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Q16875

- F263_HUMAN

UniProt

Q16875 - F263_HUMAN

Protein

6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3

Gene

PFKFB3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Synthesis and degradation of fructose 2,6-bisphosphate.

    Catalytic activityi

    Beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
    ATP + D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei75 – 751Fructose 6-phosphate1 Publication
    Binding sitei99 – 991Fructose 6-phosphate1 Publication
    Active sitei125 – 1251Sequence Analysis
    Binding sitei127 – 1271Fructose 6-phosphate1 Publication
    Binding sitei133 – 1331Fructose 6-phosphate1 Publication
    Active sitei155 – 1551Sequence Analysis
    Binding sitei169 – 1691Fructose 6-phosphate1 Publication
    Binding sitei190 – 1901Fructose 6-phosphate1 Publication
    Binding sitei194 – 1941Fructose 6-phosphate1 Publication
    Binding sitei253 – 2531Fructose 2,6-bisphosphate
    Active sitei254 – 2541Tele-phosphohistidine intermediateBy similarity
    Binding sitei260 – 2601Fructose 2,6-bisphosphateBy similarity
    Binding sitei266 – 2661Fructose 2,6-bisphosphate; via amide nitrogen
    Active sitei323 – 3231Proton donor/acceptorCurated
    Binding sitei334 – 3341Fructose 2,6-bisphosphate
    Binding sitei348 – 3481Fructose 2,6-bisphosphate
    Binding sitei352 – 3521Fructose 2,6-bisphosphate
    Binding sitei363 – 3631Fructose 2,6-bisphosphate
    Active sitei388 – 3881Proton donor/acceptorBy similarity
    Binding sitei389 – 3891Fructose 2,6-bisphosphate
    Binding sitei393 – 3931Fructose 2,6-bisphosphate
    Binding sitei425 – 4251ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi42 – 509ATP
    Nucleotide bindingi164 – 1696ATP
    Nucleotide bindingi345 – 3484ATPBy similarity
    Nucleotide bindingi389 – 3935ATPBy similarity

    GO - Molecular functioni

    1. 6-phosphofructo-2-kinase activity Source: UniProtKB
    2. ATP binding Source: UniProtKB-KW
    3. fructose-2,6-bisphosphate 2-phosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. carbohydrate phosphorylation Source: GOC
    3. fructose 2,6-bisphosphate metabolic process Source: InterPro
    4. fructose metabolic process Source: InterPro
    5. glucose metabolic process Source: Reactome
    6. glycolytic process Source: Reactome
    7. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.1.105. 2681.
    ReactomeiREACT_1383. Glycolysis.
    SABIO-RKQ16875.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3
    Short name:
    6PF-2-K/Fru-2,6-P2ase 3
    Short name:
    PFK/FBPase 3
    Alternative name(s):
    6PF-2-K/Fru-2,6-P2ase brain/placenta-type isozyme
    Renal carcinoma antigen NY-REN-56
    iPFK-2
    Including the following 2 domains:
    Fructose-2,6-bisphosphatase (EC:3.1.3.46)
    Gene namesi
    Name:PFKFB3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:8874. PFKFB3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleus Source: HPA

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33213.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 5205206-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3PRO_0000179968Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei461 – 4611Phosphoserine; by AMPK4 Publications
    Modified residuei463 – 4631Phosphothreonine1 Publication
    Modified residuei467 – 4671Phosphoserine3 Publications
    Modified residuei471 – 4711Phosphothreonine; by PKCBy similarity

    Post-translational modificationi

    Phosphorylation by AMPK stimulates activity.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ16875.
    PaxDbiQ16875.
    PRIDEiQ16875.

    PTM databases

    PhosphoSiteiQ16875.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ16875.
    BgeeiQ16875.
    CleanExiHS_PFKFB3.
    GenevestigatoriQ16875.

    Organism-specific databases

    HPAiCAB020795.
    HPA008266.
    HPA043889.

    Interactioni

    Protein-protein interaction databases

    BioGridi111230. 9 interactions.
    DIPiDIP-33964N.
    IntActiQ16875. 5 interactions.
    STRINGi9606.ENSP00000369100.

