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P16862

- PFKA2_YEAST

UniProt

P16862 - PFKA2_YEAST

Protein

ATP-dependent 6-phosphofructokinase subunit beta

Gene

PFK2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.8 PublicationsUniRule annotation

    Catalytic activityi

    ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.1 PublicationUniRule annotation

    Cofactori

    Magnesium.

    Enzyme regulationi

    Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.3 PublicationsUniRule annotation

    Kineticsi

    1. KM=0.24 mM for ATP (without effector)1 Publication
    2. KM=0.3 mM for ATP (with 1 mM AMP)1 Publication
    3. KM=0.31 mM for ATP (with 20 µM fructose 2,6-bisphosphate)1 Publication
    4. KM=1.65 mM for fructose 6-phosphate (without effector)1 Publication
    5. KM=0.51 mM for fructose 6-phosphate (with 1 mM AMP)1 Publication
    6. KM=0.11 mM for fructose 6-phosphate (with 20 µM fructose 2,6-bisphosphate)1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei206 – 2061ATP; via amide nitrogenUniRule annotation
    Metal bindingi301 – 3011Magnesium; catalytic
    Active sitei348 – 3481Proton acceptor
    Binding sitei383 – 3831Substrate; shared with subunit alpha
    Binding sitei447 – 4471Substrate
    Binding sitei475 – 4751Substrate; shared with subunit alpha
    Binding sitei658 – 6581Allosteric activator fructose 2,6-bisphosphate1 PublicationUniRule annotation
    Binding sitei754 – 7541Allosteric activator fructose 2,6-bisphosphate; shared with subunit alphaUniRule annotation
    Binding sitei847 – 8471Allosteric activator fructose 2,6-bisphosphate; shared with subunit alphaUniRule annotation
    Binding sitei935 – 9351Allosteric activator fructose 2,6-bisphosphate1 PublicationUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi270 – 2712ATPUniRule annotation
    Nucleotide bindingi300 – 3034ATPUniRule annotation

    GO - Molecular functioni

    1. 6-phosphofructokinase activity Source: SGD
    2. ATP binding Source: UniProtKB-KW
    3. metal ion binding Source: UniProtKB-KW
    4. mRNA binding Source: SGD
    5. protein binding Source: IntAct

    GO - Biological processi

    1. carbohydrate phosphorylation Source: GOC
    2. fructose 6-phosphate metabolic process Source: InterPro
    3. glycolytic process Source: SGD
    4. hydrogen ion transmembrane transport Source: GOC
    5. proton transport Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:YMR205C-MONOMER.
    SABIO-RKP16862.
    UniPathwayiUPA00109; UER00182.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent 6-phosphofructokinase subunit betaUniRule annotation (EC:2.7.1.11UniRule annotation)
    Alternative name(s):
    ATP-dependent 6-phosphofructokinaseUniRule annotation
    Short name:
    ATP-PFKUniRule annotation
    Short name:
    Phosphofructokinase 2UniRule annotation
    PhosphohexokinaseUniRule annotation
    Gene namesi
    Name:PFK2
    Ordered Locus Names:YMR205C
    ORF Names:YM8325.06C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIII

    Organism-specific databases

    SGDiS000004818. PFK2.

