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Database: UniProt/SWISS-PROT
Entry: PFKAP_HUMAN
LinkDB: PFKAP_HUMAN
Original site: 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   13-FEB-2019, entry version 201.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA   Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA   Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA   Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA   Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA   Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA   Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA   Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA   Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA   Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA   Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA   Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA   Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA   Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA   Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA   Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA   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
RT   project: 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.,
RA   Mann M.;
RT   "Proteomic characterization of the human centrosome by protein
RT   correlation profiling.";
RL   Nature 426:570-574(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-651, AND IDENTIFICATION
RP   BY 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
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, AND IDENTIFICATION
RP   BY 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
RT   phosphorylation 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
RT   the 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
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, AND IDENTIFICATION
RP   BY 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,
RP   AND 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.,
RA   Walther T.C., 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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation 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.,
RA   Buerckstuemmer T., 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
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome 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,
RP   AND 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).
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate
CC       to 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
CC         1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966,
CC         ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03184};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or
CC       fructose 2,6-bisphosphate, and allosterically inhibited by ATP or
CC       citrate. {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).
CC       Phosphofructokinase (PFK) enzyme functions as a tetramer composed
CC       of different combinations of 3 types of subunits, called PFKM
CC       (where M stands for Muscle), PFKL (Liver) and PFKP (Platelet). The
CC       composition of the PFK tetramer differs according to the tissue
CC       type it is present in. In muscles, it is composed of 4 PFKM
CC       subunits (also called M4). In the liver, the predominant form is a
CC       tetramer of PFKL subunits (L4). In erythrocytes, both PFKM and
CC       PFKL subunits randomly tetramerize to form M4, L4 and other
CC       combinations (ML3, M2L2, M3L). In platelets, brain and
CC       fibroblasts, PFK contains a higher proportion of PFKP subunits.
CC       The kinetic and regulatory properties of the tetrameric enzyme are
CC       dependent on the subunit composition, hence can vary across
CC       tissues (Probable). {ECO:0000255|HAMAP-Rule:MF_03184,
CC       ECO:0000305}.
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         Note=No experimental confirmation available.;
CC   -!- PTM: GlcNAcylation decreases enzyme activity. {ECO:0000250}.
CC   -!- MISCELLANEOUS: In human PFK exists as a system of 3 types of
CC       subunits, PFKM (muscle), PFKL (liver) and PFKP (platelet)
CC       isoenzymes.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
CC       family. ATP-dependent PFK group I subfamily. Eukaryotic two domain
CC       clade "E" sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}.
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   UniGene; Hs.26010; -.
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   ProteinModelPortal; Q01813; -.
DR   SMR; Q01813; -.
DR   BioGrid; 111235; 88.
DR   ComplexPortal; CPX-1999; 6-phosphofructokinase, P4 homotetramer.
DR   DIP; DIP-45850N; -.
DR   IntAct; Q01813; 39.
DR   MINT; Q01813; -.
DR   STRING; 9606.ENSP00000370517; -.
DR   iPTMnet; Q01813; -.
DR   PhosphoSitePlus; Q01813; -.
DR   SwissPalm; Q01813; -.
DR   BioMuta; PFKP; -.
DR   DMDM; 1346355; -.
DR   EPD; Q01813; -.
DR   jPOST; Q01813; -.
DR   MaxQB; Q01813; -.
DR   PaxDb; Q01813; -.
DR   PeptideAtlas; Q01813; -.
DR   PRIDE; Q01813; -.
DR   ProteomicsDB; 57992; -.
DR   DNASU; 5214; -.
DR   Ensembl; ENST00000381075; ENSP00000370465; ENSG00000067057. [Q01813-2]
DR   Ensembl; ENST00000381125; ENSP00000370517; ENSG00000067057. [Q01813-1]
DR   GeneID; 5214; -.
DR   KEGG; hsa:5214; -.
DR   UCSC; uc001igp.4; human. [Q01813-1]
DR   CTD; 5214; -.
DR   DisGeNET; 5214; -.
DR   EuPathDB; HostDB:ENSG00000067057.16; -.
DR   GeneCards; PFKP; -.
DR   HGNC; HGNC:8878; PFKP.
DR   HPA; HPA018257; -.
DR   HPA; HPA056484; -.
DR   MIM; 171840; gene.
DR   neXtProt; NX_Q01813; -.
DR   OpenTargets; ENSG00000067057; -.
DR   PharmGKB; PA33217; -.
DR   eggNOG; KOG2440; Eukaryota.
DR   eggNOG; COG0205; LUCA.
DR   GeneTree; ENSGT00940000155002; -.
DR   HOGENOM; HOG000200154; -.
DR   HOVERGEN; HBG000976; -.
DR   InParanoid; Q01813; -.
DR   KO; K00850; -.
DR   OMA; PLVECVQ; -.
DR   OrthoDB; 172878at2759; -.
DR   PhylomeDB; Q01813; -.
DR   TreeFam; TF300411; -.
DR   BioCyc; MetaCyc:HS00894-MONOMER; -.
DR   Reactome; R-HSA-70171; Glycolysis.
DR   SABIO-RK; Q01813; -.
DR   UniPathway; UPA00109; UER00182.
DR   ChiTaRS; PFKP; human.
DR   GeneWiki; PFKP; -.
DR   GenomeRNAi; 5214; -.
