Full text data of PFKP
PFKP
(PFKF)
[Confidence: low (only semi-automatic identification from reviews)]
6-phosphofructokinase type C; 2.7.1.11 (6-phosphofructokinase, platelet type; Phosphofructo-1-kinase isozyme C; PFK-C; Phosphofructokinase 1; Phosphohexokinase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
6-phosphofructokinase type C; 2.7.1.11 (6-phosphofructokinase, platelet type; Phosphofructo-1-kinase isozyme C; PFK-C; Phosphofructokinase 1; Phosphohexokinase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q01813
ID K6PP_HUMAN Reviewed; 784 AA.
AC Q01813; B3KS15; Q5VSR7; Q5VSR8;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1996, sequence version 2.
DT 22-JAN-2014, entry version 149.
DE RecName: Full=6-phosphofructokinase type C;
DE EC=2.7.1.11;
DE AltName: Full=6-phosphofructokinase, platelet type;
DE AltName: Full=Phosphofructo-1-kinase isozyme C;
DE Short=PFK-C;
DE AltName: Full=Phosphofructokinase 1;
DE AltName: Full=Phosphohexokinase;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-651, AND MASS
RP SPECTROMETRY.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, AND MASS
RP SPECTROMETRY.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386 AND SER-783, AND
RP MASS SPECTROMETRY.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386 AND SER-783, AND
RP MASS SPECTROMETRY.
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, AND MASS
RP SPECTROMETRY.
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-395; LYS-486 AND LYS-688,
RP AND MASS SPECTROMETRY.
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386 AND SER-783, AND
RP MASS SPECTROMETRY.
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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, AND MASS
RP SPECTROMETRY.
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).
CC -!- FUNCTION: Catalyzes the third step of glycolysis, the
CC phosphorylation of fructose-6-phosphate (F6P) by ATP to generate
CC fructose-1,6-bisphosphate (FBP) and ADP.
CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
CC fructose 1,6-bisphosphate.
CC -!- COFACTOR: Magnesium.
CC -!- ENZYME REGULATION: Allosteric enzyme activated by ADP, AMP, or
CC fructose bisphosphate and inhibited by ATP or citrate.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC -!- SUBUNIT: Tetramer. Muscle is M4, liver is L4, and red cell is M3L,
CC M2L2, or ML3. A subunit composition with a higher proportion of
CC platelet type subunits is found in platelets, brain and
CC fibroblasts.
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 (By similarity).
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 family. Two domains
CC subfamily.
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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; CAH69851.1; -; Genomic_DNA.
DR EMBL; AL451164; CAH69851.1; JOINED; Genomic_DNA.
DR EMBL; AL451164; CAI39999.1; -; Genomic_DNA.
DR EMBL; AL731533; CAI39999.1; JOINED; Genomic_DNA.
DR EMBL; BC002536; AAH02536.1; -; mRNA.
DR EMBL; BC029138; AAH29138.1; -; mRNA.
DR EMBL; M64784; AAA36435.1; -; mRNA.
DR PIR; JC2055; JC2055.
DR RefSeq; NP_001229268.1; NM_001242339.1.
DR RefSeq; NP_002618.1; NM_002627.4.
DR UniGene; Hs.26010; -.
DR ProteinModelPortal; Q01813; -.
DR SMR; Q01813; 22-765.
DR IntAct; Q01813; 15.
DR MINT; MINT-1159988; -.
DR STRING; 9606.ENSP00000370517; -.
DR BindingDB; Q01813; -.
DR PhosphoSite; Q01813; -.
DR DMDM; 1346355; -.
DR PaxDb; Q01813; -.
DR PeptideAtlas; Q01813; -.
DR PRIDE; Q01813; -.
DR DNASU; 5214; -.
DR Ensembl; ENST00000381075; ENSP00000370465; ENSG00000067057.
DR Ensembl; ENST00000381125; ENSP00000370517; ENSG00000067057.
DR GeneID; 5214; -.
DR KEGG; hsa:5214; -.
DR UCSC; uc001igp.3; human.
