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P16118

- F261_HUMAN

UniProt

P16118 - F261_HUMAN

Protein

6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1

Gene

PFKFB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 3 (01 Nov 1997)
      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.

    Enzyme regulationi

    Phosphorylation at Ser-33 inhibits the kinase and activates the bisphosphatase.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei82 – 821Fructose 6-phosphateBy similarity
    Binding sitei105 – 1051Fructose 6-phosphateBy similarity
    Active sitei131 – 1311Sequence Analysis
    Binding sitei133 – 1331Fructose 6-phosphateBy similarity
    Binding sitei139 – 1391Fructose 6-phosphateBy similarity
    Active sitei161 – 1611Sequence Analysis
    Binding sitei175 – 1751Fructose 6-phosphateBy similarity
    Binding sitei196 – 1961Fructose 6-phosphateBy similarity
    Binding sitei200 – 2001Fructose 6-phosphateBy similarity
    Binding sitei258 – 2581Fructose 2,6-bisphosphate
    Active sitei259 – 2591Tele-phosphohistidine intermediateBy similarity
    Binding sitei265 – 2651Fructose 2,6-bisphosphate
    Binding sitei271 – 2711Fructose 2,6-bisphosphate; via amide nitrogenBy similarity
    Binding sitei308 – 3081Fructose 2,6-bisphosphate
    Active sitei328 – 3281Proton donor/acceptorBy similarity
    Binding sitei339 – 3391Fructose 2,6-bisphosphate
    Binding sitei353 – 3531Fructose 2,6-bisphosphate
    Binding sitei357 – 3571Fructose 2,6-bisphosphate
    Binding sitei368 – 3681Fructose 2,6-bisphosphate
    Active sitei393 – 3931Proton donor/acceptorBy similarity
    Binding sitei394 – 3941Fructose 2,6-bisphosphateBy similarity
    Binding sitei398 – 3981Fructose 2,6-bisphosphate
    Binding sitei430 – 4301ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi49 – 579ATP
    Nucleotide bindingi170 – 1756ATP
    Nucleotide bindingi350 – 3534ATPBy similarity
    Nucleotide bindingi394 – 3985ATPBy 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
    4. fructose-6-phosphate binding Source: Ensembl
    5. protein binding Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. dephosphorylation Source: GOC
    3. energy reserve metabolic process Source: Reactome
    4. fructose 2,6-bisphosphate metabolic process Source: UniProtKB
    5. fructose metabolic process Source: InterPro
    6. gluconeogenesis Source: UniProtKB
    7. glucose metabolic process Source: Reactome
    8. glycolytic process Source: UniProtKB
    9. intracellular signal transduction Source: Reactome
    10. organ regeneration Source: Ensembl
    11. positive regulation of glucokinase activity Source: Ensembl
    12. response to cAMP Source: Ensembl
    13. response to glucagon Source: Ensembl
    14. response to glucocorticoid Source: Ensembl
    15. response to insulin Source: Ensembl
    16. response to starvation Source: Ensembl
    17. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi3.1.3.46. 2681.
    ReactomeiREACT_1383. Glycolysis.
    REACT_1520. Gluconeogenesis.
    REACT_1525. PKA-mediated phosphorylation of key metabolic factors.
    REACT_705. PP2A-mediated dephosphorylation of key metabolic factors.
    SABIO-RKP16118.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1
    Short name:
    6PF-2-K/Fru-2,6-P2ase 1
    Short name:
    PFK/FBPase 1
    Alternative name(s):
    6PF-2-K/Fru-2,6-P2ase liver isozyme
    Including the following 2 domains:
    Fructose-2,6-bisphosphatase (EC:3.1.3.46)
    Gene namesi
    Name:PFKFB1
    Synonyms:F6PK, PFRX
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:8872. PFKFB1.

    Subcellular locationi

    GO - Cellular componenti

    1. 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase complex Source: UniProtKB
    2. cytosol Source: Reactome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33211.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 4714706-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1PRO_0000179960Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei33 – 331Phosphoserine; by PKABy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP16118.
    PRIDEiP16118.

    PTM databases

    PhosphoSiteiP16118.

    Expressioni

    Tissue specificityi

    Liver.

    Gene expression databases

    ArrayExpressiP16118.
    BgeeiP16118.
    CleanExiHS_PFKFB1.
    GenevestigatoriP16118.

    Organism-specific databases

    HPAiHPA013959.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GCKP355572EBI-709807,EBI-709928

    Protein-protein interaction databases

    BioGridi111228. 6 interactions.
    IntActiP16118. 3 interactions.
    MINTiMINT-6772805.
    STRINGi9606.ENSP00000364145.

