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Protein

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

Gene

Pfkfb2

Organism
Rattus norvegicus (Rat)
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)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
Sitei259 – 2591Transition state stabilizerBy similarity
Active sitei260 – 2601Tele-phosphohistidine intermediateBy similarity
Binding sitei266 – 2661Fructose 2,6-bisphosphateBy similarity
Sitei266 – 2661Transition state stabilizerBy similarity
Binding sitei272 – 2721Fructose 2,6-bisphosphate; via amide nitrogenBy 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
Sitei394 – 3941Transition state stabilizerBy 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

  • 6-phosphofructo-2-kinase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • fructose-2,6-bisphosphate 2-phosphatase activity Source: CACAO
  • kinase binding Source: RGD

GO - Biological processi

  • fructose 2,6-bisphosphate metabolic process Source: RGD
  • fructose metabolic process Source: InterPro
  • glucose catabolic process Source: RGD
  • glycolytic process Source: UniProtKB
  • lactate metabolic process Source: RGD
  • positive regulation of glucokinase activity Source: RGD
  • positive regulation of insulin secretion Source: RGD
  • pyruvate metabolic process Source: RGD
  • response to glucose Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.105. 5301.
3.1.3.46. 5301.
ReactomeiR-RNO-70171. Glycolysis.
SABIO-RKQ9JJH5.

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
RH2K
Including the following 2 domains:
Fructose-2,6-bisphosphatase (EC:3.1.3.46)
Gene namesi
Name:Pfkfb2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 13

Organism-specific databases

RGDi3309. Pfkfb2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 5575566-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2PRO_0000179966Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Phosphorylation by AMPK stimulates activity.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9JJH5.
PRIDEiQ9JJH5.

PTM databases

iPTMnetiQ9JJH5.
PhosphoSiteiQ9JJH5.

Expressioni

Gene expression databases

ExpressionAtlasiQ9JJH5. baseline and differential.
GenevisibleiQ9JJH5. RN.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

  • kinase binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000005729.

Structurei

3D structure databases

ProteinModelPortaliQ9JJH5.
SMRiQ9JJH5. Positions 39-451.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 2512506-phosphofructo-2-kinaseAdd
BLAST
Regioni252 – 557306Fructose-2,6-bisphosphataseAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0234. Eukaryota.
COG0406. LUCA.
GeneTreeiENSGT00390000018751.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiQ9JJH5.
KOiK19029.
OMAiDQNKFAY.
OrthoDBiEOG7M3J03.
PhylomeDBiQ9JJH5.
TreeFamiTF313541.

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]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 3 (identifier: Q9JJH5-1) [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
MSENSTFSTE DSSSSSYKPH ASNLRRAGKK CSWASYMTNS PTLIVMIGLP
60 70 80 90 100
ARGKTYVSKK LTRYLNWIGV PTKVFNLGVY RREAVKSYKS 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 IGGDSGLSLR GKQFAQALKK FLEEQEIQDL
310 320 330 340 350
KVWTSQLKRT IQTAESLGVT YEQWKILNEI DAGVCEEMTY SEIEQRYPEE
360 370 380 390 400
FALRDQEKYL YRYPGGESYQ DLVQRLEPVI MELERQGNVL VISHQAVMRC
410 420 430 440 450
LLAYFLDKGA DELPYLRCPL HIIFKLTPVA YGCKVETITL NVEAVDTHRD
460 470 480 490 500
KPTHNFPKSQ TPVRMRRNSF TPLSSSNTIR RPRNYSVGSR PLKPLSPLRA
510 520 530 540 550
LDMQEGADQP KTQVQQGSAQ ATEHLQKALE FANGHREVEN VLAKHRRPSM

ASLTLLS
Length:557
Mass (Da):64,156
Last modified:October 1, 2000 - v1
Checksum:iD5707054E416629F
GO
Isoform 1 (identifier: Q9JJH5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     515-519: QQGSA → SIPVV
     520-547: Missing.

Show »
Length:529
Mass (Da):60,916
Checksum:i013AABF875C60840
GO
Isoform 2 (identifier: Q9JJH5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     514-536: Missing.

Show »
Length:534
Mass (Da):61,653
Checksum:i88C635DE3964CD53
GO
Isoform 4 (identifier: Q9JJH5-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     454-536: Missing.

Show »
Length:474
Mass (Da):54,823
Checksum:i1EDFF196B219764D
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei454 – 53683Missing in isoform 4. CuratedVSP_004678Add
BLAST
Alternative sequencei514 – 53623Missing in isoform 2. CuratedVSP_004676Add
BLAST
Alternative sequencei515 – 5195QQGSA → SIPVV in isoform 1. CuratedVSP_004677
Alternative sequencei520 – 54728Missing in isoform 1. CuratedVSP_004679Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S67900 mRNA. Translation: AAB29678.1.
L27084 mRNA. Translation: AAA41132.1.
AB040530 mRNA. Translation: BAA96495.1.
AB040531 mRNA. Translation: BAA96496.1.
AB040532 mRNA. Translation: BAA96497.1.
AB040533 mRNA. Translation: BAA96498.1.
PIRiJC2037.
RefSeqiNP_001029136.1. NM_001033964.2. [Q9JJH5-3]
NP_001029137.1. NM_001033965.2. [Q9JJH5-1]
NP_536725.2. NM_080477.3. [Q9JJH5-4]
XP_006249768.1. XM_006249706.2.
XP_006249769.1. XM_006249707.2.
XP_006249770.1. XM_006249708.1.
XP_006249771.1. XM_006249709.2. [Q9JJH5-4]
XP_006249773.1. XM_006249711.2. [Q9JJH5-1]
UniGeneiRn.44844.

Genome annotation databases

EnsembliENSRNOT00000005729; ENSRNOP00000005729; ENSRNOG00000004162. [Q9JJH5-1]
ENSRNOT00000037679; ENSRNOP00000030819; ENSRNOG00000004162. [Q9JJH5-4]
ENSRNOT00000050354; ENSRNOP00000044506; ENSRNOG00000004162. [Q9JJH5-3]
GeneIDi24640.
KEGGirno:24640.
UCSCiRGD:3309. rat. [Q9JJH5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S67900 mRNA. Translation: AAB29678.1.
L27084 mRNA. Translation: AAA41132.1.
AB040530 mRNA. Translation: BAA96495.1.
AB040531 mRNA. Translation: BAA96496.1.
AB040532 mRNA. Translation: BAA96497.1.
AB040533 mRNA. Translation: BAA96498.1.
PIRiJC2037.
RefSeqiNP_001029136.1. NM_001033964.2. [Q9JJH5-3]
NP_001029137.1. NM_001033965.2. [Q9JJH5-1]
NP_536725.2. NM_080477.3. [Q9JJH5-4]
XP_006249768.1. XM_006249706.2.
XP_006249769.1. XM_006249707.2.
XP_006249770.1. XM_006249708.1.
XP_006249771.1. XM_006249709.2. [Q9JJH5-4]
XP_006249773.1. XM_006249711.2. [Q9JJH5-1]
UniGeneiRn.44844.

3D structure databases

ProteinModelPortaliQ9JJH5.
SMRiQ9JJH5. Positions 39-451.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000005729.

PTM databases

iPTMnetiQ9JJH5.
PhosphoSiteiQ9JJH5.

Proteomic databases

PaxDbiQ9JJH5.
PRIDEiQ9JJH5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000005729; ENSRNOP00000005729; ENSRNOG00000004162. [Q9JJH5-1]
ENSRNOT00000037679; ENSRNOP00000030819; ENSRNOG00000004162. [Q9JJH5-4]
ENSRNOT00000050354; ENSRNOP00000044506; ENSRNOG00000004162. [Q9JJH5-3]
GeneIDi24640.
KEGGirno:24640.
UCSCiRGD:3309. rat. [Q9JJH5-1]

Organism-specific databases

CTDi5208.
RGDi3309. Pfkfb2.

Phylogenomic databases

eggNOGiKOG0234. Eukaryota.
COG0406. LUCA.
GeneTreeiENSGT00390000018751.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiQ9JJH5.
KOiK19029.
OMAiDQNKFAY.
OrthoDBiEOG7M3J03.
PhylomeDBiQ9JJH5.
TreeFamiTF313541.

Enzyme and pathway databases

BRENDAi2.7.1.105. 5301.
3.1.3.46. 5301.
ReactomeiR-RNO-70171. Glycolysis.
SABIO-RKQ9JJH5.

Miscellaneous databases

PROiQ9JJH5.

Gene expression databases

ExpressionAtlasiQ9JJH5. baseline and differential.
GenevisibleiQ9JJH5. RN.

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 fructose 6-phosphate,2-kinase:fructose 2,6-bisphosphatase of rat brain."
    Watanabe F., Sakai A., Furuya E., Uyeda K.
    Biochem. Biophys. Res. Commun. 198:335-340(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. "New isoforms of rat heart-type fructose 6-phosphate 2-kinase/fructose 2,6-bisphosphatase are generated by alternative splicing of novel exons."
    Watanabe F., Furuya E.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
    Strain: Sprague-Dawley.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469 AND SER-486, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiF262_RAT
AccessioniPrimary (citable) accession number: Q9JJH5
Secondary accession number(s): Q64297, Q9JHL5, Q9JJH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 134 of the entry and version 1 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. 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.