DR CTD; 5214; -.
DR GeneCards; GC10P003109; -.
DR HGNC; HGNC:8878; PFKP.
DR HPA; HPA018257; -.
DR MIM; 171840; gene.
DR neXtProt; NX_Q01813; -.
DR PharmGKB; PA33217; -.
DR eggNOG; COG0205; -.
DR HOGENOM; HOG000200154; -.
DR HOVERGEN; HBG000976; -.
DR InParanoid; Q01813; -.
DR KO; K00850; -.
DR OMA; PLVECVQ; -.
DR OrthoDB; EOG7ZSHV5; -.
DR PhylomeDB; Q01813; -.
DR BioCyc; MetaCyc:HS00894-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; Q01813; -.
DR UniPathway; UPA00109; UER00182.
DR ChiTaRS; PFKP; human.
DR GeneWiki; PFKP; -.
DR GenomeRNAi; 5214; -.
DR NextBio; 20168; -.
DR PRO; PR:Q01813; -.
DR ArrayExpress; Q01813; -.
DR Bgee; Q01813; -.
DR CleanEx; HS_PFKP; -.
DR Genevestigator; Q01813; -.
DR GO; GO:0005945; C:6-phosphofructokinase complex; NAS:UniProtKB.
DR GO; GO:0003872; F:6-phosphofructokinase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolysis; NAS:UniProtKB.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR InterPro; IPR009161; 6-phosphofructokinase_euk.
DR InterPro; IPR022953; Phosphofructokinase.
DR InterPro; IPR015912; Phosphofructokinase_CS.
DR InterPro; IPR000023; Phosphofructokinase_dom.
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 Acetylation; Allosteric enzyme; Alternative splicing; ATP-binding;
KW Complete proteome; Glycolysis; Glycoprotein; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat; Transferase.
FT CHAIN 1 784 6-phosphofructokinase type C.
FT /FTId=PRO_0000112024.
FT NP_BIND 44 48 ATP (By similarity).
FT NP_BIND 202 206 ATP (By similarity).
FT NP_BIND 219 235 ATP (By similarity).
FT ACT_SITE 175 175 Proton acceptor (By similarity).
FT METAL 233 233 Magnesium; via carbonyl oxygen (By
FT similarity).
FT BINDING 210 210 Substrate (By similarity).
FT BINDING 301 301 Substrate (By similarity).
FT BINDING 307 307 Substrate (By similarity).
FT BINDING 310 310 Substrate (By similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 12 12 Phosphoserine (By similarity).
FT MOD_RES 386 386 Phosphoserine.
FT MOD_RES 395 395 N6-acetyllysine.
FT MOD_RES 486 486 N6-acetyllysine.
FT MOD_RES 651 651 Phosphotyrosine.
FT MOD_RES 688 688 N6-acetyllysine.
FT MOD_RES 783 783 Phosphoserine.
FT CARBOHYD 540 540 O-linked (GlcNAc) (By similarity).
FT VAR_SEQ 1 87 MDADDSRAPKGSLRKFLEHLSGAGKAIGVLTSGGDAQGMNA
FT AVRAVVRMGIYVGAKVYFIYEGYQGMVDGGSNIAEADWESV
FT SSILQ -> MCGYERCRPCRGAHGYLRGGQGVLHLRGLPGH
FT GGRRLKHRRGRLGECLQHPASGAVRGDWREKPGCWSHRFPC
FT PGRHAL (in isoform 2).
FT /FTId=VSP_046416.
FT CONFLICT 484 485 PG -> IP (in Ref. 5).
FT CONFLICT 498 498 Missing (in Ref. 5; AAA36435).
FT CONFLICT 655 655 S -> P (in Ref. 2; BAG52577).
FT CONFLICT 699 699 A -> E (in Ref. 5; AAA36435).
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
//
ID K6PP_HUMAN Reviewed; 784 AA.
AC Q01813; B3KS15; Q5VSR7; Q5VSR8;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1996, sequence version 2.
DT 22-JAN-2014, entry version 149.
