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6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 (6PF-2-K/Fru-2,6-P2ase 3) (PFK/FBPase 3) (6PF-2-K/Fru-2,6-P2ase brain/placenta-type isozyme) (Renal carcinoma antigen NY-REN-56) (iPFK-2) [Includes: 6-phosphofructo-2-kinase (EC 2.7.1.105); Fructose-2,6-bisphosphatase (EC 3.1.3.46)]

 F263_HUMAN              Reviewed;         520 AA.
Q16875; B7Z955; O43622; O75902; Q5VX15; Q5VX18; Q5VX19;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 189.
RecName: Full=6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3;
Short=6PF-2-K/Fru-2,6-P2ase 3;
Short=PFK/FBPase 3;
AltName: Full=6PF-2-K/Fru-2,6-P2ase brain/placenta-type isozyme;
AltName: Full=Renal carcinoma antigen NY-REN-56;
AltName: Full=iPFK-2;
Includes:
RecName: Full=6-phosphofructo-2-kinase;
EC=2.7.1.105;
Includes:
RecName: Full=Fructose-2,6-bisphosphatase;
EC=3.1.3.46;
Name=PFKFB3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=8830046; DOI=10.1093/oxfordjournals.jbchem.a021270;
Sakai A., Kato M., Fukasawa M., Ishiguro M., Furuya E., Sakakibara R.;
"Cloning of cDNA encoding for a novel isozyme of fructose 6-phosphate,
2-kinase/fructose 2,6-bisphosphatase from human placenta.";
J. Biochem. 119:506-511(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9146922; DOI=10.1023/A:1018482511456;
Nicholl J., Hamilton J.A., Sutherland G.R., Sutherland R.L.,
Watts C.K.;
"The third human isoform of 6-phosphofructo-2-kinase/fructose-2,6-
bisphosphatase (PFKFB3) map position 10p14-p15.";
Chromosome Res. 5:150-150(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10072580;
Manzano A., Rosa J.L., Ventura F., Perez J.X., Nadal M., Estivill X.,
Ambrosio S., Gil J., Bartrons R.;
"Molecular cloning, expression, and chromosomal localization of a
ubiquitously expressed human 6-phosphofructo-2-kinase/ fructose-2, 6-
bisphosphatase gene (PFKFB3).";
Cytogenet. Cell Genet. 83:214-217(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
TISSUE=Brain;
El-Maghrabi M.R.;
"Human brain 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase.";
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Skeletal muscle;
PubMed=10077634; DOI=10.1073/pnas.96.6.3047;
Chesney J., Mitchell R.A., Benigni F., Bacher M., Spiegel L.,
Al-Abed Y., Han J.H., Metz C., Bucala R.;
"An inducible gene product for 6-phosphofructo-2-kinase with an AU-
rich instability element: role in tumor cell glycolysis and the
Warburg effect.";
Proc. Natl. Acad. Sci. U.S.A. 96:3047-3052(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-
cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[11]
PHOSPHORYLATION AT SER-461.
PubMed=12065600; DOI=10.1074/jbc.M205213200;
Marsin A.S., Bouzin C., Bertrand L., Hue L.;
"The stimulation of glycolysis by hypoxia in activated monocytes is
mediated by AMP-activated protein kinase and inducible 6-
phosphofructo-2-kinase.";
J. Biol. Chem. 277:30778-30783(2002).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461; THR-463 AND
SER-467, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461 AND SER-467, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461 AND SER-467, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH ADP AND
FRUCTOSE 6-PHOSPHATE.
PubMed=16316985; DOI=10.1074/jbc.M511019200;
Kim S.G., Manes N.P., El-Maghrabi M.R., Lee Y.H.;
"Crystal structure of the hypoxia-inducible form of 6-phosphofructo-2-
kinase/fructose-2,6-bisphosphatase (PFKFB3): a possible new target for
cancer therapy.";
J. Biol. Chem. 281:2939-2944(2006).
[17]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEXES WITH ADP; ATP;
FRUCTOSE 6-PHOSPHATE; FRUCTOSE-2,6-BISPHOSPHATE AND
PHOSPHOENOLPYRUVATE.
