(data stored in ACNUC4932 zone)

HOVERGEN: F264_HUMAN

ID   F264_HUMAN              Reviewed;         469 AA.
AC   Q16877; Q5S3G5;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 6.
DT   03-NOV-2009, entry version 94.
DE   RecName: Full=6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4;
DE   AltName: Full=6PF-2-K/Fru-2,6-P2ASE testis-type isozyme;
DE   Includes:
DE     RecName: Full=6-phosphofructo-2-kinase;
DE              EC=2.7.1.105;
DE   Includes:
DE     RecName: Full=Fructose-2,6-bisphosphatase;
DE              EC=3.1.3.46;
GN   Name=PFKFB4;
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].
RA   Sakakibara R.;
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   MEDLINE=99196986; PubMed=10095107; DOI=10.1016/S0378-1119(99)00037-2;
RA   Manzano A., Perez J.X., Nadal M., Estivill X., Lange A., Bartrons R.;
RT   "Cloning, expression and chromosomal localization of a human testis 6-
RT   phosphofructo-2-kinase/fructose-2,6-bisphosphatase gene.";
RL   Gene 229:83-89(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15642344; DOI=10.1016/j.febslet.2004.11.096;
RA   Gomez M., Manzano A., Navarro-Sabate A., Duran J., Obach M.,
RA   Perales J.C., Bartrons R.;
RT   "Specific expression of pfkfb4 gene in spermatogonia germ cells and
RT   analysis of its 5'-flanking region.";
RL   FEBS Lett. 579:357-362(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=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   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 357-469.
RC   TISSUE=Placenta;
RX   MEDLINE=96271013; PubMed=8830046;
RA   Sakai A., Kato M., Fukasawa M., Ishiguro M., Furuya E., Sakakibara R.;
RT   "Cloning of cDNA encoding for a novel isozyme of fructose 6-phosphate,
RT   2-kinase/fructose 2,6-bisphosphatase from human placenta.";
RL   J. Biochem. 119:506-511(1996).
RN   [7]
RP   VARIANT [LARGE SCALE ANALYSIS] LYS-181.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.
CC   -!- CATALYTIC ACTIVITY: Beta-D-fructose 2,6-bisphosphate + H(2)O = D-
CC       fructose 6-phosphate + phosphate.
CC   -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + beta-D-
CC       fructose 2,6-bisphosphate.
CC   -!- ENZYME REGULATION: The most important regulatory mechanism of
CC       these opposing activities is by phosphorylation and
CC       dephosphorylation of the enzyme (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       phosphoglycerate mutase family.
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CC   -!- GENE_FAMILY: HBG005628 [ FAMILY / ALN / TREE ]
DR   EMBL; D49818; BAA18921.1; -; mRNA.
DR   EMBL; AF108765; AAD09427.1; -; mRNA.
DR   EMBL; AY786551; AAV65753.1; -; Genomic_DNA.
DR   EMBL; CH471055; EAW64890.1; -; Genomic_DNA.
DR   EMBL; BC010269; AAH10269.1; -; mRNA.
DR   IPI; IPI00220070; -.
DR   PIR; JC5871; JC5871.
DR   RefSeq; NP_004558.1; -.
DR   UniGene; Hs.476217; -.
DR   HSSP; P25114; 1BIF.
DR   SMR; Q16877; 38-469.
DR   STRING; Q16877; -.
DR   PhosphoSite; Q16877; -.
DR   PRIDE; Q16877; -.
DR   Ensembl; ENST00000232375; ENSP00000232375; ENSG00000114268; Homo sapiens.
DR   Ensembl; ENST00000383734; ENSP00000373240; ENSG00000114268; Homo sapiens.
DR   Ensembl; ENST00000412035; ENSP00000393047; ENSG00000114268; Homo sapiens.
DR   Ensembl; ENST00000416568; ENSP00000388394; ENSG00000114268; Homo sapiens.
DR   Ensembl; ENST00000417753; ENSP00000389169; ENSG00000114268; Homo sapiens.
DR   Ensembl; ENST00000422701; ENSP00000415764; ENSG00000114268; Homo sapiens.
