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P17858

- PFKAL_HUMAN

UniProt

P17858 - PFKAL_HUMAN

Protein

ATP-dependent 6-phosphofructokinase, liver type

Gene

PFKL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 175 (01 Oct 2014)
      Sequence version 6 (06 Mar 2007)
      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.1 PublicationUniRule annotation

    Catalytic activityi

    ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.1 PublicationUniRule 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.1 PublicationUniRule 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: UniProtKB
    2. ATP binding Source: UniProtKB
    3. fructose-6-phosphate binding Source: BHF-UCL
    4. fructose binding Source: BHF-UCL
    5. identical protein binding Source: IntAct
    6. kinase binding Source: BHF-UCL
    7. metal ion binding Source: UniProtKB-KW
    8. protein binding Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. carbohydrate phosphorylation Source: GOC
    3. fructose 1,6-bisphosphate metabolic process Source: UniProtKB
    4. fructose 6-phosphate metabolic process Source: UniProtKB
    5. glucose metabolic process Source: Reactome
    6. glycolytic process Source: UniProtKB
    7. negative regulation of insulin secretion Source: Ensembl
    8. protein homotetramerization Source: Ensembl
    9. protein oligomerization Source: BHF-UCL
    10. response to glucose Source: UniProtKB
    11. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06881-MONOMER.
    ReactomeiREACT_1383. Glycolysis.
    SABIO-RKP17858.
    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:8876. PFKL.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. 6-phosphofructokinase complex Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi527 – 5271T → A: Does not affect GlcNAcylation. 1 Publication
    Mutagenesisi529 – 5291S → A: Prevents GlcNAcylation and enhance enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA33215.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 780779ATP-dependent 6-phosphofructokinase, liver typePRO_0000112021Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Glycosylationi529 – 5291O-linked (GlcNAc)1 Publication
    Modified residuei640 – 6401PhosphotyrosineBy similarity
    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.1 Publication

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP17858.
    PaxDbiP17858.
    PRIDEiP17858.

    PTM databases

    PhosphoSiteiP17858.

    Miscellaneous databases

    PMAP-CutDBP17858.

    Expressioni

    Gene expression databases

    ArrayExpressiP17858.
    BgeeiP17858.
    CleanExiHS_PFKL.
    GenevestigatoriP17858.

    Organism-specific databases

    HPAiHPA030047.

    Interactioni

    Subunit structurei

    Homo- and heterotetramers. Muscle is M4, liver is L4, and red cell is M3L, M2L2, or ML3.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-487243,EBI-487243
    PFKMP082376EBI-487243,EBI-514788

    Protein-protein interaction databases

    BioGridi111232. 29 interactions.
    IntActiP17858. 10 interactions.
    MINTiMINT-5004093.
    STRINGi9606.ENSP00000269848.

    Structurei

    3D structure databases

    ProteinModelPortaliP17858.
    SMRiP17858. 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.
    HOGENOMiHOG000200154.
    HOVERGENiHBG000976.
    KOiK00850.
    OMAiVQHGITN.
    OrthoDBiEOG7ZSHV5.
    PhylomeDBiP17858.
    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]

    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. Align

    Isoform 1 (identifier: P17858-1) [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

    MAAVDLEKLR ASGAGKAIGV LTSGGDAQGM NAAVRAVTRM GIYVGAKVFL    50
    IYEGYEGLVE GGENIKQANW LSVSNIIQLG GTIIGSARCK AFTTREGRRA 100
    AAYNLVQHGI TNLCVIGGDG SLTGANIFRS EWGSLLEELV AEGKISETTA 150
    RTYSHLNIAG LVGSIDNDFC GTDMTIGTDS ALHRIMEVID AITTTAQSHQ 200
    RTFVLEVMGR HCGYLALVSA LASGADWLFI PEAPPEDGWE NFMCERLGET 250
    RSRGSRLNII IIAEGAIDRN GKPISSSYVK DLVVQRLGFD TRVTVLGHVQ 300
    RGGTPSAFDR ILSSKMGMEA VMALLEATPD TPACVVTLSG NQSVRLPLME 350
    CVQMTKEVQK AMDDKRFDEA TQLRGGSFEN NWNIYKLLAH QKPPKEKSNF 400
    SLAILNVGAP AAGMNAAVRS AVRTGISHGH TVYVVHDGFE GLAKGQVQEV 450
    GWHDVAGWLG RGGSMLGTKR TLPKGQLESI VENIRIYGIH ALLVVGGFEA 500
    YEGVLQLVEA RGRYEELCIV MCVIPATISN NVPGTDFSLG SDTAVNAAME 550
    SCDRIKQSAS GTKRRVFIVE TMGGYCGYLA TVTGIAVGAD AAYVFEDPFN 600
    IHDLKVNVEH MTEKMKTDIQ RGLVLRNEKC HDYYTTEFLY NLYSSEGKGV 650
    FDCRTNVLGH LQQGGAPTPF DRNYGTKLGV KAMLWLSEKL REVYRKGRVF 700
    ANAPDSACVI GLKKKAVAFS PVTELKKDTD FEHRMPREQW WLSLRLMLKM 750
    LAQYRISMAA YVSGELEHVT RRTLSMDKGF 780
    Length:780
    Mass (Da):85,018
    Last modified:March 6, 2007 - v6
    Checksum:i0D686CE074E9626D
    GO
    Isoform 2 (identifier: P17858-2) [UniParc]FASTAAdd to Basket