PubMed=17499765; DOI=10.1016/j.jmb.2007.03.038;
Kim S.G., Cavalier M., El-Maghrabi M.R., Lee Y.H.;
"A direct substrate-substrate interaction found in the kinase domain
of the bifunctional enzyme, 6-phosphofructo-2-kinase/fructose-2,6-
bisphosphatase.";
J. Mol. Biol. 370:14-26(2007).
[18]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS), AND ACTIVE SITE.
PubMed=22275052; DOI=10.1002/prot.24015;
Cavalier M.C., Kim S.G., Neau D., Lee Y.H.;
"Molecular basis of the fructose-2,6-bisphosphatase reaction of
PFKFB3: transition state and the C-terminal function.";
Proteins 80:1143-1153(2012).
[19]
X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) IN COMPLEX WITH
FRUCTOSE-2,6-BISPHOSPHATE.
PubMed=25849762; DOI=10.1021/acs.jmedchem.5b00352;
Boyd S., Brookfield J.L., Critchlow S.E., Cumming I.A., Curtis N.J.,
Debreczeni J., Degorce S.L., Donald C., Evans N.J., Groombridge S.,
Hopcroft P., Jones N.P., Kettle J.G., Lamont S., Lewis H.J.,
MacFaull P., McLoughlin S.B., Rigoreau L.J., Smith J.M., St-Gallay S.,
Stock J.K., Turnbull A.P., Wheatley E.R., Winter J., Wingfield J.;
"Structure-based design of potent and selective inhibitors of the
metabolic kinase PFKFB3.";
J. Med. Chem. 58:3611-3625(2015).
-!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.
-!- CATALYTIC ACTIVITY: Beta-D-fructose 2,6-bisphosphate + H(2)O = D-
fructose 6-phosphate + phosphate.
-!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + beta-D-
fructose 2,6-bisphosphate.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q16875-1; Sequence=Displayed;
Name=2;
IsoId=Q16875-2; Sequence=VSP_004680;
Name=3;
IsoId=Q16875-3; Sequence=VSP_047165;
Note=Gene prediction based on EST data.;
Name=4;
IsoId=Q16875-4; Sequence=VSP_054549;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- PTM: Phosphorylation by AMPK stimulates activity.
{ECO:0000269|PubMed:12065600}.
-!- SIMILARITY: In the C-terminal section; belongs to the
phosphoglycerate mutase family. {ECO:0000305}.
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EMBL; D49817; BAA08624.1; -; mRNA.
EMBL; L77662; AAL40083.1; -; mRNA.
EMBL; AF109735; AAD08818.1; -; mRNA.
EMBL; AF041831; AAB99795.1; -; Genomic_DNA.
EMBL; AF041823; AAB99795.1; JOINED; Genomic_DNA.
EMBL; AF041824; AAB99795.1; JOINED; Genomic_DNA.
EMBL; AF041825; AAB99795.1; JOINED; Genomic_DNA.
EMBL; AF041826; AAB99795.1; JOINED; Genomic_DNA.
EMBL; AF041827; AAB99795.1; JOINED; Genomic_DNA.
EMBL; AF041828; AAB99795.1; JOINED; Genomic_DNA.
EMBL; AF041829; AAB99795.1; JOINED; Genomic_DNA.
EMBL; AF041830; AAB99795.1; JOINED; Genomic_DNA.
EMBL; AF056320; AAC62000.1; -; mRNA.
EMBL; AK291263; BAF83952.1; -; mRNA.
EMBL; AK304450; BAH14191.1; -; mRNA.
EMBL; AL359960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL157395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471072; EAW86398.1; -; Genomic_DNA.
EMBL; CH471072; EAW86399.1; -; Genomic_DNA.
EMBL; BC040482; AAH40482.1; -; mRNA.