    Structurei

    Secondary structure

    1
    520
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 73
    Turni9 – 113
    Beta strandi14 – 163
    Beta strandi36 – 416
    Beta strandi44 – 474
    Helixi48 – 6114
    Beta strandi66 – 705
    Helixi71 – 799
    Helixi85 – 884
    Helixi93 – 11624
    Beta strandi121 – 1266
    Helixi131 – 14313
    Beta strandi147 – 1548
    Helixi158 – 16811
    Turni169 – 1713
    Helixi173 – 1753
    Helixi180 – 19516
    Turni203 – 2097
    Beta strandi210 – 2167
    Turni217 – 2204
    Beta strandi221 – 2255
    Helixi230 – 23910
    Beta strandi249 – 2535
    Helixi258 – 2625
    Helixi273 – 28917
    Beta strandi295 – 2984
    Helixi302 – 3098
    Turni310 – 3123
    Beta strandi315 – 3173
    Helixi319 – 3213
    Helixi327 – 3293
    Helixi334 – 3407
    Helixi342 – 3509
    Turni352 – 3543
    Helixi363 – 37917
    Beta strandi381 – 3877
    Helixi389 – 39911
    Turni404 – 4063
    Helixi407 – 4093
    Beta strandi416 – 4238
    Beta strandi426 – 4338
    Helixi442 – 4465
    Helixi455 – 4573

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AXNX-ray2.10A1-520[»]
    2DWOX-ray2.25A1-520[»]
    2DWPX-ray2.70A1-520[»]
    2I1VX-ray2.50B1-520[»]
    3QPUX-ray2.30A1-520[»]
    3QPVX-ray2.50A1-520[»]
    3QPWX-ray2.25A1-520[»]
    4MA4X-ray2.23A1-520[»]
    ProteinModelPortaliQ16875.
    SMRiQ16875. Positions 4-440.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16875.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 2452456-phosphofructo-2-kinaseAdd
    BLAST
    Regioni246 – 520275Fructose-2,6-bisphosphataseAdd
    BLAST

    Sequence similaritiesi

    In the C-terminal section; belongs to the phosphoglycerate mutase family.Curated

    Phylogenomic databases

    eggNOGiCOG0406.
    HOGENOMiHOG000181112.
    HOVERGENiHBG005628.
    KOiK01103.
    OrthoDBiEOG7M3J03.
    PhylomeDBiQ16875.
    TreeFamiTF313541.

    Family and domain databases

    Gene3Di3.40.50.1240. 1 hit.
    3.40.50.300. 1 hit.
    InterProiIPR003094. 6Pfruct_kin.
    IPR013079. 6Phosfructo_kin.
    IPR016260. Bifunct_6PFK/fruc_bisP_Ptase.
    IPR013078. His_Pase_superF_clade-1.
    IPR029033. His_PPase_superfam.
    IPR027417. P-loop_NTPase.
    IPR001345. PG/BPGM_mutase_AS.
    [Graphical view]
    PANTHERiPTHR10606. PTHR10606. 1 hit.
    PfamiPF01591. 6PF2K. 1 hit.
    PF00300. His_Phos_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000709. 6PFK_2-Ptase. 1 hit.
    PRINTSiPR00991. 6PFRUCTKNASE.
    SMARTiSM00855. PGAM. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    SSF53254. SSF53254. 1 hit.
    PROSITEiPS00175. PG_MUTASE. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q16875-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPLELTQSRV QKIWVPVDHR PSLPRSCGPK LTNSPTVIVM VGLPARGKTY    50
    ISKKLTRYLN WIGVPTKVFN VGEYRREAVK QYSSYNFFRP DNEEAMKVRK 100
    QCALAALRDV KSYLAKEGGQ IAVFDATNTT RERRHMILHF AKENDFKAFF 150
    IESVCDDPTV VASNIMEVKI SSPDYKDCNS AEAMDDFMKR ISCYEASYQP 200
    LDPDKCDRDL SLIKVIDVGR RFLVNRVQDH IQSRIVYYLM NIHVQPRTIY 250
    LCRHGENEHN LQGRIGGDSG LSSRGKKFAS ALSKFVEEQN LKDLRVWTSQ 300
    LKSTIQTAEA LRLPYEQWKA LNEIDAGVCE ELTYEEIRDT YPEEYALREQ 350
    DKYYYRYPTG ESYQDLVQRL EPVIMELERQ ENVLVICHQA VLRCLLAYFL 400
    DKSAEEMPYL KCPLHTVLKL TPVAYGCRVE SIYLNVESVC THRERSEDAK 450
    KGPNPLMRRN SVTPLASPEP TKKPRINSFE EHVASTSAAL PSCLPPEVPT 500
    QLPGQNMKGS RSSADSSRKH 520
    Length:520
    Mass (Da):59,609
    Last modified:November 1, 1996 - v1
    Checksum:iA7675A4ADC376879
    GO
    Isoform 2 (identifier: Q16875-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         506-520: NMKGSRSSADSSRKH → PLLGQACLT