    Subcellular locationi

    GO - Cellular componenti

    1. 6-phosphofructokinase complex Source: SGD
    2. mitochondrial outer membrane Source: UniProtKB-SubCell
    3. mitochondrion Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi301 – 3011D → T: Reduces maximal activity of the holoenzyme by 30%. 1 Publication
    Mutagenesisi348 – 3481D → S: Reduces maximal activity of the holoenzyme by 50%. Completely abolishes catalytic activity; when associated with 'T-309' or 'S-356' in subunit alpha. 1 Publication
    Mutagenesisi439 – 4391R → V: Reduces maximal activity of the holoenzyme by less than 25%. 1 Publication
    Mutagenesisi481 – 4811H → S: Increases the KM for fructose 6-phosphate 50 fold. 1 Publication
    Mutagenesisi718 – 7181S → D: Abolishes sensitivity of the holoenzyme to fructose 2,6-bisphosphate activation; when associated with 'D-724' in subunit alpha. 1 Publication
    Mutagenesisi722 – 7221P → L: Drastically reduces sensitivity of the holoenzyme to ATP inhibition. 1 Publication
    Mutagenesisi853 – 8531H → S: Reduces sensitivity of the holoenzyme to fructose 2,6-bisphosphate activation; when associated with 'S-859' in subunit alpha. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 959958ATP-dependent 6-phosphofructokinase subunit betaPRO_0000112046Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei152 – 1521Phosphothreonine1 Publication
    Modified residuei163 – 1631Phosphoserine2 Publications
    Modified residuei171 – 1711Phosphoserine2 Publications
    Modified residuei803 – 8031Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP16862.
    PaxDbiP16862.
    PeptideAtlasiP16862.

    Expressioni

    Gene expression databases

    GenevestigatoriP16862.

    Interactioni

    Subunit structurei

    Heterooctamer of 4 alpha and 4 beta chains.3 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PFK1P168614EBI-9435,EBI-9428
    RSP5P399403EBI-9435,EBI-16219

    Protein-protein interaction databases

    BioGridi35383. 169 interactions.
    DIPiDIP-2619N.
    IntActiP16862. 42 interactions.
    MINTiMINT-424355.
    STRINGi4932.YMR205C.

    Structurei

    Secondary structure

    1
    959
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi198 – 2069
    Helixi211 – 22515
    Beta strandi228 – 2325
    Helixi235 – 2406
    Turni244 – 2463
    Beta strandi247 – 2504
    Helixi252 – 2554
    Helixi258 – 2603
    Helixi273 – 2753
    Helixi277 – 28913
    Beta strandi294 – 2996
    Helixi301 – 32222
    Beta strandi325 – 3273
    Helixi329 – 3346
    Beta strandi339 – 3457
    Helixi360 – 38021
    Beta strandi384 – 3896
    Helixi396 – 40510
    Beta strandi408 – 4114
    Helixi421 – 43515
    Beta strandi441 – 4466
    Helixi459 – 46810
    Beta strandi474 – 4785
    Helixi480 – 4834
    Helixi490 – 50920
    Beta strandi517 – 5248
    Beta strandi526 – 5305
    Helixi531 – 54616
    Helixi550 – 5567
    Helixi561 – 57313
    Beta strandi581 – 5844
    Beta strandi588 – 5969
    Helixi601 – 61515
    Beta strandi618 – 6225
    Helixi625 – 6328
    Beta strandi635 – 6373
    Helixi640 – 6434
    Helixi646 – 6483
    Helixi661 – 6644
    Helixi666 – 67611
    Beta strandi679 – 6868
    Helixi687 – 69711
    Turni698 – 7025
    Helixi704 – 7063
    Beta strandi712 – 7154
    Helixi730 – 75122
    Beta strandi752 – 7609
    Helixi767 – 77610
    Beta strandi779 – 7824
    Turni784 – 7863
    Helixi790 – 80718
    Beta strandi815 – 8206
    Helixi821 – 8233
    Helixi829 – 84012
    Beta strandi845 – 8506
    Helixi852 – 8565
    Helixi862 – 88120
    Helixi884 – 8896
    Beta strandi890 – 8945
    Helixi901 – 9044
    Beta strandi907 – 9115
    Beta strandi913 – 9153
    Beta strandi918 – 9214
    Helixi922 – 9287
    Helixi932 – 9343
    Beta strandi935 – 9395
    Helixi943 – 95210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3O8OX-ray2.90B/D/F/H194-959[»]
    ProteinModelPortaliP16862.
    SMRiP16862. Positions 9-957.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 573572N-terminal catalytic PFK domain 1Add
    BLAST
    Regioni346 – 3483Substrate binding
    Regioni390 – 3923Substrate binding
    Regioni481 – 4844Substrate binding
    Regioni574 – 58714Interdomain linkerAdd
    BLAST
    Regioni588 – 959372C-terminal regulatory PFK domain 2Add
    BLAST
    Regioni716 – 7205Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
    Regioni716 – 7183Allosteric activator fructose 2,6-bisphosphate binding
    Regioni761 – 7633Allosteric activator fructose 2,6-bisphosphate binding
    Regioni853 – 8564Allosteric activator fructose 2,6-bisphosphate binding