CCDS; CCDS44353.1; -. [Q16875-3]
CCDS; CCDS60479.1; -. [Q16875-4]
CCDS; CCDS7078.1; -. [Q16875-1]
CCDS; CCDS81439.1; -. [Q16875-2]
PIR; JC4626; JC4626.
RefSeq; NP_001269559.1; NM_001282630.2. [Q16875-4]
RefSeq; NP_001300992.1; NM_001314063.1. [Q16875-2]
RefSeq; NP_004557.1; NM_004566.3. [Q16875-1]
UniGene; Hs.195471; -.
PDB; 2AXN; X-ray; 2.10 A; A=1-520.
PDB; 2DWO; X-ray; 2.25 A; A=1-520.
PDB; 2DWP; X-ray; 2.70 A; A=1-520.
PDB; 2I1V; X-ray; 2.50 A; B=1-520.
PDB; 3QPU; X-ray; 2.30 A; A=1-520.
PDB; 3QPV; X-ray; 2.50 A; A=1-520.
PDB; 3QPW; X-ray; 2.25 A; A=1-520.
PDB; 4D4J; X-ray; 3.00 A; A=1-449.
PDB; 4D4K; X-ray; 3.24 A; A=1-449.
PDB; 4D4L; X-ray; 3.16 A; A=1-449.
PDB; 4D4M; X-ray; 2.32 A; A=1-449.
PDB; 4MA4; X-ray; 2.23 A; A=1-520.
PDB; 5AJV; X-ray; 3.01 A; B=1-520.
PDB; 5AJW; X-ray; 2.50 A; A=1-520.
PDB; 5AJX; X-ray; 2.58 A; A=1-520.
PDB; 5AJY; X-ray; 2.37 A; A=1-520.
PDB; 5AJZ; X-ray; 2.35 A; A=1-520.
PDB; 5AK0; X-ray; 2.03 A; A=1-520.
PDBsum; 2AXN; -.
PDBsum; 2DWO; -.
PDBsum; 2DWP; -.
PDBsum; 2I1V; -.
PDBsum; 3QPU; -.
PDBsum; 3QPV; -.
PDBsum; 3QPW; -.
PDBsum; 4D4J; -.
PDBsum; 4D4K; -.
PDBsum; 4D4L; -.
PDBsum; 4D4M; -.
PDBsum; 4MA4; -.
PDBsum; 5AJV; -.
PDBsum; 5AJW; -.
PDBsum; 5AJX; -.
PDBsum; 5AJY; -.
PDBsum; 5AJZ; -.
PDBsum; 5AK0; -.
ProteinModelPortal; Q16875; -.
SMR; Q16875; -.
BioGrid; 111230; 15.
ComplexPortal; CPX-1995; 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3 complex.
DIP; DIP-33964N; -.
IntAct; Q16875; 6.
STRING; 9606.ENSP00000369100; -.
BindingDB; Q16875; -.
ChEMBL; CHEMBL2331053; -.
GuidetoPHARMACOLOGY; 2937; -.
DEPOD; Q16875; -.
iPTMnet; Q16875; -.
PhosphoSitePlus; Q16875; -.
BioMuta; PFKFB3; -.
DMDM; 3023733; -.
PaxDb; Q16875; -.
PeptideAtlas; Q16875; -.
PRIDE; Q16875; -.
ProteomicsDB; 61114; -.
ProteomicsDB; 61115; -. [Q16875-2]
DNASU; 5209; -.
Ensembl; ENST00000360521; ENSP00000353712; ENSG00000170525. [Q16875-2]
Ensembl; ENST00000379775; ENSP00000369100; ENSG00000170525. [Q16875-1]
Ensembl; ENST00000379789; ENSP00000369115; ENSG00000170525. [Q16875-3]
Ensembl; ENST00000536985; ENSP00000443319; ENSG00000170525. [Q16875-4]
GeneID; 5209; -.
KEGG; hsa:5209; -.
UCSC; uc001ijd.4; human. [Q16875-1]
CTD; 5209; -.