DE RecName: Full=6-phosphofructokinase type C;
DE EC=2.7.1.11;
DE AltName: Full=6-phosphofructokinase, platelet type;
DE AltName: Full=Phosphofructo-1-kinase isozyme C;
DE Short=PFK-C;
DE AltName: Full=Phosphofructokinase 1;
DE AltName: Full=Phosphohexokinase;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-651, AND MASS
RP SPECTROMETRY.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, AND MASS
RP SPECTROMETRY.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386 AND SER-783, AND
RP MASS SPECTROMETRY.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386 AND SER-783, AND
RP MASS SPECTROMETRY.
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, AND MASS
RP SPECTROMETRY.
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-395; LYS-486 AND LYS-688,
RP AND MASS SPECTROMETRY.
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386 AND SER-783, AND
RP MASS SPECTROMETRY.
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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, AND MASS
RP SPECTROMETRY.
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).
CC -!- FUNCTION: Catalyzes the third step of glycolysis, the
CC phosphorylation of fructose-6-phosphate (F6P) by ATP to generate
CC fructose-1,6-bisphosphate (FBP) and ADP.
CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
CC fructose 1,6-bisphosphate.
CC -!- COFACTOR: Magnesium.
CC -!- ENZYME REGULATION: Allosteric enzyme activated by ADP, AMP, or
CC fructose bisphosphate and inhibited by ATP or citrate.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC -!- SUBUNIT: Tetramer. Muscle is M4, liver is L4, and red cell is M3L,
CC M2L2, or ML3. A subunit composition with a higher proportion of
CC platelet type subunits is found in platelets, brain and
CC fibroblasts.
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 (By similarity).
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 family. Two domains
CC subfamily.
CC -----------------------------------------------------------------------
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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; CAH69851.1; -; Genomic_DNA.
DR EMBL; AL451164; CAH69851.1; JOINED; Genomic_DNA.
DR EMBL; AL451164; CAI39999.1; -; Genomic_DNA.
DR EMBL; AL731533; CAI39999.1; JOINED; Genomic_DNA.
DR EMBL; BC002536; AAH02536.1; -; mRNA.
DR EMBL; BC029138; AAH29138.1; -; mRNA.
DR EMBL; M64784; AAA36435.1; -; mRNA.
DR PIR; JC2055; JC2055.
DR RefSeq; NP_001229268.1; NM_001242339.1.
DR RefSeq; NP_002618.1; NM_002627.4.
DR UniGene; Hs.26010; -.
DR ProteinModelPortal; Q01813; -.
DR SMR; Q01813; 22-765.
DR IntAct; Q01813; 15.
DR MINT; MINT-1159988; -.
DR STRING; 9606.ENSP00000370517; -.
DR BindingDB; Q01813; -.
DR PhosphoSite; Q01813; -.
DR DMDM; 1346355; -.
DR PaxDb; Q01813; -.
DR PeptideAtlas; Q01813; -.
DR PRIDE; Q01813; -.
DR DNASU; 5214; -.
DR Ensembl; ENST00000381075; ENSP00000370465; ENSG00000067057.
DR Ensembl; ENST00000381125; ENSP00000370517; ENSG00000067057.
DR GeneID; 5214; -.
DR KEGG; hsa:5214; -.
DR UCSC; uc001igp.3; human.
DR CTD; 5214; -.
DR GeneCards; GC10P003109; -.
DR HGNC; HGNC:8878; PFKP.
DR HPA; HPA018257; -.
DR MIM; 171840; gene.
DR neXtProt; NX_Q01813; -.
DR PharmGKB; PA33217; -.
DR eggNOG; COG0205; -.
DR HOGENOM; HOG000200154; -.
DR HOVERGEN; HBG000976; -.
DR InParanoid; Q01813; -.
DR KO; K00850; -.
DR OMA; PLVECVQ; -.
DR OrthoDB; EOG7ZSHV5; -.
DR PhylomeDB; Q01813; -.
DR BioCyc; MetaCyc:HS00894-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; Q01813; -.