    Structurei

    Secondary structure

    1
    471
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi43 – 486
    Helixi55 – 6814
    Beta strandi73 – 775
    Helixi78 – 836
    Helixi91 – 944
    Helixi99 – 12123
    Beta strandi126 – 1327
    Helixi137 – 15014
    Beta strandi153 – 1608
    Helixi164 – 17512
    Helixi187 – 20115
    Turni209 – 2146
    Beta strandi217 – 2215
    Turni222 – 2254
    Beta strandi226 – 2305
    Helixi235 – 24410
    Beta strandi254 – 2585
    Helixi263 – 2664
    Helixi278 – 29316
    Beta strandi300 – 3034
    Helixi307 – 3148
    Helixi324 – 3263
    Helixi332 – 3343
    Helixi339 – 3457
    Helixi347 – 3559
    Turni357 – 3593
    Helixi368 – 38417
    Beta strandi386 – 3927
    Helixi394 – 40512
    Turni409 – 4113
    Helixi412 – 4143
    Beta strandi421 – 4277
    Beta strandi429 – 43810
    Helixi460 – 4645

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1K6MX-ray2.40A/B40-471[»]
    ProteinModelPortaliP16118.
    SMRiP16118. Positions 7-471.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16118.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 2502496-phosphofructo-2-kinaseAdd
    BLAST
    Regioni251 – 471221Fructose-2,6-bisphosphataseAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0406.
    HOGENOMiHOG000181112.
    HOVERGENiHBG005628.
    InParanoidiP16118.
    KOiK01103.
    OMAiNIRGRIG.
    OrthoDBiEOG7M3J03.
    PhylomeDBiP16118.
    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 (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P16118-1) [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

    MSPEMGELTQ TRLQKIWIPH SSGSSRLQRR RGSSIPQFTN SPTMVIMVGL    50
    PARGKTYIST KLTRYLNWIG TPTKVFNLGQ YRREAVSYKN YEFFLPDNME 100
    ALQIRKQCAL AALKDVHNYL SHEEGHVAVF DATNTTRERR SLILQFAKEH 150
    GYKVFFIESI CNDPGIIAEN IRQVKLGSPD YIDCDREKVL EDFLKRIECY 200
    EVNYQPLDEE LDSHLSYIKI FDVGTRYMVN RVQDHIQSRT VYYLMNIHVT 250
    PRSIYLCRHG ESELNIRGRI GGDSGLSVRG KQYAYALANF IQSQGISSLK 300
    VWTSHMKRTI QTAEALGVPY EQWKALNEID AGVCEEMTYE EIQEHYPEEF 350
    ALRDQDKYRY RYPKGESYED LVQRLEPVIM ELERQENVLV ICHQAVMRCL 400
    LAYFLDKSSD ELPYLKCPLH TVLKLTPVAY GCKVESIYLN VEAVNTHREK 450
    PENVDITREP EEALDTVPAH Y 471
    Length:471
    Mass (Da):54,681
    Last modified:November 1, 1997 - v3
    Checksum:iC4FF081A295FB7D3
    GO
    Isoform 2 (identifier: P16118-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-73: MSPEMGELTQ...RYLNWIGTPT → MEEKTSRI

    Show »
    Length:406
    Mass (Da):47,426
    Checksum:i5D982E7DFBAC5CC1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti305 – 3051H → R in CAA36861. (PubMed:2163524)Curated
    Sequence conflicti359 – 3591R → H in AAA35818. (PubMed:2837207)Curated
    Sequence conflicti397 – 3982MR → HA in AAA35818. (PubMed:2837207)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7373MSPEM…IGTPT → MEEKTSRI in isoform 2. 1 PublicationVSP_054795Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52638 mRNA. Translation: CAA36861.1.
    AK314089 mRNA. Translation: BAG36785.1.
    AK300724 mRNA. Translation: BAG62397.1.
    AL049732, AL020991 Genomic DNA. Translation: CAI42048.1.
    AL020991, AL049732 Genomic DNA. Translation: CAI43127.1.
    BC096079 mRNA. Translation: AAH96079.1.
    M19938 mRNA. Translation: AAA35818.1.
    CCDSiCCDS14364.1. [P16118-1]
    CCDS65273.1. [P16118-2]
    PIRiS12732.
    RefSeqiNP_001258733.1. NM_001271804.1.
    NP_001258734.1. NM_001271805.1. [P16118-2]
    NP_002616.2. NM_002625.3. [P16118-1]
    UniGeneiHs.444304.