DisGeNET; 5209; -.
EuPathDB; HostDB:ENSG00000170525.18; -.
GeneCards; PFKFB3; -.
HGNC; HGNC:8874; PFKFB3.
HPA; CAB020795; -.
HPA; HPA008266; -.
HPA; HPA043889; -.
MIM; 605319; gene.
neXtProt; NX_Q16875; -.
OpenTargets; ENSG00000170525; -.
PharmGKB; PA33213; -.
eggNOG; KOG0234; Eukaryota.
eggNOG; COG0406; LUCA.
GeneTree; ENSGT00390000018751; -.
HOGENOM; HOG000181112; -.
HOVERGEN; HBG005628; -.
InParanoid; Q16875; -.
KO; K01103; -.
OMA; MKRINCY; -.
OrthoDB; EOG091G0A43; -.
PhylomeDB; Q16875; -.
TreeFam; TF313541; -.
BioCyc; MetaCyc:HS10144-MONOMER; -.
BRENDA; 2.7.1.105; 2681.
BRENDA; 3.1.3.46; 2681.
Reactome; R-HSA-70171; Glycolysis.
SABIO-RK; Q16875; -.
SIGNOR; Q16875; -.
ChiTaRS; PFKFB3; human.
EvolutionaryTrace; Q16875; -.
GeneWiki; PFKFB3; -.
GenomeRNAi; 5209; -.
PRO; PR:Q16875; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000170525; Expressed in 224 organ(s), highest expression level in oviduct epithelium.
CleanEx; HS_PFKFB3; -.
ExpressionAtlas; Q16875; baseline and differential.
Genevisible; Q16875; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0003873; F:6-phosphofructo-2-kinase activity; EXP:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IEA:Ensembl.
GO; GO:0006000; P:fructose metabolic process; IEA:InterPro.
GO; GO:0045821; P:positive regulation of glycolytic process; TAS:Reactome.
CDD; cd07067; HP_PGM_like; 1.
Gene3D; 3.40.50.1240; -; 1.
InterPro; IPR003094; 6Pfruct_kin.
InterPro; IPR013079; 6Phosfructo_kin.
InterPro; IPR013078; His_Pase_superF_clade-1.
InterPro; IPR029033; His_PPase_superfam.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR001345; PG/BPGM_mutase_AS.
PANTHER; PTHR10606; PTHR10606; 1.
Pfam; PF01591; 6PF2K; 1.
Pfam; PF00300; His_Phos_1; 1.
PRINTS; PR00991; 6PFRUCTKNASE.
SMART; SM00855; PGAM; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF53254; SSF53254; 1.
PROSITE; PS00175; PG_MUTASE; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Hydrolase; Kinase; Multifunctional enzyme; Nucleotide-binding;
Phosphoprotein; Reference proteome; Transferase.
CHAIN 1 520 6-phosphofructo-2-kinase/fructose-2,6-
bisphosphatase 3.
/FTId=PRO_0000179968.
NP_BIND 42 50 ATP. {ECO:0000269|PubMed:16316985,
ECO:0000269|PubMed:17499765,
ECO:0000269|PubMed:22275052}.
NP_BIND 164 169 ATP. {ECO:0000269|PubMed:16316985,
ECO:0000269|PubMed:17499765,
ECO:0000269|PubMed:22275052}.
NP_BIND 345 348 ATP. {ECO:0000250|UniProtKB:P07953}.
NP_BIND 389 393 ATP. {ECO:0000250|UniProtKB:P07953}.
REGION 1 245 6-phosphofructo-2-kinase.
REGION 246 520 Fructose-2,6-bisphosphatase.
ACT_SITE 125 125 {ECO:0000255}.
ACT_SITE 155 155 {ECO:0000255}.
ACT_SITE 254 254 Tele-phosphohistidine intermediate.
{ECO:0000269|PubMed:22275052}.
ACT_SITE 323 323 Proton donor/acceptor.