    Also known as: a

    The sequence of this isoform differs from the canonical sequence as follows:
         1-28: MAAVDLEKLRASGAGKAIGVLTSGGDAQ → MCNQGRGRES...GGTSIMSRLG

    Note: No experimental confirmation available.

    Show »
    Length:827
    Mass (Da):90,203
    Checksum:iADBECCB9B1FB234C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti27 – 271A → R in CAA33597. (PubMed:2533063)Curated
    Sequence conflicti27 – 271A → R in CAB46744. (PubMed:2139864)Curated
    Sequence conflicti86 – 861S → T in CAB46744. (PubMed:2139864)Curated
    Sequence conflicti89 – 891C → S in CAA33597. (PubMed:2533063)Curated
    Sequence conflicti89 – 891C → S in CAB46744. (PubMed:2139864)Curated
    Sequence conflicti103 – 1031Y → N in CAB46744. (PubMed:2139864)Curated
    Sequence conflicti236 – 2361E → EAPPE in CAB46744. (PubMed:2139864)Curated
    Sequence conflicti386 – 3861K → R in CAB46744. (PubMed:2139864)Curated
    Sequence conflicti389 – 3891A → T in CAA33597. (PubMed:2533063)Curated
    Sequence conflicti389 – 3891A → T in CAB46744. (PubMed:2139864)Curated
    Sequence conflicti648 – 6481K → N in AAH08964. (PubMed:15489334)Curated
    Sequence conflicti648 – 6481K → N in AAH09919. (PubMed:15489334)Curated
    Sequence conflicti717 – 7171V → A in AAH08964. (PubMed:15489334)Curated
    Sequence conflicti717 – 7171V → A in AAH09919. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti81 – 811G → A.1 Publication
    VAR_006070
    Natural varianti151 – 1511R → W.1 Publication
    VAR_006071
    Natural varianti237 – 2371D → V.
    Corresponds to variant rs1057037 [ dbSNP | Ensembl ].
    VAR_030872

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2828MAAVD…GGDAQ → MCNQGRGRESSRGGLHVQGS CRGLSRSPQQETGFAKAPAG TDCFFHCSPGSRGQGDRKEE VTSEPGGTSIMSRLG in isoform 2. 1 PublicationVSP_011854Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15573 mRNA. Translation: CAA33597.1.
    X16911
    , X16912, X16913, X16914, X16915, X16916, X16917, X16918, X16919, X16920, X16921, X16922, X16923, X16924, X16925, X16926, X16927, X16928, X16929, X16930 Genomic DNA. Translation: CAB46744.1.
    AP001754 Genomic DNA. Translation: BAA95561.1.
    BC006422 mRNA. Translation: AAH06422.1.
    BC007536 mRNA. Translation: AAH07536.1.
    BC008964 mRNA. Translation: AAH08964.1.
    BC009919 mRNA. Translation: AAH09919.1.
    CCDSiCCDS33582.1. [P17858-1]
    PIRiA33639.
    RefSeqiNP_001002021.2. NM_001002021.2.
    NP_002617.3. NM_002626.5. [P17858-1]
    UniGeneiHs.255093.

    Genome annotation databases

    EnsembliENST00000349048; ENSP00000269848; ENSG00000141959. [P17858-1]
    GeneIDi5211.
    KEGGihsa:5211.
    UCSCiuc002zek.3. human. [P17858-2]
    uc002zel.3. human. [P17858-1]

    Polymorphism databases

    DMDMi134048493.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15573 mRNA. Translation: CAA33597.1 .
    X16911
    , X16912 , X16913 , X16914 , X16915 , X16916 , X16917 , X16918 , X16919 , X16920 , X16921 , X16922 , X16923 , X16924 , X16925 , X16926 , X16927 , X16928 , X16929 , X16930 Genomic DNA. Translation: CAB46744.1 .
    AP001754 Genomic DNA. Translation: BAA95561.1 .
    BC006422 mRNA. Translation: AAH06422.1 .
    BC007536 mRNA. Translation: AAH07536.1 .
    BC008964 mRNA. Translation: AAH08964.1 .
    BC009919 mRNA. Translation: AAH09919.1 .
    CCDSi CCDS33582.1. [P17858-1 ]
    PIRi A33639.
    RefSeqi NP_001002021.2. NM_001002021.2.
    NP_002617.3. NM_002626.5. [P17858-1 ]
    UniGenei Hs.255093.