    Genome annotation databases

    EnsembliENST00000375006; ENSP00000364145; ENSG00000158571. [P16118-1]
    ENST00000545676; ENSP00000444074; ENSG00000158571. [P16118-2]
    GeneIDi5207.
    KEGGihsa:5207.
    UCSCiuc004dty.2. human. [P16118-1]

    Polymorphism databases

    DMDMi2507178.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52638 mRNA. Translation: CAA36861.1 .
    AK314089 mRNA. Translation: BAG36785.1 .
    AK300724 mRNA. Translation: BAG62397.1 .
    AL049732 , AL020991 Genomic DNA. Translation: CAI42048.1 .
    AL020991 , AL049732 Genomic DNA. Translation: CAI43127.1 .
    BC096079 mRNA. Translation: AAH96079.1 .
    M19938 mRNA. Translation: AAA35818.1 .
    CCDSi CCDS14364.1. [P16118-1 ]
    CCDS65273.1. [P16118-2 ]
    PIRi S12732.
    RefSeqi NP_001258733.1. NM_001271804.1.
    NP_001258734.1. NM_001271805.1. [P16118-2 ]
    NP_002616.2. NM_002625.3. [P16118-1 ]
    UniGenei Hs.444304.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1K6M X-ray 2.40 A/B 40-471 [» ]
    ProteinModelPortali P16118.
    SMRi P16118. Positions 7-471.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111228. 6 interactions.
    IntActi P16118. 3 interactions.
    MINTi MINT-6772805.
    STRINGi 9606.ENSP00000364145.

    PTM databases

    PhosphoSitei P16118.

    Polymorphism databases

    DMDMi 2507178.

    Proteomic databases

    PaxDbi P16118.
    PRIDEi P16118.

    Protocols and materials databases

    DNASUi 5207.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375006 ; ENSP00000364145 ; ENSG00000158571 . [P16118-1 ]
    ENST00000545676 ; ENSP00000444074 ; ENSG00000158571 . [P16118-2 ]
    GeneIDi 5207.
    KEGGi hsa:5207.
    UCSCi uc004dty.2. human. [P16118-1 ]

    Organism-specific databases

    CTDi 5207.
    GeneCardsi GC0XM054976.
    HGNCi HGNC:8872. PFKFB1.
    HPAi HPA013959.
    MIMi 311790. gene.
    neXtProti NX_P16118.
    PharmGKBi PA33211.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0406.
    HOGENOMi HOG000181112.
    HOVERGENi HBG005628.
    InParanoidi P16118.
    KOi K01103.
    OMAi NIRGRIG.
    OrthoDBi EOG7M3J03.
    PhylomeDBi P16118.
    TreeFami TF313541.

    Enzyme and pathway databases

    BRENDAi 3.1.3.46. 2681.
    Reactomei REACT_1383. Glycolysis.
    REACT_1520. Gluconeogenesis.
    REACT_1525. PKA-mediated phosphorylation of key metabolic factors.
    REACT_705. PP2A-mediated dephosphorylation of key metabolic factors.
    SABIO-RK P16118.

    Miscellaneous databases

    EvolutionaryTracei P16118.
    GenomeRNAii 5207.
    NextBioi 20136.
    PROi P16118.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16118.
    Bgeei P16118.
    CleanExi HS_PFKFB1.
    Genevestigatori P16118.

    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. "Sequence of human liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."
      Lange A.J., Pilkis S.J.
      Nucleic Acids Res. 18:3652-3652(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    2. "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 2).
      Tissue: Liver.
    3. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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).
    5. "Molecular cloning, sequence analysis, and expression of a human liver cDNA coding for fructose-6-P,2-kinase:fructose-2,6-bisphosphatase."
      Algaier J., Uyeda K.
      Biochem. Biophys. Res. Commun. 153:328-333(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 94-471.
      Tissue: Liver.
    6. "Tissue-specific structure/function differentiation of the liver isoform of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."
      Lee Y.H., Li Y., Uyeda K., Hasemann C.A.
      J. Biol. Chem. 278:523-530(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 40-471 IN COMPLEX WITH ATP ANALOG, SUBUNIT.

    Entry informationi

    Entry nameiF261_HUMAN
    AccessioniPrimary (citable) accession number: P16118
    Secondary accession number(s): B2RA88
    , B4DUN5, Q5JXS5, Q99951
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 159 of the entry and version 3 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 X
      Human chromosome X: 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