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P17858

- PFKAL_HUMAN

UniProt

P17858 - PFKAL_HUMAN

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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

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

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
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

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
Complete GO annotation...

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

BgeeiP17858.
CleanExiHS_PFKL.
ExpressionAtlasiP17858. baseline and differential.
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. 30 interactions.
IntActiP17858. 10 interactions.
MINTiMINT-5004093.
STRINGi9606.ENSP00000269848.

Structurei

3D structure databases

ProteinModelPortaliP17858.
SMRiP17858. Positions 13-754.
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.
InParanoidiP17858.
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

        10         20         30         40         50
MAAVDLEKLR ASGAGKAIGV LTSGGDAQGM NAAVRAVTRM GIYVGAKVFL
60 70 80 90 100
IYEGYEGLVE GGENIKQANW LSVSNIIQLG GTIIGSARCK AFTTREGRRA
110 120 130 140 150
AAYNLVQHGI TNLCVIGGDG SLTGANIFRS EWGSLLEELV AEGKISETTA
160 170 180 190 200
RTYSHLNIAG LVGSIDNDFC GTDMTIGTDS ALHRIMEVID AITTTAQSHQ
210 220 230 240 250
RTFVLEVMGR HCGYLALVSA LASGADWLFI PEAPPEDGWE NFMCERLGET
260 270 280 290 300
RSRGSRLNII IIAEGAIDRN GKPISSSYVK DLVVQRLGFD TRVTVLGHVQ
310 320 330 340 350
RGGTPSAFDR ILSSKMGMEA VMALLEATPD TPACVVTLSG NQSVRLPLME
360 370 380 390 400
CVQMTKEVQK AMDDKRFDEA TQLRGGSFEN NWNIYKLLAH QKPPKEKSNF
410 420 430 440 450
SLAILNVGAP AAGMNAAVRS AVRTGISHGH TVYVVHDGFE GLAKGQVQEV
460 470 480 490 500
GWHDVAGWLG RGGSMLGTKR TLPKGQLESI VENIRIYGIH ALLVVGGFEA
510 520 530 540 550
YEGVLQLVEA RGRYEELCIV MCVIPATISN NVPGTDFSLG SDTAVNAAME
560 570 580 590 600
SCDRIKQSAS GTKRRVFIVE TMGGYCGYLA TVTGIAVGAD AAYVFEDPFN
610 620 630 640 650
IHDLKVNVEH MTEKMKTDIQ RGLVLRNEKC HDYYTTEFLY NLYSSEGKGV
660 670 680 690 700
FDCRTNVLGH LQQGGAPTPF DRNYGTKLGV KAMLWLSEKL REVYRKGRVF
710 720 730 740 750
ANAPDSACVI GLKKKAVAFS PVTELKKDTD FEHRMPREQW WLSLRLMLKM
760 770 780
LAQYRISMAA YVSGELEHVT RRTLSMDKGF
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 13-754.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111232. 30 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.
GeneTreei ENSGT00390000013209.
HOGENOMi HOG000200154.
HOVERGENi HBG000976.
InParanoidi P17858.
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

Bgeei P17858.
CleanExi HS_PFKL.
ExpressionAtlasi P17858. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 176 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