PFKAP_HUMAN
ID PFKAP_HUMAN Reviewed; 784 AA.
AC Q01813; B3KS15; Q5VSR7; Q5VSR8;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=ATP-dependent 6-phosphofructokinase, platelet type {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=PFK-P;
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
DE AltName: Full=6-phosphofructokinase type C;
DE AltName: Full=Phosphofructo-1-kinase isozyme C;
DE Short=PFK-C;
DE AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_03184};
GN Name=PFKP; Synonyms=PFKF;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Pancreatic islet;
RX PubMed=8117307; DOI=10.1006/bbrc.1994.1141;
RA Eto K., Sakura H., Yasuda K., Hayakawa T., Kawasaki E., Moriuchi R.,
RA Nagataki S., Yazaki Y., Kadowaki T.;
RT "Cloning of a complete protein-coding sequence of human platelet-type
RT phosphofructokinase isozyme from pancreatic islet.";
RL Biochem. Biophys. Res. Commun. 198:990-998(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Prostate;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 484-784 (ISOFORM 1).
RX PubMed=1834056; DOI=10.1016/s0006-291x(05)81276-8;
RA Simpson C.J., Fothergill-Gilmore L.A.;
RT "Isolation and sequence of a cDNA encoding human platelet
RT phosphofructokinase.";
RL Biochem. Biophys. Res. Commun. 180:197-203(1991).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-651, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386 AND SER-783, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386 AND SER-783, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-395; LYS-486 AND LYS-688, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386 AND SER-783, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-21 AND SER-386, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP INTERACTION WITH ATG4B, PHOSPHORYLATION AT SER-386, AND MUTAGENESIS OF
RP SER-386.
RX PubMed=33607258; DOI=10.1016/j.cellsig.2021.109956;
RA Li X., Sun L., Yan G., Yan X.;
RT "PFKP facilitates ATG4B phosphorylation during amino acid deprivation-
RT induced autophagy.";
RL Cell. Signal. 82:109956-109956(2021).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to
CC fructose 1,6-bisphosphate by ATP, the first committing step of
CC glycolysis.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03184};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or fructose
CC 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.
CC {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- SUBUNIT: Homo- and heterotetramers (By similarity). Phosphofructokinase
CC (PFK) enzyme functions as a tetramer composed of different combinations
CC of 3 types of subunits, called PFKM (where M stands for Muscle), PFKL
CC (Liver) and PFKP (Platelet). The composition of the PFK tetramer
CC differs according to the tissue type it is present in. In muscles, it
CC is composed of 4 PFKM subunits (also called M4). In the liver, the
CC predominant form is a tetramer of PFKL subunits (L4). In erythrocytes,
CC both PFKM and PFKL subunits randomly tetramerize to form M4, L4 and
CC other combinations (ML3, M2L2, M3L). In platelets, brain and
CC fibroblasts, PFK contains a higher proportion of PFKP subunits. The
CC kinetic and regulatory properties of the tetrameric enzyme are
CC dependent on the subunit composition, hence can vary across tissues
CC (Probable). Interacts with ATG4B; promoting phosphorylation of ATG4B
CC (PubMed:33607258). {ECO:0000255|HAMAP-Rule:MF_03184,
CC ECO:0000269|PubMed:33607258, ECO:0000305}.
CC -!- INTERACTION:
CC Q01813; P61970: NUTF2; NbExp=3; IntAct=EBI-359022, EBI-591778;
CC Q01813-1; Q01813-1: PFKP; NbExp=3; IntAct=EBI-16157890, EBI-16157890;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q01813-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q01813-2; Sequence=VSP_046416;
CC -!- PTM: Phosphorylation at Ser-386 promotes interaction with ATG4B.
CC {ECO:0000269|PubMed:33607258}.
CC -!- PTM: GlcNAcylation decreases enzyme activity. {ECO:0000250}.
CC -!- MISCELLANEOUS: In human PFK exists as a system of 3 types of subunits,
CC PFKM (muscle), PFKL (liver) and PFKP (platelet) isoenzymes.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E'
CC sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}.
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DR EMBL; D25328; BAA04998.1; -; mRNA.
DR EMBL; AK092597; BAG52577.1; -; mRNA.
DR EMBL; AK291841; BAF84530.1; -; mRNA.
DR EMBL; AL731533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL451164; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002536; AAH02536.1; -; mRNA.
DR EMBL; BC029138; AAH29138.1; -; mRNA.
DR EMBL; M64784; AAA36435.1; -; mRNA.
DR CCDS; CCDS55698.1; -. [Q01813-2]
DR CCDS; CCDS7059.1; -. [Q01813-1]
DR PIR; JC2055; JC2055.
DR RefSeq; NP_001229268.1; NM_001242339.1. [Q01813-2]
DR RefSeq; NP_002618.1; NM_002627.4. [Q01813-1]
DR PDB; 4RH3; X-ray; 3.02 A; A/B/C/D=26-762.
DR PDB; 4U1R; X-ray; 2.80 A; A/B/C/D=26-762.
DR PDB; 4WL0; X-ray; 2.89 A; A/B/C/D=26-762.