{ECO:0000269|PubMed:22275052}.
BINDING 75 75 Fructose 6-phosphate.
{ECO:0000269|PubMed:16316985}.
BINDING 99 99 Fructose 6-phosphate.
{ECO:0000269|PubMed:16316985}.
BINDING 127 127 Fructose 6-phosphate.
{ECO:0000269|PubMed:16316985}.
BINDING 133 133 Fructose 6-phosphate.
{ECO:0000269|PubMed:16316985}.
BINDING 169 169 Fructose 6-phosphate.
{ECO:0000269|PubMed:16316985}.
BINDING 190 190 Fructose 6-phosphate.
{ECO:0000269|PubMed:16316985}.
BINDING 194 194 Fructose 6-phosphate.
{ECO:0000269|PubMed:16316985}.
BINDING 253 253 Fructose 2,6-bisphosphate.
{ECO:0000269|PubMed:25849762}.
BINDING 260 260 Fructose 2,6-bisphosphate.
{ECO:0000269|PubMed:25849762}.
BINDING 266 266 Fructose 2,6-bisphosphate; via amide
nitrogen. {ECO:0000269|PubMed:25849762}.
BINDING 334 334 Fructose 2,6-bisphosphate.
{ECO:0000269|PubMed:25849762}.
BINDING 348 348 Fructose 2,6-bisphosphate.
{ECO:0000269|PubMed:25849762}.
BINDING 352 352 Fructose 2,6-bisphosphate.
{ECO:0000269|PubMed:25849762}.
BINDING 363 363 Fructose 2,6-bisphosphate.
{ECO:0000269|PubMed:25849762}.
BINDING 389 389 Fructose 2,6-bisphosphate.
{ECO:0000269|PubMed:25849762}.
BINDING 393 393 Fructose 2,6-bisphosphate.
{ECO:0000250|UniProtKB:P07953}.
BINDING 425 425 ATP. {ECO:0000269|PubMed:16316985,
ECO:0000269|PubMed:17499765,
ECO:0000269|PubMed:22275052}.
SITE 253 253 Transition state stabilizer.
{ECO:0000269|PubMed:22275052}.
SITE 260 260 Transition state stabilizer.
{ECO:0000269|PubMed:22275052}.
SITE 388 388 Transition state stabilizer.
{ECO:0000269|PubMed:22275052}.
MOD_RES 461 461 Phosphoserine; by AMPK.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:12065600}.
MOD_RES 463 463 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 467 467 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 471 471 Phosphothreonine; by PKC. {ECO:0000250}.
VAR_SEQ 1 26 MPLELTQSRVQKIWVPVDHRPSLPRS -> MPFRKA (in
isoform 3). {ECO:0000305}.
/FTId=VSP_047165.
VAR_SEQ 1 26 MPLELTQSRVQKIWVPVDHRPSLPRS -> MGEGGQKEGDS
QQAGALPLLCQLDTFSPKATVFGVSINPA (in isoform
4). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_054549.
VAR_SEQ 506 520 NMKGSRSSADSSRKH -> PLLGQACLT (in isoform
2). {ECO:0000303|PubMed:10077634}.
/FTId=VSP_004680.
CONFLICT 136 136 M -> V (in Ref. 4; AAB99795).
{ECO:0000305}.
CONFLICT 141 141 A -> G (in Ref. 5; AAC62000).
{ECO:0000305}.
STRAND 5 7 {ECO:0000244|PDB:5AK0}.
TURN 9 11 {ECO:0000244|PDB:5AK0}.
STRAND 14 16 {ECO:0000244|PDB:5AK0}.
STRAND 36 43 {ECO:0000244|PDB:5AK0}.
STRAND 44 47 {ECO:0000244|PDB:2DWP}.
HELIX 48 61 {ECO:0000244|PDB:5AK0}.
STRAND 66 70 {ECO:0000244|PDB:5AK0}.
HELIX 71 78 {ECO:0000244|PDB:5AK0}.