DR   PRO; PR:Q01813; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   Bgee; ENSG00000067057; Expressed in 232 organ(s), highest expression level in testis.
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; EXP:Reactome.
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   GO; GO:0006007; P:glucose catabolic process; IBA:GO_Central.
DR   HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR   InterPro; IPR009161; 6-Pfructokinase_euk.
DR   InterPro; IPR022953; ATP_PFK.
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; Complete proteome; Cytoplasm; Glycolysis; Glycoprotein;
KW   Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN         1    784       ATP-dependent 6-phosphofructokinase,
FT                                platelet type.
FT                                /FTId=PRO_0000112024.
FT   NP_BIND      97     98       ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   NP_BIND     127    130       ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   REGION        1    399       N-terminal catalytic PFK domain 1.
FT   REGION      173    175       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      217    219       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      307    310       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      400    411       Interdomain linker.
FT   REGION      412    784       C-terminal regulatory PFK domain 2.
FT   REGION      538    542       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      583    585       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      671    674       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   ACT_SITE    175    175       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   METAL       128    128       Magnesium; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING      34     34       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     210    210       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     273    273       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     301    301       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     481    481       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     576    576       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     639    639       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     665    665       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     744    744       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000244|PubMed:19413330}.
FT   MOD_RES       6      6       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES      12     12       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P47859}.
FT   MOD_RES      21     21       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     142    142       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P47860}.
FT   MOD_RES     386    386       Phosphoserine.
FT                                {ECO:0000244|PubMed:16964243,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:18691976,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     395    395       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     486    486       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     651    651       Phosphotyrosine.
FT                                {ECO:0000244|PubMed:15592455}.
FT   MOD_RES     688    688       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     783    783       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:18691976,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231}.
FT   CARBOHYD    540    540       O-linked (GlcNAc) serine. {ECO:0000250}.
FT   VAR_SEQ       1     87       MDADDSRAPKGSLRKFLEHLSGAGKAIGVLTSGGDAQGMNA
FT                                AVRAVVRMGIYVGAKVYFIYEGYQGMVDGGSNIAEADWESV
FT                                SSILQ -> MCGYERCRPCRGAHGYLRGGQGVLHLRGLPGH
FT                                GGRRLKHRRGRLGECLQHPASGAVRGDWREKPGCWSHRFPC
FT                                PGRHAL (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_046416.
FT   CONFLICT    484    485       PG -> IP (in Ref. 5). {ECO:0000305}.
FT   CONFLICT    498    498       Missing (in Ref. 5; AAA36435).
FT                                {ECO:0000305}.
FT   CONFLICT    655    655       S -> P (in Ref. 2; BAG52577).
FT                                {ECO:0000305}.
FT   CONFLICT    699    699       A -> E (in Ref. 5; AAA36435).
FT                                {ECO:0000305}.
FT   TURN         17     19       {ECO:0000244|PDB:4XYJ}.
FT   STRAND       26     31       {ECO:0000244|PDB:4XZ2}.
FT   HELIX        39     53       {ECO:0000244|PDB:4XZ2}.
FT   STRAND       56     60       {ECO:0000244|PDB:4XZ2}.
FT   HELIX        63     69       {ECO:0000244|PDB:4XZ2}.
FT   HELIX        71     73       {ECO:0000244|PDB:4XZ2}.
FT   STRAND       74     76       {ECO:0000244|PDB:4XZ2}.
FT   HELIX        79     81       {ECO:0000244|PDB:4XZ2}.
FT   TURN         83     87       {ECO:0000244|PDB:4RH3}.
FT   STRAND       88     90       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       100    102       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       104    116       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      119    126       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       128    139       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       140    142       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       143    149       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      150    152       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       155    160       {ECO:0000244|PDB:4XZ2}.
FT   TURN        161    163       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      166    171       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      179    183       {ECO:0000244|PDB:4XYK}.
FT   HELIX       187    208       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      210    217       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       223    232       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      235    238       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      240    242       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       248    261       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      266    272       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      278    280       {ECO:0000244|PDB:4XYK}.
FT   HELIX       285    296       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      300    304       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       306    310       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       316    335       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      338    340       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      343    348       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      351    356       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       357    373       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       376    383       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       385    398       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       403    405       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      412    420       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       425    438       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      442    446       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       449    454       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      458    460       {ECO:0000244|PDB:4XZ2}.
FT   TURN        463    468       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      474    477       {ECO:0000244|PDB:4XYJ}.
FT   HELIX       484    487       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       488    497       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      500    508       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       509    520       {ECO:0000244|PDB:4XZ2}.
FT   TURN        521    524       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       526    528       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      532    540       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       552    568       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      570    573       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      576    582       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       589    598       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      601    604       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      606    608       {ECO:0000244|PDB:4XYJ}.
FT   HELIX       612    625       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      632    638       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      643    645       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       647    657       {ECO:0000244|PDB:4XZ2}.
FT   TURN        658    661       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      663    668       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       670    673       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       680    702       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       714    716       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      717    723       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      726    731       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       732    735       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       736    738       {ECO:0000244|PDB:4U1R}.
FT   TURN        741    744       {ECO:0000244|PDB:4XZ2}.
FT   STRAND      745    748       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       750    755       {ECO:0000244|PDB:4XZ2}.
FT   HELIX       756    761       {ECO:0000244|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
//
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