DR PDB; 4XYJ; X-ray; 3.10 A; A/B/C/D/E/F/G/H=1-784.
DR PDB; 4XYK; X-ray; 3.40 A; A/B/C/D=1-784.
DR PDB; 4XZ2; X-ray; 2.67 A; A/B/C/D=26-762.
DR PDBsum; 4RH3; -.
DR PDBsum; 4U1R; -.
DR PDBsum; 4WL0; -.
DR PDBsum; 4XYJ; -.
DR PDBsum; 4XYK; -.
DR PDBsum; 4XZ2; -.
DR AlphaFoldDB; Q01813; -.
DR SMR; Q01813; -.
DR BioGRID; 111235; 212.
DR ComplexPortal; CPX-1999; 6-phosphofructokinase, P4 homotetramer.
DR DIP; DIP-45850N; -.
DR IntAct; Q01813; 65.
DR MINT; Q01813; -.
DR STRING; 9606.ENSP00000370517; -.
DR ChEMBL; CHEMBL2972; -.
DR GlyGen; Q01813; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q01813; -.
DR MetOSite; Q01813; -.
DR PhosphoSitePlus; Q01813; -.
DR SwissPalm; Q01813; -.
DR BioMuta; PFKP; -.
DR DMDM; 1346355; -.
DR CPTAC; CPTAC-251; -.
DR CPTAC; CPTAC-252; -.
DR EPD; Q01813; -.
DR jPOST; Q01813; -.
DR MassIVE; Q01813; -.
DR MaxQB; Q01813; -.
DR PaxDb; Q01813; -.
DR PeptideAtlas; Q01813; -.
DR PRIDE; Q01813; -.
DR ProteomicsDB; 57992; -. [Q01813-1]
DR ProteomicsDB; 65275; -.
DR Antibodypedia; 23840; 517 antibodies from 35 providers.
DR DNASU; 5214; -.
DR Ensembl; ENST00000381125.9; ENSP00000370517.4; ENSG00000067057.18. [Q01813-1]
DR GeneID; 5214; -.
DR KEGG; hsa:5214; -.
DR MANE-Select; ENST00000381125.9; ENSP00000370517.4; NM_002627.5; NP_002618.1.
DR UCSC; uc001igp.4; human. [Q01813-1]
DR CTD; 5214; -.
DR DisGeNET; 5214; -.
DR GeneCards; PFKP; -.
DR HGNC; HGNC:8878; PFKP.
DR HPA; ENSG00000067057; Tissue enhanced (retina).
DR MIM; 171840; gene.
DR neXtProt; NX_Q01813; -.
DR OpenTargets; ENSG00000067057; -.
DR PharmGKB; PA33217; -.
DR VEuPathDB; HostDB:ENSG00000067057; -.
DR eggNOG; KOG2440; Eukaryota.
DR GeneTree; ENSGT00940000155002; -.
DR HOGENOM; CLU_011053_0_0_1; -.
DR InParanoid; Q01813; -.
DR OMA; TIALMEM; -.
DR OrthoDB; 172878at2759; -.
DR PhylomeDB; Q01813; -.
DR TreeFam; TF300411; -.
DR BioCyc; MetaCyc:HS00894-MON; -.
DR BRENDA; 2.7.1.11; 2681.
DR PathwayCommons; Q01813; -.
DR Reactome; R-HSA-70171; Glycolysis.
DR SABIO-RK; Q01813; -.
DR SignaLink; Q01813; -.
DR SIGNOR; Q01813; -.
DR UniPathway; UPA00109; UER00182.
DR BioGRID-ORCS; 5214; 21 hits in 1077 CRISPR screens.
DR ChiTaRS; PFKP; human.
DR GeneWiki; PFKP; -.
DR GenomeRNAi; 5214; -.
DR Pharos; Q01813; Tbio.
DR PRO; PR:Q01813; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q01813; protein.
DR Bgee; ENSG00000067057; Expressed in tendon of biceps brachii and 204 other tissues.
DR ExpressionAtlas; Q01813; baseline and differential.
DR Genevisible; Q01813; HS.
DR GO; GO:0005945; C:6-phosphofructokinase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0003872; F:6-phosphofructokinase activity; ISS:UniProtKB.
DR GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0070095; F:fructose-6-phosphate binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR CDD; cd00764; Eukaryotic_PFK; 1.
DR Gene3D; 3.40.50.460; -; 2.
DR HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR InterPro; IPR009161; 6-Pfructokinase_euk.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR041914; PFK_vert-type.
DR InterPro; IPR015912; Phosphofructokinase_CS.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR Pfam; PF00365; PFK; 2.
DR PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 2.