    3D structure databases

    ProteinModelPortali P17858.
    SMRi P17858. Positions 10-754.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111232. 29 interactions.
    IntActi P17858. 10 interactions.
    MINTi MINT-5004093.
    STRINGi 9606.ENSP00000269848.

    Chemistry

    BindingDBi P17858.

    PTM databases

    PhosphoSitei P17858.

    Polymorphism databases

    DMDMi 134048493.

    Proteomic databases

    MaxQBi P17858.
    PaxDbi P17858.
    PRIDEi P17858.

    Protocols and materials databases

    DNASUi 5211.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000349048 ; ENSP00000269848 ; ENSG00000141959 . [P17858-1 ]
    GeneIDi 5211.
    KEGGi hsa:5211.
    UCSCi uc002zek.3. human. [P17858-2 ]
    uc002zel.3. human. [P17858-1 ]

    Organism-specific databases

    CTDi 5211.
    GeneCardsi GC21P045719.
    H-InvDB HIX0016166.
    HGNCi HGNC:8876. PFKL.
    HPAi HPA030047.
    MIMi 171860. gene.
    neXtProti NX_P17858.
    PharmGKBi PA33215.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0205.
    HOGENOMi HOG000200154.
    HOVERGENi HBG000976.
    KOi K00850.
    OMAi VQHGITN.
    OrthoDBi EOG7ZSHV5.
    PhylomeDBi P17858.
    TreeFami TF300411.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00182 .
    BioCyci MetaCyc:HS06881-MONOMER.
    Reactomei REACT_1383. Glycolysis.
    SABIO-RK P17858.

    Miscellaneous databases

    ChiTaRSi PFKL. human.
    GeneWikii PFKL.
    GenomeRNAii 5211.
    NextBioi 20154.
    PMAP-CutDB P17858.
    PROi P17858.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P17858.
    Bgeei P17858.
    CleanExi HS_PFKL.
    Genevestigatori P17858.

    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. "The primary structure of human liver type phosphofructokinase and its comparison with other types of PFK."
      Levanon D., Danciger E., Dafni N., Bernstein Y., Elson A., Moens W., Brandeis M., Groner Y.
      DNA 8:733-743(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT TRP-151.
      Tissue: Liver.
    2. "The structure of the human liver-type phosphofructokinase gene."
      Elson A., Levanon D., Brandeis M., Dafni N., Bernstein Y., Danciger E., Groner Y.
      Genomics 7:47-56(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT ALA-81.
    3. "The DNA sequence of human chromosome 21."
      Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
      , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
      Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORMS 1 AND 2).
      Tissue: Kidney, Lung and Muscle.
    5. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-10 (ISOFORM 1).
      Tissue: Platelet.
    6. Bienvenut W.V., Gao M., Leug H., Pchelintsev N., Adams P.D.
      Submitted (JUL-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-10; 17-35 AND 185-210, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Prostatic carcinoma.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-775, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Phosphofructokinase 1 glycosylation regulates cell growth and metabolism."
      Yi W., Clark P.M., Mason D.E., Keenan M.C., Hill C., Goddard W.A. III, Peters E.C., Driggers E.M., Hsieh-Wilson L.C.
      Science 337:975-980(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, GLYCOSYLATION AT SER-529, MUTAGENESIS OF THR-527 AND SER-529.

    Entry informationi

    Entry nameiPFKAL_HUMAN
    AccessioniPrimary (citable) accession number: P17858
    Secondary accession number(s): Q96A64, Q96IH4, Q9BR91
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 175 of the entry and version 6 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    In human PFK exists as a system of 3 types of subunits, PFKM (muscle), PFKL (liver) and PFKP (platelet) isoenzymes.
    Glycosylation may play a role in cancer cell proliferation: inhibition of 6-phosphofructokinase activity and subsequent redirection of the glucose flux through the oxidative pentose phosphate pathway confers a selective growth advantage on cancer cells. Moreover GlcNAcylation is observed in multiple cancer cell lines and tissue samples and GlcNAcylation leads to larger xenografts tunors in mice (PubMed:22923583).1 Publication

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 21
      Human chromosome 21: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3