    Show »
    Length:514
    Mass (Da):58,876
    Checksum:i18FD1D267306853D
    GO
    Isoform 3 (identifier: Q16875-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-26: MPLELTQSRVQKIWVPVDHRPSLPRS → MPFRKA

    Note: Gene prediction based on EST data.

    Show »
    Length:500
    Mass (Da):57,287
    Checksum:i32D2924D3D207C17
    GO
    Isoform 4 (identifier: Q16875-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-26: MPLELTQSRVQKIWVPVDHRPSLPRS → MGEGGQKEGDSQQAGALPLLCQLDTFSPKATVFGVSINPA

    Note: No experimental confirmation available.

    Show »
    Length:534
    Mass (Da):60,602
    Checksum:iFB3222408A8BC7EE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti136 – 1361M → V in AAB99795. 1 PublicationCurated
    Sequence conflicti141 – 1411A → G in AAC62000. (PubMed:10077634)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2626MPLEL…SLPRS → MPFRKA in isoform 3. CuratedVSP_047165Add
    BLAST
    Alternative sequencei1 – 2626MPLEL…SLPRS → MGEGGQKEGDSQQAGALPLL CQLDTFSPKATVFGVSINPA in isoform 4. 1 PublicationVSP_054549Add
    BLAST
    Alternative sequencei506 – 52015NMKGS…SSRKH → PLLGQACLT in isoform 2. 1 PublicationVSP_004680Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D49817 mRNA. Translation: BAA08624.1.
    L77662 mRNA. Translation: AAL40083.1.
    AF109735 mRNA. Translation: AAD08818.1.
    AF041831
    , AF041823, AF041824, AF041825, AF041826, AF041827, AF041828, AF041829, AF041830 Genomic DNA. Translation: AAB99795.1.
    AF056320 mRNA. Translation: AAC62000.1.
    AK291263 mRNA. Translation: BAF83952.1.
    AK304450 mRNA. Translation: BAH14191.1.
    AL359960, AL157395 Genomic DNA. Translation: CAH72163.1.
    AL157395, AL359960 Genomic DNA. Translation: CAH73606.1.
    CH471072 Genomic DNA. Translation: EAW86398.1.
    CH471072 Genomic DNA. Translation: EAW86399.1.
    BC040482 mRNA. Translation: AAH40482.1.
    CCDSiCCDS44353.1. [Q16875-3]
    CCDS60479.1. [Q16875-4]
    CCDS7078.1. [Q16875-1]
    PIRiJC4626.
    RefSeqiNP_001138915.1. NM_001145443.1. [Q16875-3]
    NP_001269559.1. NM_001282630.1. [Q16875-4]
    NP_004557.1. NM_004566.3. [Q16875-1]
    XP_005252520.1. XM_005252463.1. [Q16875-2]
    UniGeneiHs.195471.