DR UniPathway; UPA00109; UER00182.
DR ChiTaRS; PFKP; human.
DR GeneWiki; PFKP; -.
DR GenomeRNAi; 5214; -.
DR NextBio; 20168; -.
DR PRO; PR:Q01813; -.
DR ArrayExpress; Q01813; -.
DR Bgee; Q01813; -.
DR CleanEx; HS_PFKP; -.
DR Genevestigator; Q01813; -.
DR GO; GO:0005945; C:6-phosphofructokinase complex; NAS:UniProtKB.
DR GO; GO:0003872; F:6-phosphofructokinase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolysis; NAS:UniProtKB.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR InterPro; IPR009161; 6-phosphofructokinase_euk.
DR InterPro; IPR022953; Phosphofructokinase.
DR InterPro; IPR015912; Phosphofructokinase_CS.
DR InterPro; IPR000023; Phosphofructokinase_dom.
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 Acetylation; Allosteric enzyme; Alternative splicing; ATP-binding;
KW Complete proteome; Glycolysis; Glycoprotein; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat; Transferase.
FT CHAIN 1 784 6-phosphofructokinase type C.
FT /FTId=PRO_0000112024.
FT NP_BIND 44 48 ATP (By similarity).
FT NP_BIND 202 206 ATP (By similarity).
FT NP_BIND 219 235 ATP (By similarity).
FT ACT_SITE 175 175 Proton acceptor (By similarity).
FT METAL 233 233 Magnesium; via carbonyl oxygen (By
FT similarity).
FT BINDING 210 210 Substrate (By similarity).
FT BINDING 301 301 Substrate (By similarity).
FT BINDING 307 307 Substrate (By similarity).
FT BINDING 310 310 Substrate (By similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 12 12 Phosphoserine (By similarity).
FT MOD_RES 386 386 Phosphoserine.
FT MOD_RES 395 395 N6-acetyllysine.
FT MOD_RES 486 486 N6-acetyllysine.
FT MOD_RES 651 651 Phosphotyrosine.
FT MOD_RES 688 688 N6-acetyllysine.
FT MOD_RES 783 783 Phosphoserine.
FT CARBOHYD 540 540 O-linked (GlcNAc) (By similarity).
FT VAR_SEQ 1 87 MDADDSRAPKGSLRKFLEHLSGAGKAIGVLTSGGDAQGMNA
FT AVRAVVRMGIYVGAKVYFIYEGYQGMVDGGSNIAEADWESV
FT SSILQ -> MCGYERCRPCRGAHGYLRGGQGVLHLRGLPGH
FT GGRRLKHRRGRLGECLQHPASGAVRGDWREKPGCWSHRFPC
FT PGRHAL (in isoform 2).
FT /FTId=VSP_046416.
FT CONFLICT 484 485 PG -> IP (in Ref. 5).
FT CONFLICT 498 498 Missing (in Ref. 5; AAA36435).
FT CONFLICT 655 655 S -> P (in Ref. 2; BAG52577).
FT CONFLICT 699 699 A -> E (in Ref. 5; AAA36435).
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
//
MIM
171840
*RECORD*
*FIELD* NO
171840
*FIELD* TI
*171840 PHOSPHOFRUCTOKINASE, PLATELET TYPE; PFKP
;;PFK, PLATELET TYPE;;
PFK, FIBROBLAST TYPE; PFKF
read more*FIELD* TX
DESCRIPTION
The PFKP gene encodes the platelet isoform of phosphofructokinase (PFK)
(ATP:D-fructose-6-phosphate-1-phosphotransferase, EC 2.7.1.11). PFK
catalyzes the irreversible conversion of fructose-6-phosphate to
fructose-1,6-bisphosphate and is a key regulatory enzyme in glycolysis.
The PFKP gene, which maps to chromosome 10p, is also expressed in
fibroblasts. See also the muscle (PFKM; 610681) and liver (PFKL; 171860)
isoforms of phosphofructokinase, which map to chromosomes 12q13 and
21q22, respectively.
