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P12382

- PFKAL_MOUSE

UniProt

P12382 - PFKAL_MOUSE

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Protein
ATP-dependent 6-phosphofructokinase, liver type
Gene
Pfkl, Pfk-l, Pfkb
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.UniRule annotation

Catalytic activityi

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.UniRule annotation

Cofactori

Magnesium.

Enzyme regulationi

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate. GlcNAcylation by OGT overcomes allosteric regulation By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei25 – 251ATP; via amide nitrogen By similarity
Metal bindingi119 – 1191Magnesium; catalytic By similarity
Active sitei166 – 1661Proton acceptor By similarity
Binding sitei201 – 2011Substrate; shared with dimeric partner By similarity
Binding sitei264 – 2641Substrate By similarity
Binding sitei292 – 2921Substrate; shared with dimeric partner By similarity
Binding sitei470 – 4701Allosteric activator fructose 2,6-bisphosphate By similarity
Binding sitei565 – 5651Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding sitei628 – 6281Allosteric activator fructose 2,6-bisphosphate By similarity
Binding sitei654 – 6541Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding sitei734 – 7341Allosteric activator fructose 2,6-bisphosphate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi88 – 892ATP By similarity
Nucleotide bindingi118 – 1214ATP By similarity

GO - Molecular functioni

  1. 6-phosphofructokinase activity Source: MGI
  2. ATP binding Source: UniProtKB-KW
  3. fructose binding Source: Ensembl
  4. fructose-6-phosphate binding Source: Ensembl
  5. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. carbohydrate phosphorylation Source: GOC
  2. fructose 1,6-bisphosphate metabolic process Source: UniProtKB
  3. fructose 6-phosphate metabolic process Source: MGI
  4. glycolytic process Source: MGI
  5. negative regulation of insulin secretion Source: MGI
  6. protein homotetramerization Source: Ensembl
  7. response to glucose Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RKP12382.
UniPathwayiUPA00109; UER00182.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent 6-phosphofructokinase, liver type (EC:2.7.1.11)
Short name:
ATP-PFK
Short name:
PFK-L
Alternative name(s):
6-phosphofructokinase type B
Phosphofructo-1-kinase isozyme B
Short name:
PFK-B
Phosphohexokinase
Gene namesi
Name:Pfkl
Synonyms:Pfk-l, Pfkb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:97547. Pfkl.

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. 6-phosphofructokinase complex Source: Ensembl
  2. cytosol Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 780779ATP-dependent 6-phosphofructokinase, liver typeUniRule annotation
PRO_0000112022Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Glycosylationi529 – 5291O-linked (GlcNAc) By similarity
Modified residuei640 – 6401Phosphotyrosine1 Publication
Modified residuei775 – 7751Phosphoserine1 Publication

Post-translational modificationi

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.UniRule annotation

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP12382.
PaxDbiP12382.
PRIDEiP12382.

PTM databases

PhosphoSiteiP12382.

Expressioni

Gene expression databases

ArrayExpressiP12382.
BgeeiP12382.
CleanExiMM_PFKL.
GenevestigatoriP12382.

Interactioni

Subunit structurei

Homo- and heterotetramers.

Protein-protein interaction databases

BioGridi202124. 4 interactions.
IntActiP12382. 7 interactions.
MINTiMINT-135975.

Structurei

3D structure databases

ProteinModelPortaliP12382.
SMRiP12382. Positions 10-754.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 390389N-terminal catalytic PFK domain 1UniRule annotation
Add
BLAST
Regioni164 – 1663Substrate binding By similarity
Regioni208 – 2103Substrate binding By similarity
Regioni298 – 3014Substrate binding By similarity
Regioni391 – 40010Interdomain linkerUniRule annotation
Regioni401 – 780380C-terminal regulatory PFK domain 2UniRule annotation
Add
BLAST
Regioni527 – 5315Allosteric activator fructose 2,6-bisphosphate binding By similarity
Regioni572 – 5743Allosteric activator fructose 2,6-bisphosphate binding By similarity
Regioni660 – 6634Allosteric activator fructose 2,6-bisphosphate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0205.
GeneTreeiENSGT00390000013209.
HOGENOMiHOG000200154.
HOVERGENiHBG000976.
InParanoidiQ8VDX7.
KOiK00850.
OMAiVQHGITN.
OrthoDBiEOG7ZSHV5.
TreeFamiTF300411.