    Sequence similaritiesi

    Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E" sub-subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0205.
    GeneTreeiENSGT00390000013209.
    HOGENOMiHOG000200154.
    KOiK00850.
    OMAiMEYCDVV.
    OrthoDBiEOG7Q5HPV.

    Family and domain databases

    Gene3Di3.10.180.10. 1 hit.
    HAMAPiMF_03184. Phosphofructokinase_I_E.
    InterProiIPR009161. 6-phosphofructokinase_euk.
    IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
    IPR022953. Phosphofructokinase.
    IPR015912. Phosphofructokinase_CS.
    IPR000023. Phosphofructokinase_dom.
    [Graphical view]
    PfamiPF00365. PFK. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
    PRINTSiPR00476. PHFRCTKINASE.
    SUPFAMiSSF53784. SSF53784. 2 hits.
    SSF54593. SSF54593. 1 hit.
    TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
    PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P16862-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTVTTPFVNG TSYCTVTAYS VQSYKAAIDF YTKFLSLENR SSPDENSTLL    50
    SNDSISLKIL LRPDEKINKN VEAHLKELNS ITKTQDWRSH ATQSLVFNTS 100
    DILAVKDTLN AMNAPLQGYP TELFPMQLYT LDPLGNVVGV TSTKNAVSTK 150
    PTPPPAPEAS AESGLSSKVH SYTDLAYRMK TTDTYPSLPK PLNRPQKAIA 200
    VMTSGGDAPG MNSNVRAIVR SAIFKGCRAF VVMEGYEGLV RGGPEYIKEF 250
    HWEDVRGWSA EGGTNIGTAR CMEFKKREGR LLGAQHLIEA GVDALIVCGG 300
    DGSLTGADLF RSEWPSLIEE LLKTNRISNE QYERMKHLNI CGTVGSIDND 350
    MSTTDATIGA YSALDRICKA IDYVEATANS HSRAFVVEVM GRNCGWLALL 400
    AGIATSADYI FIPEKPATSS EWQDQMCDIV SKHRSRGKRT TIVVVAEGAI 450
    AADLTPISPS DVHKVLVDRL GLDTRITTLG HVQRGGTAVA YDRILATLQG 500
    LEAVNAVLES TPDTPSPLIA VNENKIVRKP LMESVKLTKA VAEAIQAKDF 550
    KRAMSLRDTE FIEHLNNFMA INSADHNEPK LPKDKRLKIA IVNVGAPAGG 600
    INSAVYSMAT YCMSQGHRPY AIYNGWSGLA RHESVRSLNW KDMLGWQSRG 650
    GSEIGTNRVT PEEADLGMIA YYFQKYEFDG LIIVGGFEAF ESLHQLERAR 700
    ESYPAFRIPM VLIPATLSNN VPGTEYSLGS DTALNALMEY CDVVKQSASS 750
    TRGRAFVVDC QGGNSGYLAT YASLAVGAQV SYVPEEGISL EQLSEDIEYL 800
    AQSFEKAEGR GRFGKLILKS TNASKALSAT KLAEVITAEA DGRFDAKPAY 850
    PGHVQQGGLP SPIDRTRATR MAIKAVGFIK DNQAAIAEAR AAEENFNADD 900
    KTISDTAAVV GVKGSHVVYN SIRQLYDYET EVSMRMPKVI HWQATRLIAD 950
    HLVGRKRVD 959
    Length:959
    Mass (Da):104,618
    Last modified:January 23, 2007 - v4
    Checksum:i82CE6402CEDBBCB2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti137 – 1371V → G in AAA34860. (PubMed:2528496)Curated
    Sequence conflicti880 – 8801K → E in AAA34860. (PubMed:2528496)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26944 Genomic DNA. Translation: AAA34860.1.
    Z48755 Genomic DNA. Translation: CAA88646.1.
    BK006946 Genomic DNA. Translation: DAA10104.1.
    PIRiS59446. JQ0017.
    RefSeqiNP_013932.1. NM_001182712.1.

