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P12382

- PFKAL_MOUSE

UniProt

P12382 - PFKAL_MOUSE

Protein

ATP-dependent 6-phosphofructokinase, liver type

Gene

Pfkl

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 4 (27 Jul 2011)
      Previous versions | rss
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    Functioni

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

    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 nitrogenUniRule annotation
    Metal bindingi119 – 1191Magnesium; catalyticUniRule annotation
    Active sitei166 – 1661Proton acceptorUniRule annotation
    Binding sitei201 – 2011Substrate; shared with dimeric partnerUniRule annotation
    Binding sitei264 – 2641SubstrateUniRule annotation
    Binding sitei292 – 2921Substrate; shared with dimeric partnerUniRule annotation
    Binding sitei470 – 4701Allosteric activator fructose 2,6-bisphosphateUniRule annotation
    Binding sitei565 – 5651Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
    Binding sitei628 – 6281Allosteric activator fructose 2,6-bisphosphateUniRule annotation
    Binding sitei654 – 6541Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
    Binding sitei734 – 7341Allosteric activator fructose 2,6-bisphosphateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi88 – 892ATPUniRule annotation
    Nucleotide bindingi118 – 1214ATPUniRule annotation

    GO - Molecular functioni

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

    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 typeUniRule annotation (EC:2.7.1.11UniRule annotation)
    Short name:
    ATP-PFKUniRule annotation
    Short name:
    PFK-L
    Alternative name(s):
    6-phosphofructokinase type B
    Phosphofructo-1-kinase isozyme B
    Short name:
    PFK-B
    PhosphohexokinaseUniRule annotation
    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 UniRule annotation

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 780779ATP-dependent 6-phosphofructokinase, liver typePRO_0000112022Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy 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.By similarity

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E" sub-subfamily.UniRule annotation

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti419 – 4191R → P in AAA20076. (PubMed:2969893)Curated

    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

    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: October 1, 2014
    This is version 139 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