DR TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Allosteric enzyme; Alternative splicing;
KW ATP-binding; Cytoplasm; Glycolysis; Glycoprotein; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..784
FT /note="ATP-dependent 6-phosphofructokinase, platelet type"
FT /id="PRO_0000112024"
FT REGION 1..399
FT /note="N-terminal catalytic PFK domain 1"
FT REGION 400..411
FT /note="Interdomain linker"
FT REGION 412..784
FT /note="C-terminal regulatory PFK domain 2"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 97..98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 127..130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 173..175
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 210
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 217..219
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 273
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 301
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 307..310
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 481
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 538..542
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 576
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 583..585
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 639
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 665
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 671..674
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 744
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47859"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47860"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33607258,
FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 395
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 486
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 651
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 688
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT CARBOHYD 540
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..87
FT /note="MDADDSRAPKGSLRKFLEHLSGAGKAIGVLTSGGDAQGMNAAVRAVVRMGIY
FT VGAKVYFIYEGYQGMVDGGSNIAEADWESVSSILQ -> MCGYERCRPCRGAHGYLRGG
FT QGVLHLRGLPGHGGRRLKHRRGRLGECLQHPASGAVRGDWREKPGCWSHRFPCPGRHAL
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046416"
FT MUTAGEN 386
FT /note="S->A: Decreased interaction with ATG4B."
FT /evidence="ECO:0000269|PubMed:33607258"
FT CONFLICT 484..485
FT /note="PG -> IP (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="Missing (in Ref. 5; AAA36435)"
FT /evidence="ECO:0000305"
FT CONFLICT 655
FT /note="S -> P (in Ref. 2; BAG52577)"
FT /evidence="ECO:0000305"
FT CONFLICT 699
FT /note="A -> E (in Ref. 5; AAA36435)"
FT /evidence="ECO:0000305"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:4XYJ"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 39..53
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 63..69
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:4XZ2"
FT TURN 83..87
FT /evidence="ECO:0007829|PDB:4RH3"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 128..139
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 143..149
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 155..160
FT /evidence="ECO:0007829|PDB:4XZ2"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:4XYK"
FT HELIX 187..208
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 223..232
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 248..261
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:4XYK"
FT HELIX 285..296
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 306..310
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 316..335
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 343..348
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 351..356
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 357..373
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 376..383
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 385..398
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 412..420
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 425..438
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 442..446
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 449..454
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:4XZ2"
FT TURN 463..468
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:4XYJ"
FT HELIX 484..487
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 488..497
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 500..508
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 509..520
FT /evidence="ECO:0007829|PDB:4XZ2"
FT TURN 521..524
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 526..528
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 532..540
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 552..568
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 570..573
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 576..582
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 589..598
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 601..604
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 606..608
FT /evidence="ECO:0007829|PDB:4XYJ"
FT HELIX 612..625
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 632..638
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 643..645
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 647..657
FT /evidence="ECO:0007829|PDB:4XZ2"
FT TURN 658..661
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 663..668
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 670..673
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 680..702
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 714..716
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 717..723
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 726..731
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 732..735
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 736..738
FT /evidence="ECO:0007829|PDB:4U1R"
FT TURN 741..744
FT /evidence="ECO:0007829|PDB:4XZ2"
FT STRAND 745..748
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 750..755
FT /evidence="ECO:0007829|PDB:4XZ2"
FT HELIX 756..761
FT /evidence="ECO:0007829|PDB:4XZ2"
SQ SEQUENCE 784 AA; 85596 MW; 22522E77E9AF80F6 CRC64;
MDADDSRAPK GSLRKFLEHL SGAGKAIGVL TSGGDAQGMN AAVRAVVRMG IYVGAKVYFI
YEGYQGMVDG GSNIAEADWE SVSSILQVGG TIIGSARCQA FRTREGRLKA ACNLLQRGIT
NLCVIGGDGS LTGANLFRKE WSGLLEELAR NGQIDKEAVQ KYAYLNVVGM VGSIDNDFCG
TDMTIGTDSA LHRIIEVVDA IMTTAQSHQR TFVLEVMGRH CGYLALVSAL ACGADWVFLP
ESPPEEGWEE QMCVKLSENR ARKKRLNIII VAEGAIDTQN KPITSEKIKE LVVTQLGYDT
RVTILGHVQR GGTPSAFDRI LASRMGVEAV IALLEATPDT PACVVSLNGN HAVRLPLMEC
VQMTQDVQKA MDERRFQDAV RLRGRSFAGN LNTYKRLAIK LPDDQIPKTN CNVAVINVGA
PAAGMNAAVR SAVRVGIADG HRMLAIYDGF DGFAKGQIKE IGWTDVGGWT GQGGSILGTK
RVLPGKYLEE IATQMRTHSI NALLIIGGFE AYLGLLELSA AREKHEEFCV PMVMVPATVS
NNVPGSDFSI GADTALNTIT DTCDRIKQSA SGTKRRVFII ETMGGYCGYL ANMGGLAAGA
DAAYIFEEPF DIRDLQSNVE HLTEKMKTTI QRGLVLRNES CSENYTTDFI YQLYSEEGKG
VFDCRKNVLG HMQQGGAPSP FDRNFGTKIS ARAMEWITAK LKEARGRGKK FTTDDSICVL
GISKRNVIFQ PVAELKKQTD FEHRIPKEQW WLKLRPLMKI LAKYKASYDV SDSGQLEHVQ
PWSV
