Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P12382 (K6PL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
6-phosphofructokinase, liver type

EC=2.7.1.11
Alternative name(s):
Phosphofructo-1-kinase isozyme B
Short name=PFK-B
Phosphofructokinase 1
Phosphohexokinase
Gene names
Name:Pfkl
Synonyms:Pfk-l, Pfkb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length780 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the third step of glycolysis, the phosphorylation of fructose-6-phosphate (F6P) by ATP to generate fructose-1,6-bisphosphate (FBP) and ADP. HAMAP-Rule MF_00339

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_00339

Cofactor

Magnesium.

Enzyme regulation

Allosteric enzyme activated by ADP, AMP, or fructose bisphosphate and inhibited by ATP or citrate. GlcNAcylation by OGT overcomes allosteric regulation By similarity. HAMAP-Rule MF_00339

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_00339

Subunit structure

Homotetramer.

Post-translational modification

GlcNAcylation at Ser-529 by OGT decreases enzyme activity, leading to redirect glucose flux through the oxidative pentose phosphate pathway. Glycosylation is stimulated by both hypoxia and glucose deprivation By similarity. HAMAP-Rule MF_00339

Sequence similarities

Belongs to the phosphofructokinase family. Two domains subfamily.

Ontologies

Keywords
   Biological processGlycolysis
   DomainRepeat
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
Glycoprotein
Phosphoprotein
   Technical termAllosteric enzyme
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate phosphorylation

Inferred from direct assay PubMed 8172601PubMed 9287040. Source: GOC

fructose 1,6-bisphosphate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

fructose 6-phosphate metabolic process

Inferred from direct assay PubMed 8172601PubMed 9287040. Source: MGI

glycolysis

Inferred from direct assay PubMed 8172601PubMed 9287040. Source: MGI

negative regulation of insulin secretion

Inferred from direct assay PubMed 9287040. Source: MGI

protein homotetramerization

Inferred from electronic annotation. Source: Ensembl

response to glucose

Inferred from direct assay PubMed 9287040. Source: MGI

   Cellular_component6-phosphofructokinase complex

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from direct assay PubMed 2521854. Source: MGI

   Molecular_function6-phosphofructokinase activity

Inferred from direct assay PubMed 8172601PubMed 9287040. Source: MGI

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

fructose binding

Inferred from electronic annotation. Source: Ensembl

fructose-6-phosphate binding

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 7807796-phosphofructokinase, liver type HAMAP-Rule MF_00339
PRO_0000112022

Regions

Nucleotide binding35 – 395ATP By similarity
Nucleotide binding193 – 1975ATP By similarity
Nucleotide binding210 – 22617ATP By similarity

Sites

Active site1661Proton acceptor By similarity
Metal binding2241Magnesium; via carbonyl oxygen By similarity
Binding site2011Substrate By similarity
Binding site2921Substrate By similarity
Binding site2981Substrate By similarity
Binding site3011Substrate By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue6401Phosphotyrosine Ref.6
Modified residue7751Phosphoserine Ref.7
Glycosylation5291O-linked (GlcNAc) By similarity

Experimental info

Sequence conflict4191R → P in AAA20076. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P12382 [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: 0C12E2C222020B7F

FASTA78085,360
        10         20         30         40         50         60 
MATVDLEKLR MSGAGKAIGV LTSGGDAQGM NAAVRAVTRM GIYVGAKVFL IYEGYEGLVE 

        70         80         90        100        110        120 
GGENIKPANW LSVSNIIQLG GTIIGSARCK AFTTREGRLA AAYNLLQHGI TNLCVIGGDG 

       130        140        150        160        170        180 
SLTGANIFRN EWGSLLEELV KEGKISESTA QNYAHLTIAG LVGSIDNDFC GTDMTIGTDS 

       190        200        210        220        230        240 
ALHRIMEVID AITTTAQSHQ RTFVLEVMGR HCGYLALVSA LASGADWLFI PEAPPEDGWE 

       250        260        270        280        290        300 
NFMCERLGET RSRGSRLNII IIAEGAIDRH GKPISSSYVK DLVVQRLGFD TRVTVLGHVQ 