Vora (1981) determined that full tetrameric phophofructokinase enzyme
expressed in platelets can be composed of subunits P4, P3L, and P2L2.
CLONING
Simpson and Fothergill-Gilmore (1991) isolated a cDNA corresponding to
the PFKP gene from a human lymphocyte Raji cell line cDNA library using
a cDNA for human muscle PFK as a probe. The deduced amino acid sequence
showed 71% identity to the amino acid sequence for the human muscle
isoenzyme and 63% identity to the human liver isoenzyme.
GENE FUNCTION
Yi et al. (2012) demonstrated that the dynamic posttranslational
modification of proteins by O-linked beta-N-acetylglucosamine
(O-GlcNAcylation) is a key metabolic regulator of glucose metabolism.
O-GlcNAcylation was induced at ser529 of phosphofructokinase-1 (PFK1) in
response to hypoxia. Glycosylation inhibited PFK1 activity and
redirected glucose flux through the pentose phosphate pathway, thereby
conferring a selective growth advantage on cancer cells. Blocking
glycosylation of PFK1 at ser529 reduced cancer cell proliferation in
vitro and impaired tumor formation in vivo.
MAPPING
Weil et al. (1980) developed a method of specific immunoprecipitation of
human PFK and used it to locate the structural gene for fibroblast PFK
(PFKF) to chromosome 10 in somatic cell hybrids. Vora et al. (1983)
assigned the PFKP gene to 10p by use of a mouse antihuman
P-subunit-specific antiserum in the study of human/rodent somatic cell
hybrids. A single discordant hybrid cell containing only 10q did not
express PFKP, and fibroblasts from a patient with duplication of 10p
exhibited PFK activity values 180% of normal.
Schwartz et al. (1984) confirmed the assignment of PFKP and hexokinase-1
(HK1; 142600) to 10p by dosage effects in a case of 10p partial trisomy.
The synteny of PFKP and HK1 may have functional significance because the
enzymes which they encode are the primary and secondary control points
of the glycolytic pathway.
By use of the cDNA clone as a biotinylated probe for in situ
hybridization to human chromosome spreads, Morrison et al. (1992)
assigned the PFKP gene to chromosome 10p15.3-p15.2.
NOMENCLATURE
Francke (1983) suggested that this form of PFK is best called the
'platelet' type and symbolized PFKP because it is the only form made by
platelets, whereas fibroblasts have more than one form of PFK.
*FIELD* SA
Gonzalez et al. (1983); Vora et al. (1980)
*FIELD* RF
1. Francke, U.: Personal Communication. New Haven, Conn. 8/1983.
2. Gonzalez, G. H.; Billerbeck, A. E. C.; Takayama, L. C.; Wajntal,
A.: Duplication 10p in a girl due to a maternal translocation t(10;14)(p11;q12). Am.
J. Med. Genet. 14: 159-167, 1983.
3. Morrison, N.; Simpson, C.; Fothergill-Gilmore, L.; Boyd, E.; Connor,
J. M.: Regional chromosomal assignment of the human platelet phosphofructokinase
gene to 10p15. Hum. Genet. 89: 105-106, 1992.
4. Schwartz, S.; Cohen, M. M.; Panny, S. R.; Beisel, J. H.; Vora,
S.: Duplication of chromosome 10p: confirmation of regional assignments
of platelet-type phosphofructokinase. Am. J. Hum. Genet. 36: 750-759,
1984.
5. Simpson, C. J.; Fothergill-Gilmore, L. A.: Isolation and sequence
of a cDNA encoding human platelet phosphofructokinase. Biochem. Biophys.
Res. Commun. 180: 197-203, 1991.
6. Vora, S.: Isozymes of human phosphofructokinase in blood cells
and cultured cell lines: molecular and genetic evidence for a trigenic
system. Blood 57: 724-732, 1981.
7. Vora, S.; Miranda, A. F.; Hernandez, E.; Francke, U.: Regional
assignment of the human gene for platelet-type phosphofructokinase
(PFKP) to chromosome 10p: novel use of polyspecific rodent antisera
to localize human enzyme genes. Hum. Genet. 63: 374-379, 1983.
