphateBy similarity
Binding sitei259 – 2591Fructose 2,6-bisphosphateBy similarity
Active sitei260 – 2601Tele-phosphohistidine intermediateBy similarity
Binding sitei266 – 2661Fructose 2,6-bisphosphateBy similarity
Binding sitei272 – 2721Fructose 2,6-bisphosphate; via amide nitrogenBy similarity
Binding sitei309 – 3091Fructose 2,6-bisphosphateBy similarity
Active sitei329 – 3291Proton donor/acceptorBy similarity
Binding sitei340 – 3401Fructose 2,6-bisphosphateBy similarity
Binding sitei354 – 3541Fructose 2,6-bisphosphateBy similarity
Binding sitei358 – 3581Fructose 2,6-bisphosphateBy similarity
Binding sitei369 – 3691Fructose 2,6-bisphosphateBy similarity
Active sitei394 – 3941Proton donor/acceptorBy similarity
Binding sitei395 – 3951Fructose 2,6-bisphosphateBy similarity
Binding sitei399 – 3991Fructose 2,6-bisphosphateBy similarity
Binding sitei431 – 4311ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi48 – 569ATPBy similarity
Nucleotide bindingi170 – 1756ATPBy similarity
Nucleotide bindingi351 – 3544ATPBy similarity
Nucleotide bindingi395 – 3995ATPBy similarity

GO - Molecular functioni

  1. 6-phosphofructo-2-kinase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. fructose-2,6-bisphosphate 2-phosphatase activity Source: CACAO

GO - Biological processi

  1. carbohydrate phosphorylation Source: GOC
  2. dephosphorylation Source: GOC
  3. fructose 2,6-bisphosphate metabolic process Source: InterPro
  4. fructose metabolic process Source: InterPro
  5. glycolytic process Source: UniProtKB
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
ProteomesiUP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:107815. Pfkfb2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 5195186-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2PRO_0000179965Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei32 – 321Phosphoserine; by PKABy similarity
Modified residuei469 – 4691Phosphoserine; by AMPK and PKABy similarity
Modified residuei471 – 4711PhosphothreonineBy similarity
Modified residuei478 – 4781Phosphothreonine; by PKCBy similarity
Modified residuei486 – 4861PhosphoserineBy similarity
Modified residuei496 – 4961PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation by AMPK stimulates activity.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP70265.
PaxDbiP70265.
PRIDEiP70265.

PTM databases

PhosphoSiteiP70265.

Expressioni

Tissue specificityi

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

Gene expression databases

GenevestigatoriP70265.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi202123. 1 interaction.
IntActiP70265. 2 interactions.
STRINGi10090.ENSMUSP00000066426.

Structurei

3D structure databases

ProteinModelPortaliP70265.
SMRiP70265. Positions 40-451.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 2512506-phosphofructo-2-kinaseAdd
BLAST
Regioni252 – 519268Fructose-2,6-bisphosphataseAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0406.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiP70265.
KOiK19029.
PhylomeDBiP70265.

Family and domain databases

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91T → P in AAH18418 (PubMed:15489334).Curated
Sequence conflicti12 – 121Missing in AAH18418 (PubMed:15489334).Curated
Sequence conflicti222 – 2221M → I in AAH18418 (PubMed:15489334).Curated
Sequence conflicti496 – 4961S → K in CAA67352 (PubMed:8814283).Curated

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. Positions 40-451.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202123. 1 interaction.
IntActiP70265. 2 interactions.
STRINGi10090.ENSMUSP00000066426.

PTM databases

PhosphoSiteiP70265.

Proteomic databases

MaxQBiP70265.
PaxDbiP70265.
PRIDEiP70265.

Protocols and materials databases

DNASUi18640.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi18640.
KEGGimmu:18640.

Organism-specific databases

CTDi5208.
MGIiMGI:107815. Pfkfb2.

Phylogenomic databases

eggNOGiCOG0406.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiP70265.
KOiK19029.
PhylomeDBiP70265.

Enzyme and pathway databases

BRENDAi2.7.1.105. 3474.
3.1.3.46. 3474.

Miscellaneous databases

NextBioi294622.
PROiP70265.
SOURCEiSearch...

Gene expression databases

GenevestigatoriP70265.

Family and domain databases

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...

Publicationsi

« Hide 'large scale' publications
  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].

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: April 29, 2015
This is version 135 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

External Data

Dasty 3

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 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.