    Genome annotation databases

    EnsembliENST00000360521; ENSP00000353712; ENSG00000170525. [Q16875-2]
    ENST00000379775; ENSP00000369100; ENSG00000170525. [Q16875-1]
    ENST00000379789; ENSP00000369115; ENSG00000170525. [Q16875-3]
    GeneIDi5209.
    KEGGihsa:5209.
    UCSCiuc001ije.3. human. [Q16875-1]
    uc001ijf.3. human. [Q16875-2]

    Polymorphism databases

    DMDMi3023733.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D49817 mRNA. Translation: BAA08624.1 .
    L77662 mRNA. Translation: AAL40083.1 .
    AF109735 mRNA. Translation: AAD08818.1 .
    AF041831
    , AF041823 , AF041824 , AF041825 , AF041826 , AF041827 , AF041828 , AF041829 , AF041830 Genomic DNA. Translation: AAB99795.1 .
    AF056320 mRNA. Translation: AAC62000.1 .
    AK291263 mRNA. Translation: BAF83952.1 .
    AK304450 mRNA. Translation: BAH14191.1 .
    AL359960 , AL157395 Genomic DNA. Translation: CAH72163.1 .
    AL157395 , AL359960 Genomic DNA. Translation: CAH73606.1 .
    CH471072 Genomic DNA. Translation: EAW86398.1 .
    CH471072 Genomic DNA. Translation: EAW86399.1 .
    BC040482 mRNA. Translation: AAH40482.1 .
    CCDSi CCDS44353.1. [Q16875-3 ]
    CCDS60479.1. [Q16875-4 ]
    CCDS7078.1. [Q16875-1 ]
    PIRi JC4626.
    RefSeqi NP_001138915.1. NM_001145443.1. [Q16875-3 ]
    NP_001269559.1. NM_001282630.1. [Q16875-4 ]
    NP_004557.1. NM_004566.3. [Q16875-1 ]
    XP_005252520.1. XM_005252463.1. [Q16875-2 ]
    UniGenei Hs.195471.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AXN X-ray 2.10 A 1-520 [» ]
    2DWO X-ray 2.25 A 1-520 [» ]
    2DWP X-ray 2.70 A 1-520 [» ]
    2I1V X-ray 2.50 B 1-520 [» ]
    3QPU X-ray 2.30 A 1-520 [» ]
    3QPV X-ray 2.50 A 1-520 [» ]
    3QPW X-ray 2.25 A 1-520 [» ]
    4MA4 X-ray 2.23 A 1-520 [» ]
    ProteinModelPortali Q16875.
    SMRi Q16875. Positions 4-440.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111230. 9 interactions.
    DIPi DIP-33964N.
    IntActi Q16875. 5 interactions.
    STRINGi 9606.ENSP00000369100.

    Chemistry

    ChEMBLi CHEMBL2331053.

    PTM databases

    PhosphoSitei Q16875.

    Polymorphism databases

    DMDMi 3023733.

    Proteomic databases

    MaxQBi Q16875.
    PaxDbi Q16875.
    PRIDEi Q16875.

    Protocols and materials databases

    DNASUi 5209.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360521 ; ENSP00000353712 ; ENSG00000170525 . [Q16875-2 ]
    ENST00000379775 ; ENSP00000369100 ; ENSG00000170525 . [Q16875-1 ]
    ENST00000379789 ; ENSP00000369115 ; ENSG00000170525 . [Q16875-3 ]
    GeneIDi 5209.
    KEGGi hsa:5209.
    UCSCi uc001ije.3. human. [Q16875-1 ]
    uc001ijf.3. human. [Q16875-2 ]

    Organism-specific databases

    CTDi 5209.
    GeneCardsi GC10P006186.
    HGNCi HGNC:8874. PFKFB3.
    HPAi CAB020795.
    HPA008266.
    HPA043889.
    MIMi 605319. gene.
    neXtProti NX_Q16875.
    PharmGKBi PA33213.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0406.
    HOGENOMi HOG000181112.
    HOVERGENi HBG005628.
    KOi K01103.
    OrthoDBi EOG7M3J03.
    PhylomeDBi Q16875.
    TreeFami TF313541.

    Enzyme and pathway databases

    BRENDAi 2.7.1.105. 2681.
    Reactomei REACT_1383. Glycolysis.
    SABIO-RK Q16875.

    Miscellaneous databases

    ChiTaRSi Pfkfb3. human.
    EvolutionaryTracei Q16875.
    GeneWikii PFKFB3.
    GenomeRNAii 5209.
    NextBioi 20146.
    PROi Q16875.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16875.
    Bgeei Q16875.
    CleanExi HS_PFKFB3.
    Genevestigatori Q16875.

