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 27-MAR-2024, entry version 230. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 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 PDB; 7TFF; X-ray; 3.60 A; A/B/C/D=1-784. DR PDBsum; 4RH3; -. DR PDBsum; 4U1R; -. DR PDBsum; 4WL0; -. DR PDBsum; 4XYJ; -. DR PDBsum; 4XYK; -. DR PDBsum; 4XZ2; -. DR PDBsum; 7TFF; -. DR AlphaFoldDB; Q01813; -. DR SMR; Q01813; -. DR BioGRID; 111235; 295. DR ComplexPortal; CPX-1999; 6-phosphofructokinase, P4 homotetramer. DR DIP; DIP-45850N; -. DR IntAct; Q01813; 85. DR MINT; Q01813; -. DR STRING; 9606.ENSP00000370517; -. DR ChEMBL; CHEMBL2972; -. DR GlyCosmos; Q01813; 2 sites, 1 glycan. DR GlyGen; Q01813; 3 sites, 1 O-linked glycan (2 sites). 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; 9606-ENSP00000370517; -. DR PeptideAtlas; Q01813; -. DR ProteomicsDB; 57992; -. [Q01813-1] DR ProteomicsDB; 65275; -. DR Pumba; Q01813; -. DR Antibodypedia; 23840; 599 antibodies from 35 providers. DR DNASU; 5214; -. DR Ensembl; ENST00000381125.9; ENSP00000370517.4; ENSG00000067057.19. [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 AGR; HGNC:8878; -. 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; EWQDQMC; -. DR OrthoDB; 374214at2759; -. DR PhylomeDB; Q01813; -. DR TreeFam; TF300411; -. DR BioCyc; MetaCyc:HS00894-MONOMER; -. 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; 22 hits in 1158 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 206 other cell types or tissues. DR ExpressionAtlas; Q01813; baseline and differential. 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; 3.40.50.450; -; 2. DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 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 NCBIfam; TIGR02478; 6PF1K_euk; 1. DR PANTHER; PTHR13697:SF5; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE, PLATELET TYPE; 1. DR PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1. DR Pfam; PF00365; PFK; 2. DR PIRSF; PIRSF000533; ATP_PFK_euk; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; Phosphofructokinase; 2. DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2. DR Genevisible; Q01813; HS. 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 //