Family and domain databases

HAMAPiMF_03184. Phosphofructokinase_I_E.
InterProiIPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamiPF00365. PFK. 2 hits.
[Graphical view]
PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSiPR00476. PHFRCTKINASE.
SUPFAMiSSF53784. SSF53784. 2 hits.
TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P12382-1 [UniParc]FASTAAdd to Basket

« Hide

MATVDLEKLR MSGAGKAIGV LTSGGDAQGM NAAVRAVTRM GIYVGAKVFL    50
IYEGYEGLVE GGENIKPANW LSVSNIIQLG GTIIGSARCK AFTTREGRLA 100
AAYNLLQHGI TNLCVIGGDG SLTGANIFRN EWGSLLEELV KEGKISESTA 150
QNYAHLTIAG LVGSIDNDFC GTDMTIGTDS ALHRIMEVID AITTTAQSHQ 200
RTFVLEVMGR HCGYLALVSA LASGADWLFI PEAPPEDGWE NFMCERLGET 250
RSRGSRLNII IIAEGAIDRH GKPISSSYVK DLVVQRLGFD TRVTVLGHVQ 300
RGGTPSAFDR ILSSKMGMEA VMALLEATPD TPACVVSLSG NQSVRLPLME 350
CVQVTKDVQK AMDEERFDEA IQLRGRSFEN NWKIYKLLAH QKVSKEKSNF 400
SLAILNVGAP AAGMNAAVRS AVRTGISEGH TVYIVHDGFE GLAKGQVQEV 450
GWHDVAGWLG RGGSMLGTKR TLPKPHLEAI VENLRTYNIH ALLVIGGFEA 500
YEGVLQLVEA RGRYEELCIV MCVIPATISN NVPGTDFSLG SDTAVNAAME 550
SCDRIKQSAS GTKRRVFIVE TMGGYCGYLA TVTGIAVGAD AAYVFEDPFN 600
IHDLKANVEH MTEKMKTDIQ RGLVLRNEKC HEHYTTEFLY NLYSSEGRGV 650
FDCRTNVLGH LQQGGAPTPF DRNYGTKLGV KAMLWVSEKL RDVYRKGRVF 700
ANAPDSACVI GLRKKVVAFS PVTELKKETD FEHRMPREQW WLNLRLMLKM 750
LAHYRISMAD YVSGELEHVT RRTLSIDKGF 780
Length:780
Mass (Da):85,360
Last modified:July 27, 2011 - v4
Checksum:i0C12E2C222020B7F
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti419 – 4191R → P in AAA20076. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS35955.1.
PIRiA31070.
RefSeqiNP_032852.2. NM_008826.4.
UniGeneiMm.269649.

Genome annotation databases

EnsembliENSMUST00000020522; ENSMUSP00000020522; ENSMUSG00000020277.
GeneIDi18641.
KEGGimmu:18641.
UCSCiuc007fwo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS35955.1.
PIRi A31070.
RefSeqi NP_032852.2. NM_008826.4.
UniGenei Mm.269649.

3D structure databases

ProteinModelPortali P12382.
SMRi P12382. Positions 10-754.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202124. 4 interactions.
IntActi P12382. 7 interactions.
MINTi MINT-135975.

PTM databases

PhosphoSitei P12382.

Proteomic databases

MaxQBi P12382.
PaxDbi P12382.
PRIDEi P12382.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000020522 ; ENSMUSP00000020522 ; ENSMUSG00000020277 .
GeneIDi 18641.
KEGGi mmu:18641.
UCSCi uc007fwo.2. mouse.

Organism-specific databases

CTDi 5211.
MGIi MGI:97547. Pfkl.

Phylogenomic databases

eggNOGi COG0205.
GeneTreei ENSGT00390000013209.
HOGENOMi HOG000200154.
HOVERGENi HBG000976.
InParanoidi Q8VDX7.
KOi K00850.
OMAi VQHGITN.
OrthoDBi EOG7ZSHV5.
TreeFami TF300411.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00182 .
SABIO-RK P12382.

Miscellaneous databases

NextBioi 294626.
PROi P12382.
SOURCEi Search...

Gene expression databases

ArrayExpressi P12382.
Bgeei P12382.
CleanExi MM_PFKL.
Genevestigatori P12382.

Family and domain databases

HAMAPi MF_03184. Phosphofructokinase_I_E.
InterProi IPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view ]
Pfami PF00365. PFK. 2 hits.
[Graphical view ]
PIRSFi PIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSi PR00476. PHFRCTKINASE.
SUPFAMi SSF53784. SSF53784. 2 hits.
TIGRFAMsi TIGR02478. 6PF1K_euk. 1 hit.
PROSITEi PS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiPFKAL_MOUSE
AccessioniPrimary (citable) accession number: P12382
Secondary accession number(s): Q8VDX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 138 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

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