    Family and domain databases

    Gene3Di 3.40.50.1240. 1 hit.
    3.40.50.300. 1 hit.
    InterProi IPR003094. 6Pfruct_kin.
    IPR013079. 6Phosfructo_kin.
    IPR016260. Bifunct_6PFK/fruc_bisP_Ptase.
    IPR013078. His_Pase_superF_clade-1.
    IPR029033. His_PPase_superfam.
    IPR027417. P-loop_NTPase.
    IPR001345. PG/BPGM_mutase_AS.
    [Graphical view ]
    PANTHERi PTHR10606. PTHR10606. 1 hit.
    Pfami PF01591. 6PF2K. 1 hit.
    PF00300. His_Phos_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000709. 6PFK_2-Ptase. 1 hit.
    PRINTSi PR00991. 6PFRUCTKNASE.
    SMARTi SM00855. PGAM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    SSF53254. SSF53254. 1 hit.
    PROSITEi PS00175. PG_MUTASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of cDNA encoding for a novel isozyme of fructose 6-phosphate, 2-kinase/fructose 2,6-bisphosphatase from human placenta."
      Sakai A., Kato M., Fukasawa M., Ishiguro M., Furuya E., Sakakibara R.
      J. Biochem. 119:506-511(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. "The third human isoform of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB3) map position 10p14-p15."
      Nicholl J., Hamilton J.A., Sutherland G.R., Sutherland R.L., Watts C.K.
      Chromosome Res. 5:150-150(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Molecular cloning, expression, and chromosomal localization of a ubiquitously expressed human 6-phosphofructo-2-kinase/ fructose-2, 6-bisphosphatase gene (PFKFB3)."
      Manzano A., Rosa J.L., Ventura F., Perez J.X., Nadal M., Estivill X., Ambrosio S., Gil J., Bartrons R.
      Cytogenet. Cell Genet. 83:214-217(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    4. "Human brain 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."
      El-Maghrabi M.R.
      Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
      Tissue: Brain.
    5. "An inducible gene product for 6-phosphofructo-2-kinase with an AU-rich instability element: role in tumor cell glycolysis and the Warburg effect."
      Chesney J., Mitchell R.A., Benigni F., Bacher M., Spiegel L., Al-Abed Y., Han J.H., Metz C., Bucala R.
      Proc. Natl. Acad. Sci. U.S.A. 96:3047-3052(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Skeletal muscle.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
      Tissue: Trachea.
    7. "The DNA sequence and comparative analysis of human chromosome 10."
      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.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Testis.
    10. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
      Tissue: Renal cell carcinoma.
    11. "The stimulation of glycolysis by hypoxia in activated monocytes is mediated by AMP-activated protein kinase and inducible 6-phosphofructo-2-kinase."
      Marsin A.S., Bouzin C., Bertrand L., Hue L.
      J. Biol. Chem. 277:30778-30783(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-461.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461; THR-463 AND SER-467, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461 AND SER-467, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461 AND SER-467, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Crystal structure of the hypoxia-inducible form of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB3): a possible new target for cancer therapy."
      Kim S.G., Manes N.P., El-Maghrabi M.R., Lee Y.H.
      J. Biol. Chem. 281:2939-2944(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH ADP AND FRUCTOSE 6-PHOSPHATE.
    16. "A direct substrate-substrate interaction found in the kinase domain of the bifunctional enzyme, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."
      Kim S.G., Cavalier M., El-Maghrabi M.R., Lee Y.H.
      J. Mol. Biol. 370:14-26(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEXES WITH ADP; ATP; FRUCTOSE 6-PHOSPHATE; FRUCTOSE-2,6-BISPHOSPHATE AND PHOSPHOENOLPYRUVATE.
    17. "Molecular basis of the fructose-2,6-bisphosphatase reaction of PFKFB3: transition state and the C-terminal function."
      Cavalier M.C., Kim S.G., Neau D., Lee Y.H.
      Proteins 80:1143-1153(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).

    Entry informationi

    Entry nameiF263_HUMAN
    AccessioniPrimary (citable) accession number: Q16875
    Secondary accession number(s): B7Z955
    , O43622, O75902, Q5VX15, Q5VX18, Q5VX19
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 151 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3