8. Vora, S.; Seaman, C.; Durham, S.; Piomelli, S.: Isozymes of human
phosphofructokinase: identification and subunit structural characterization
of a new system. Proc. Nat. Acad. Sci. 77: 62-66, 1980.
9. Weil, D.; Cottreau, D.; Cong, N. V.; Rebourcet, R.; Foubert, C.;
Gross, M.-S.; Dreyfus, J.-C.; Kahn, A.: Assignment of the gene for
F-type phosphofructokinase to human chromosome 10 by somatic cell
hybridization and specific immunoprecipitation. Ann. Hum. Genet. 44:
11-16, 1980.
10. Yi, W.; Clark, P. M.; Mason, D. E.; Keenan, M. C.; Hill, C.; Goddard,
W. A., III; Peters, E. C.; Driggers, E. M.; Hsieh-Wilson, L. C.:
Phosphofructokinase 1 glycosylation regulates cell growth and metabolism. Science 337:
975-980, 2012.
*FIELD* CN
Ada Hamosh - updated: 9/6/2012
Cassandra L. Kniffin - reorganized: 3/8/2007
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
alopez: 09/07/2012
terry: 9/6/2012
carol: 3/8/2007
ckniffin: 2/26/2007
carol: 10/7/1999
warfield: 4/12/1994
carol: 6/10/1992
supermim: 3/16/1992
carol: 3/6/1992
carol: 2/23/1992
carol: 1/9/1992
*RECORD*
*FIELD* NO
171840
*FIELD* TI
*171840 PHOSPHOFRUCTOKINASE, PLATELET TYPE; PFKP
;;PFK, PLATELET TYPE;;
PFK, FIBROBLAST TYPE; PFKF
read more*FIELD* TX
DESCRIPTION
The PFKP gene encodes the platelet isoform of phosphofructokinase (PFK)
(ATP:D-fructose-6-phosphate-1-phosphotransferase, EC 2.7.1.11). PFK
catalyzes the irreversible conversion of fructose-6-phosphate to
fructose-1,6-bisphosphate and is a key regulatory enzyme in glycolysis.
The PFKP gene, which maps to chromosome 10p, is also expressed in
fibroblasts. See also the muscle (PFKM; 610681) and liver (PFKL; 171860)
isoforms of phosphofructokinase, which map to chromosomes 12q13 and
21q22, respectively.
Vora (1981) determined that full tetrameric phophofructokinase enzyme
expressed in platelets can be composed of subunits P4, P3L, and P2L2.
CLONING
Simpson and Fothergill-Gilmore (1991) isolated a cDNA corresponding to
the PFKP gene from a human lymphocyte Raji cell line cDNA library using
a cDNA for human muscle PFK as a probe. The deduced amino acid sequence
showed 71% identity to the amino acid sequence for the human muscle
isoenzyme and 63% identity to the human liver isoenzyme.
GENE FUNCTION
Yi et al. (2012) demonstrated that the dynamic posttranslational
modification of proteins by O-linked beta-N-acetylglucosamine
(O-GlcNAcylation) is a key metabolic regulator of glucose metabolism.
O-GlcNAcylation was induced at ser529 of phosphofructokinase-1 (PFK1) in
response to hypoxia. Glycosylation inhibited PFK1 activity and
redirected glucose flux through the pentose phosphate pathway, thereby
conferring a selective growth advantage on cancer cells. Blocking
glycosylation of PFK1 at ser529 reduced cancer cell proliferation in
vitro and impaired tumor formation in vivo.
MAPPING
Weil et al. (1980) developed a method of specific immunoprecipitation of
human PFK and used it to locate the structural gene for fibroblast PFK
(PFKF) to chromosome 10 in somatic cell hybrids. Vora et al. (1983)
assigned the PFKP gene to 10p by use of a mouse antihuman
P-subunit-specific antiserum in the study of human/rodent somatic cell
hybrids. A single discordant hybrid cell containing only 10q did not
express PFKP, and fibroblasts from a patient with duplication of 10p
exhibited PFK activity values 180% of normal.