    Genome annotation databases

    EnsemblFungiiYMR205C; YMR205C; YMR205C.
    GeneIDi855245.
    KEGGisce:YMR205C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26944 Genomic DNA. Translation: AAA34860.1 .
    Z48755 Genomic DNA. Translation: CAA88646.1 .
    BK006946 Genomic DNA. Translation: DAA10104.1 .
    PIRi S59446. JQ0017.
    RefSeqi NP_013932.1. NM_001182712.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3O8O X-ray 2.90 B/D/F/H 194-959 [» ]
    ProteinModelPortali P16862.
    SMRi P16862. Positions 9-957.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35383. 169 interactions.
    DIPi DIP-2619N.
    IntActi P16862. 42 interactions.
    MINTi MINT-424355.
    STRINGi 4932.YMR205C.

    Proteomic databases

    MaxQBi P16862.
    PaxDbi P16862.
    PeptideAtlasi P16862.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YMR205C ; YMR205C ; YMR205C .
    GeneIDi 855245.
    KEGGi sce:YMR205C.

    Organism-specific databases

    SGDi S000004818. PFK2.

    Phylogenomic databases

    eggNOGi COG0205.
    GeneTreei ENSGT00390000013209.
    HOGENOMi HOG000200154.
    KOi K00850.
    OMAi MEYCDVV.
    OrthoDBi EOG7Q5HPV.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00182 .
    BioCyci YEAST:YMR205C-MONOMER.
    SABIO-RK P16862.

    Miscellaneous databases

    NextBioi 978807.

    Gene expression databases

    Genevestigatori P16862.