DR   Ensembl; ENST00000445633; ENSP00000400772; ENSG00000114268; Homo sapiens.
DR   Ensembl; ENST00000452531; ENSP00000407657; ENSG00000114268; Homo sapiens.
DR   GeneID; 5210; -.
DR   KEGG; hsa:5210; -.
DR   UCSC; uc003ctv.1; human.
DR   CTD; 5210; -.
DR   GeneCards; GC03M048530; -.
DR   H-InvDB; HIX0003288; -.
DR   HGNC; HGNC:8875; PFKFB4.
DR   MIM; 605320; gene.
DR   PharmGKB; PA33214; -.
DR   HOGENOM; Q16877; -.
DR   HOVERGEN; Q16877; -.
DR   OMA; SYETLDE; -.
DR   BRENDA; 2.7.1.105; 247.
DR   BRENDA; 3.1.3.46; 247.
DR   Reactome; REACT_1505; Integration of energy metabolism.
DR   Reactome; REACT_15380; Diabetes pathways.
DR   Reactome; REACT_474; Metabolism of carbohydrates.
DR   NextBio; 20150; -.
DR   ArrayExpress; Q16877; -.
DR   Bgee; Q16877; -.
DR   CleanEx; HS_PFKFB4; -.
DR   Genevestigator; Q16877; -.
DR   GermOnline; ENSG00000114268; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0003873; F:6-phosphofructo-2-kinase activity; NAS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase act...; IEA:EC.
DR   GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; NAS:UniProtKB.
DR   InterPro; IPR003094; 6Pfruct_kin.
DR   InterPro; IPR013079; 6Phosfructo_kin.
DR   InterPro; IPR016260; Bifunct_6PFK/fruc_bisP_Ptase.
DR   InterPro; IPR001345; PG/BPGM_mutase_AC.
DR   InterPro; IPR013078; PG_mutase.
DR   PANTHER; PTHR10606; 6Pfruct_kin; 1.
DR   Pfam; PF01591; 6PF2K; 1.
DR   Pfam; PF00300; PGAM; 1.
DR   PIRSF; PIRSF000709; 6PFK_2-Ptase; 1.
DR   PRINTS; PR00991; 6PFRUCTKNASE.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; Q16877.
DR   SWISS-2DPAGE; Q16877.
KW   ATP-binding; Complete proteome; Hydrolase; Kinase;
KW   Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
KW   Polymorphism; Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    469       6-phosphofructo-2-kinase/fructose-2,6-
FT                                biphosphatase 4.
FT                                /FTId=PRO_0000179970.
FT   NP_BIND      46     53       ATP (By similarity).
FT   REGION        2    249       6-phosphofructo-2-kinase.
FT   REGION      250    469       Fructose-2,6-bisphosphatase.
FT   ACT_SITE    129    129       Potential.
FT   ACT_SITE    159    159       Potential.
FT   ACT_SITE    257    257       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   ACT_SITE    326    326       Potential.
FT   ACT_SITE    391    391       Proton donor (By similarity).
FT   BINDING     103    103       Fructose-6-phosphate (By similarity).
FT   BINDING     194    194       Fructose-6-phosphate (By similarity).
FT   MOD_RES     444    444       Phosphothreonine; by PKC (Potential).
FT   VARIANT     181    181       N -> K (in a breast cancer sample;
FT                                somatic mutation).
FT                                /FTId=VAR_036075.
SQ   SEQUENCE   469 AA;  54040 MW;  7E190C3C0A197D9F CRC64;
     MASPRELTQN PLKKIWMPYS NGRPALHACQ RGVCMTNCPT LIVMVGLPAR GKTYISKKLT
     RYLNWIGVPT REFNVGQYRR DVVKTYKSFE FFLPDNEEGL KIRKQCALAA LRDVRRFLSE
     EGGHVAVFDA TNTTRERRAT IFNFGEQNGY KTFFVESICV DPEVIAANIV QVKLGSPDYV
     NRDSDEATED FMRRIECYEN SYESLDEDLD RDLSYIKIMD VGQSYVVNRV ADHIQSRIVY
     YLMNIHVTPR SIYLCRHGES ELNLKGRIGG DPGLSPRGRE FAKSLAQFIS DQNIKDLKVW
     TSQMKRTIQT AEALGVPYEQ WKVLNEIDAG VCEEMTYEEI QDNYPLEFAL RDQDKYRYRY
     PKGESYEDLV QRLEPVIMEL ERQENVLVIC HQAVMRCLLA YFLDKAAEQL PYLKCPLHTV
     LKLTPVAYGC KVESIFLNVA AVNTHRDRPQ NVDISRPPEE ALVTVPAHQ
//

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