Schwartz et al. (1984) confirmed the assignment of PFKP and hexokinase-1
(HK1; 142600) to 10p by dosage effects in a case of 10p partial trisomy.
The synteny of PFKP and HK1 may have functional significance because the
enzymes which they encode are the primary and secondary control points
of the glycolytic pathway.
By use of the cDNA clone as a biotinylated probe for in situ
hybridization to human chromosome spreads, Morrison et al. (1992)
assigned the PFKP gene to chromosome 10p15.3-p15.2.
NOMENCLATURE
Francke (1983) suggested that this form of PFK is best called the
'platelet' type and symbolized PFKP because it is the only form made by
platelets, whereas fibroblasts have more than one form of PFK.
*FIELD* SA
Gonzalez et al. (1983); Vora et al. (1980)
*FIELD* RF
1. Francke, U.: Personal Communication. New Haven, Conn. 8/1983.
2. Gonzalez, G. H.; Billerbeck, A. E. C.; Takayama, L. C.; Wajntal,
A.: Duplication 10p in a girl due to a maternal translocation t(10;14)(p11;q12). Am.
J. Med. Genet. 14: 159-167, 1983.
3. Morrison, N.; Simpson, C.; Fothergill-Gilmore, L.; Boyd, E.; Connor,
J. M.: Regional chromosomal assignment of the human platelet phosphofructokinase
gene to 10p15. Hum. Genet. 89: 105-106, 1992.
4. Schwartz, S.; Cohen, M. M.; Panny, S. R.; Beisel, J. H.; Vora,
S.: Duplication of chromosome 10p: confirmation of regional assignments
of platelet-type phosphofructokinase. Am. J. Hum. Genet. 36: 750-759,
1984.
5. Simpson, C. J.; Fothergill-Gilmore, L. A.: Isolation and sequence
of a cDNA encoding human platelet phosphofructokinase. Biochem. Biophys.
Res. Commun. 180: 197-203, 1991.
6. Vora, S.: Isozymes of human phosphofructokinase in blood cells
and cultured cell lines: molecular and genetic evidence for a trigenic
system. Blood 57: 724-732, 1981.
7. Vora, S.; Miranda, A. F.; Hernandez, E.; Francke, U.: Regional
assignment of the human gene for platelet-type phosphofructokinase
(PFKP) to chromosome 10p: novel use of polyspecific rodent antisera
to localize human enzyme genes. Hum. Genet. 63: 374-379, 1983.
8. Vora, S.; Seaman, C.; Durham, S.; Piomelli, S.: Isozymes of human
phosphofructokinase: identification and subunit structural characterization
of a new system. Proc. Nat. Acad. Sci. 77: 62-66, 1980.
9. Weil, D.; Cottreau, D.; Cong, N. V.; Rebourcet, R.; Foubert, C.;
Gross, M.-S.; Dreyfus, J.-C.; Kahn, A.: Assignment of the gene for
F-type phosphofructokinase to human chromosome 10 by somatic cell
hybridization and specific immunoprecipitation. Ann. Hum. Genet. 44:
11-16, 1980.
10. Yi, W.; Clark, P. M.; Mason, D. E.; Keenan, M. C.; Hill, C.; Goddard,
W. A., III; Peters, E. C.; Driggers, E. M.; Hsieh-Wilson, L. C.:
Phosphofructokinase 1 glycosylation regulates cell growth and metabolism. Science 337:
975-980, 2012.
*FIELD* CN
Ada Hamosh - updated: 9/6/2012
Cassandra L. Kniffin - reorganized: 3/8/2007
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
alopez: 09/07/2012
terry: 9/6/2012
carol: 3/8/2007
ckniffin: 2/26/2007
carol: 10/7/1999
warfield: 4/12/1994
carol: 6/10/1992
supermim: 3/16/1992
carol: 3/6/1992
carol: 2/23/1992
carol: 1/9/1992