    Family and domain databases

    Gene3Di 3.10.180.10. 1 hit.
    HAMAPi MF_03184. Phosphofructokinase_I_E.
    InterProi IPR009161. 6-phosphofructokinase_euk.
    IPR029068. Glyas_Bleomycin-R_OHBP_Dase.
    IPR022953. Phosphofructokinase.
    IPR015912. Phosphofructokinase_CS.
    IPR000023. Phosphofructokinase_dom.
    [Graphical view ]
    Pfami PF00365. PFK. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF000533. ATP_PFK_euk. 1 hit.
    PRINTSi PR00476. PHFRCTKINASE.
    SUPFAMi SSF53784. SSF53784. 2 hits.
    SSF54593. SSF54593. 1 hit.
    TIGRFAMsi TIGR02478. 6PF1K_euk. 1 hit.
    PROSITEi PS00433. PHOSPHOFRUCTOKINASE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The phosphofructokinase genes of yeast evolved from two duplication events."
      Heinisch J.J., Ritzel R.G., von Borstel R.C., Aguilera A., Rodicio R., Zimmermann F.K.
      Gene 78:309-321(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Limited proteolysis of yeast phosphofructokinase. Sequence locations of cleavage sites created by the actions of different proteinases."
      Kopperschlaeger G., Baer J., Stellwagen E.
      Eur. J. Biochem. 217:527-533(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-12; 181-185 AND 193-197.
    5. "Physicochemical parameters and subunit composition of yeast phosphofructokinase."
      Kopperschlaeger G., Baer J., Nissler K., Hofmann E.
      Eur. J. Biochem. 81:317-325(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    6. "Activation by phosphate of yeast phosphofructokinase."
      Banuelos M., Gancedo C., Gancedo J.M.
      J. Biol. Chem. 252:6394-6398(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    7. "Phosphorus-31 nuclear magnetic resonance studies of wild-type and glycolytic pathway mutants of Saccharomyces cerevisiae."
      Navon G., Shulman R.G., Yamane T., Eccleshall T.R., Lam K.B., Baronofsky J.J., Marmur J.
      Biochemistry 18:4487-4499(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Stimulation of yeast phosphofructokinase activity by fructose 2,6-bisphosphate."
      Avigad G.
      Biochem. Biophys. Res. Commun. 102:985-991(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    9. "Mutant studies of yeast phosphofructokinase."
      Clifton D., Fraenkel D.G.
      Biochemistry 21:1935-1942(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Similarity of activation of yeast phosphofructokinase by AMP and fructose-2,6-bisphosphate."
      Nissler K., Otto A., Schellenberger W., Hofmann E.
      Biochem. Biophys. Res. Commun. 111:294-300(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    11. "Temporal organization of the phosphofructokinase/fructose-1,6-biphosphatase cycle."
      Hofmann E., Eschrich K., Schellenberger W.
      Adv. Enzyme Regul. 23:331-362(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "An electron microscopy study of the quarternary structure of yeast phosphofructokinase."
      Nissler K., Hofmann E., Stel'maschchuk V., Orlova E., Kiselev N.
      Biomed. Biochim. Acta 44:251-259(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    13. "Isolation and characterization of the two structural genes coding for phosphofructokinase in yeast."
      Heinisch J.
      Mol. Gen. Genet. 202:75-82(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Studies on the function of yeast phosphofructokinase subunits by in vitro mutagenesis."
      Arvanitidis A., Heinisch J.J.
      J. Biol. Chem. 269:8911-8918(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-301; ASP-348; ARG-439 AND HIS-481.
    15. "A yeast phosphofructokinase insensitive to the allosteric activator fructose 2,6-bisphosphate. Glycolysis/metabolic regulation/allosteric control."
      Heinisch J.J., Boles E., Timpel C.
      J. Biol. Chem. 271:15928-15933(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF SER-718 AND HIS-853.
    16. "Single point mutations in either gene encoding the subunits of the heterooctameric yeast phosphofructokinase abolish allosteric inhibition by ATP."
      Rodicio R., Strauss A., Heinisch J.J.
      J. Biol. Chem. 275:40952-40960(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF PRO-722.
    17. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    18. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
      Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
      Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: YAL6B.
    19. Cited for: SUBCELLULAR LOCATION.
    20. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND SER-171, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    21. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Detection and localisation of protein-protein interactions in Saccharomyces cerevisiae using a split-GFP method."
      Barnard E., McFerran N.V., Trudgett A., Nelson J., Timson D.J.
      Fungal Genet. Biol. 45:597-604(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    23. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-803, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-152; SER-163 AND SER-171, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "The crystal structures of eukaryotic phosphofructokinases from baker's yeast and rabbit skeletal muscle."
      Banaszak K., Mechin I., Obmolova G., Oldham M., Chang S.H., Ruiz T., Radermacher M., Kopperschlager G., Rypniewski W.
      J. Mol. Biol. 407:284-297(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 194-959 IN COMPLEX WITH SUBSTRATE FRUCTOSE 6-PHOSPHATE AND ALLOSTERIC ACTIVATOR FRUCTOSE 2,6-BISPHOSPHATE.

    Entry informationi

    Entry nameiPFKA2_YEAST
    AccessioniPrimary (citable) accession number: P16862
    Secondary accession number(s): D6W030
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 149 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 90200 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome XIII
      Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

    External Data

    Dasty 3