       310        320        330        340        350        360 
RGGTPSAFDR ILSSKMGMEA VMALLEATPD TPACVVSLSG NQSVRLPLME CVQVTKDVQK 

       370        380        390        400        410        420 
AMDEERFDEA IQLRGRSFEN NWKIYKLLAH QKVSKEKSNF SLAILNVGAP AAGMNAAVRS 

       430        440        450        460        470        480 
AVRTGISEGH TVYIVHDGFE GLAKGQVQEV GWHDVAGWLG RGGSMLGTKR TLPKPHLEAI 

       490        500        510        520        530        540 
VENLRTYNIH ALLVIGGFEA YEGVLQLVEA RGRYEELCIV MCVIPATISN NVPGTDFSLG 

       550        560        570        580        590        600 
SDTAVNAAME SCDRIKQSAS GTKRRVFIVE TMGGYCGYLA TVTGIAVGAD AAYVFEDPFN 

       610        620        630        640        650        660 
IHDLKANVEH MTEKMKTDIQ RGLVLRNEKC HEHYTTEFLY NLYSSEGRGV FDCRTNVLGH 

       670        680        690        700        710        720 
LQQGGAPTPF DRNYGTKLGV KAMLWVSEKL RDVYRKGRVF ANAPDSACVI GLRKKVVAFS 

       730        740        750        760        770        780 
PVTELKKETD FEHRMPREQW WLNLRLMLKM LAHYRISMAD YVSGELEHVT RRTLSIDKGF 

« Hide

References

« Hide 'large scale' references
[1]"Liver (B-type) phosphofructokinase mRNA. Cloning, structure, and expression."
Gehnrich S.C., Gekakis N., Sul H.S.
J. Biol. Chem. 263:11755-11759(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"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. expand/collapse author list , 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].
Strain: C57BL/6J.
Tissue: Cerebellum, Head and Pituitary.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
Strain: Czech II.
Tissue: Mammary tumor.
[5]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 130-141; 257-269; 367-374; 655-672 AND 716-726, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[6]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-640, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[7]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-775, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03928 mRNA. Translation: AAA20076.1.
AK030511 mRNA. Translation: BAC26997.1.
AK036318 mRNA. Translation: BAC29382.1.
AK081313 mRNA. Translation: BAC38193.1.
AK159328 mRNA. Translation: BAE34994.1.
CH466553 Genomic DNA. Translation: EDL31763.1.
BC020097 mRNA. Translation: AAH20097.1.
PIRA31070.
RefSeqNP_032852.2. NM_008826.4.
UniGeneMm.269649.

3D structure databases

ProteinModelPortalP12382.
SMRP12382. Positions 10-754.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202124. 3 interactions.
IntActP12382. 7 interactions.
MINTMINT-135975.

PTM databases

PhosphoSiteP12382.

Proteomic databases

PaxDbP12382.
PRIDEP12382.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020522; ENSMUSP00000020522; ENSMUSG00000020277.
GeneID18641.
KEGGmmu:18641.
UCSCuc007fwo.2. mouse.

Organism-specific databases

CTD5211.
MGIMGI:97547. Pfkl.

Phylogenomic databases

eggNOGCOG0205.
GeneTreeENSGT00390000013209.
HOGENOMHOG000200154.
HOVERGENHBG000976.
InParanoidQ8VDX7.
KOK00850.
OMAVQHGITN.
OrthoDBEOG7ZSHV5.
TreeFamTF300411.

Enzyme and pathway databases

SABIO-RKP12382.
UniPathwayUPA00109; UER00182.

Gene expression databases

ArrayExpressP12382.
BgeeP12382.
CleanExMM_PFKL.
GenevestigatorP12382.

Family and domain databases

HAMAPMF_00339. Phosphofructokinase.
InterProIPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamPF00365. PFK. 2 hits.
[Graphical view]
PIRSFPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSPR00476. PHFRCTKINASE.
SUPFAMSSF53784. SSF53784. 2 hits.
TIGRFAMsTIGR02478. 6PF1K_euk. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio294626.
PROP12382.
SOURCESearch...

Entry information

Entry nameK6PL_MOUSE
AccessionPrimary (citable) accession number: P12382
Secondary accession number(s): Q8VDX7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 135 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot