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Protein

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

Gene

Pfkfb1

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

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei82 – 821Fructose 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 sitei258 – 2581Fructose 2,6-bisphosphateBy similarity
Active sitei259 – 2591Tele-phosphohistidine intermediateBy similarity
Binding sitei265 – 2651Fructose 2,6-bisphosphateBy similarity
Binding sitei271 – 2711Fructose 2,6-bisphosphate; via amide nitrogenBy similarity
Binding sitei308 – 3081Fructose 2,6-bisphosphateBy similarity
Active sitei328 – 3281Proton donor/acceptorBy similarity
Binding sitei339 – 3391Fructose 2,6-bisphosphateBy similarity
Binding sitei353 – 3531Fructose 2,6-bisphosphateBy similarity
Binding sitei357 – 3571Fructose 2,6-bisphosphateBy similarity
Binding sitei368 – 3681Fructose 2,6-bisphosphateBy similarity
Active sitei393 – 3931Proton donor/acceptorBy similarity
Binding sitei394 – 3941Fructose 2,6-bisphosphateBy similarity
Binding sitei398 – 3981Fructose 2,6-bisphosphateBy similarity
Binding sitei430 – 4301ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi49 – 579ATPBy similarity
Nucleotide bindingi170 – 1756ATPBy similarity
Nucleotide bindingi350 – 3534ATPBy similarity
Nucleotide bindingi394 – 3985ATPBy similarity

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

ReactomeiREACT_287123. PKA-mediated phosphorylation of key metabolic factors.
REACT_307423. PP2A-mediated dephosphorylation of key metabolic factors.
REACT_308431. Gluconeogenesis.
REACT_314687. Glycolysis.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:107816. Pfkfb1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 4714706-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1PRO_0000179961Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei33 – 331Phosphoserine; by PKABy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP70266.
PaxDbiP70266.
PRIDEiP70266.

PTM databases

PhosphoSiteiP70266.

Expressioni

Tissue specificityi

Liver.

Gene expression databases

BgeeiP70266.
ExpressionAtlasiP70266. baseline and differential.
GenevisibleiP70266. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000079692.

Structurei

3D structure databases

ProteinModelPortaliP70266.
SMRiP70266. Positions 7-471.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 2502496-phosphofructo-2-kinaseBy similarityAdd
BLAST
Regioni251 – 471221Fructose-2,6-bisphosphataseBy similarityAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0406.
GeneTreeiENSGT00390000018751.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiP70266.
KOiK19028.
OMAiINSLKVW.
PhylomeDBiP70266.
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 (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: P70266-1) [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
MSREMGELTQ TRLQKIWIPH SSSSSLLQRR RGSSIPQFTN SPTMVIMVGL
60 70 80 90 100
PARGKTYIST KLTRYLNWIG TPTKVFNLGQ YRREAVSYRN YEFFRPDNME
110 120 130 140 150
AQLIRKQCAL AALKDVHKYL SREEGHVAVF DATNTTRERR SLILQFAKEH
160 170 180 190 200
GYKVFFIESI CNDPDIIAEN IKQVKLGSPD YIDCDQEKVL EDFLKRIECY
210 220 230 240 250
EINYQPLDEE LDSHLSYIKI FDVGTRYMVN RVQDHVQSRT AYYLMNIHVT
260 270 280 290 300
PRSIYLCRHG ESELNLRGRI GGDSGLSARG KQYAYALANF IRSQSISSLK
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 GCRVESIYLN VEAVNTHRDK
460 470
PENVDITREP EEALDTVPAH Y
Length:471
Mass (Da):54,849
Last modified:January 9, 2007 - v2
Checksum:iA8EA464FB4B2DA42
GO
Isoform 2 (identifier: P70266-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MSREMGELTQTRLQKIWIPHSSSSSLLQRRRGS → MEEKASKRAA

Note: No experimental confirmation available.
Show »
Length:448
Mass (Da):52,112
Checksum:i6CF417A9F775B167
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti460 – 4601P → A in CAA67353 (PubMed:8814283).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3333MSREM…RRRGS → MEEKASKRAA in isoform 2. 1 PublicationVSP_022168Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK132629 mRNA. Translation: BAE21271.1.
AL672150 Genomic DNA. Translation: CAM21428.1.
X98848 mRNA. Translation: CAA67353.1.
CCDSiCCDS30464.1. [P70266-2]
PIRiS74243.
RefSeqiNP_032850.1. NM_008824.3. [P70266-2]
XP_006528818.1. XM_006528755.1. [P70266-1]
XP_011246093.1. XM_011247791.1. [P70266-2]
UniGeneiMm.249131.

Genome annotation databases

EnsembliENSMUST00000112713; ENSMUSP00000108333; ENSMUSG00000025271. [P70266-1]
GeneIDi18639.
KEGGimmu:18639.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK132629 mRNA. Translation: BAE21271.1.
AL672150 Genomic DNA. Translation: CAM21428.1.
X98848 mRNA. Translation: CAA67353.1.
CCDSiCCDS30464.1. [P70266-2]
PIRiS74243.
RefSeqiNP_032850.1. NM_008824.3. [P70266-2]
XP_006528818.1. XM_006528755.1. [P70266-1]
XP_011246093.1. XM_011247791.1. [P70266-2]
UniGeneiMm.249131.

3D structure databases

ProteinModelPortaliP70266.
SMRiP70266. Positions 7-471.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000079692.

PTM databases

PhosphoSiteiP70266.

Proteomic databases

MaxQBiP70266.
PaxDbiP70266.
PRIDEiP70266.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000112713; ENSMUSP00000108333; ENSMUSG00000025271. [P70266-1]
GeneIDi18639.
KEGGimmu:18639.

Organism-specific databases

CTDi5207.
MGIiMGI:107816. Pfkfb1.

Phylogenomic databases

eggNOGiCOG0406.
GeneTreeiENSGT00390000018751.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiP70266.
KOiK19028.
OMAiINSLKVW.
PhylomeDBiP70266.
TreeFamiTF313541.

Enzyme and pathway databases

ReactomeiREACT_287123. PKA-mediated phosphorylation of key metabolic factors.
REACT_307423. PP2A-mediated dephosphorylation of key metabolic factors.
REACT_308431. Gluconeogenesis.
REACT_314687. Glycolysis.

Miscellaneous databases

NextBioi294618.
PROiP70266.
SOURCEiSearch...

Gene expression databases

BgeeiP70266.
ExpressionAtlasiP70266. baseline and differential.
GenevisibleiP70266. MM.

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. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Head.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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] OF 402-471 (ISOFORM 1).
    Strain: BALB/c.
    Tissue: Liver.

Entry informationi

Entry nameiF261_MOUSE
AccessioniPrimary (citable) accession number: P70266
Secondary accession number(s): A2AFN0, Q3V180
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 9, 2007
Last modified: July 22, 2015
This is version 124 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.