STRAND 79 81 {ECO:0000244|PDB:4D4M}.
HELIX 85 88 {ECO:0000244|PDB:5AK0}.
HELIX 93 116 {ECO:0000244|PDB:5AK0}.
STRAND 120 126 {ECO:0000244|PDB:5AK0}.
HELIX 131 144 {ECO:0000244|PDB:5AK0}.
STRAND 147 154 {ECO:0000244|PDB:5AK0}.
HELIX 157 163 {ECO:0000244|PDB:5AK0}.
HELIX 165 169 {ECO:0000244|PDB:5AK0}.
HELIX 173 175 {ECO:0000244|PDB:5AK0}.
HELIX 180 195 {ECO:0000244|PDB:5AK0}.
TURN 203 209 {ECO:0000244|PDB:5AK0}.
STRAND 210 216 {ECO:0000244|PDB:5AK0}.
TURN 217 220 {ECO:0000244|PDB:5AK0}.
STRAND 221 225 {ECO:0000244|PDB:5AK0}.
HELIX 230 241 {ECO:0000244|PDB:5AK0}.
STRAND 249 253 {ECO:0000244|PDB:5AK0}.
HELIX 258 261 {ECO:0000244|PDB:5AK0}.
HELIX 273 289 {ECO:0000244|PDB:5AK0}.
STRAND 295 298 {ECO:0000244|PDB:5AK0}.
HELIX 302 309 {ECO:0000244|PDB:5AK0}.
TURN 310 312 {ECO:0000244|PDB:5AK0}.
STRAND 315 317 {ECO:0000244|PDB:2AXN}.
HELIX 319 321 {ECO:0000244|PDB:5AK0}.
HELIX 327 329 {ECO:0000244|PDB:5AK0}.
HELIX 334 340 {ECO:0000244|PDB:5AK0}.
HELIX 342 350 {ECO:0000244|PDB:5AK0}.
TURN 352 354 {ECO:0000244|PDB:5AK0}.
HELIX 363 379 {ECO:0000244|PDB:5AK0}.
STRAND 381 387 {ECO:0000244|PDB:5AK0}.
HELIX 389 399 {ECO:0000244|PDB:5AK0}.
TURN 404 406 {ECO:0000244|PDB:5AK0}.
HELIX 407 409 {ECO:0000244|PDB:5AK0}.
STRAND 416 423 {ECO:0000244|PDB:5AK0}.
STRAND 426 433 {ECO:0000244|PDB:5AK0}.
HELIX 442 446 {ECO:0000244|PDB:3QPU}.
HELIX 455 457 {ECO:0000244|PDB:2AXN}.
SEQUENCE 520 AA; 59609 MW; A7675A4ADC376879 CRC64;
MPLELTQSRV QKIWVPVDHR PSLPRSCGPK LTNSPTVIVM VGLPARGKTY ISKKLTRYLN
WIGVPTKVFN VGEYRREAVK QYSSYNFFRP DNEEAMKVRK QCALAALRDV KSYLAKEGGQ
IAVFDATNTT RERRHMILHF AKENDFKAFF IESVCDDPTV VASNIMEVKI SSPDYKDCNS
AEAMDDFMKR ISCYEASYQP LDPDKCDRDL SLIKVIDVGR RFLVNRVQDH IQSRIVYYLM
NIHVQPRTIY LCRHGENEHN LQGRIGGDSG LSSRGKKFAS ALSKFVEEQN LKDLRVWTSQ
LKSTIQTAEA LRLPYEQWKA LNEIDAGVCE ELTYEEIRDT YPEEYALREQ DKYYYRYPTG
ESYQDLVQRL EPVIMELERQ ENVLVICHQA VLRCLLAYFL DKSAEEMPYL KCPLHTVLKL
TPVAYGCRVE SIYLNVESVC THRERSEDAK KGPNPLMRRN SVTPLASPEP TKKPRINSFE
EHVASTSAAL PSCLPPEVPT QLPGQNMKGS RSSADSSRKH


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