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P16862

- PFKA2_YEAST

UniProt

P16862 - PFKA2_YEAST

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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

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

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
Complete GO annotation...

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-KW
  3. mitochondrion Source: SGD
Complete GO annotation...

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. 171 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.
InParanoidiP16862.
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

        10         20         30         40         50
MTVTTPFVNG TSYCTVTAYS VQSYKAAIDF YTKFLSLENR SSPDENSTLL
60 70 80 90 100
SNDSISLKIL LRPDEKINKN VEAHLKELNS ITKTQDWRSH ATQSLVFNTS
110 120 130 140 150
DILAVKDTLN AMNAPLQGYP TELFPMQLYT LDPLGNVVGV TSTKNAVSTK
160 170 180 190 200
PTPPPAPEAS AESGLSSKVH SYTDLAYRMK TTDTYPSLPK PLNRPQKAIA
210 220 230 240 250
VMTSGGDAPG MNSNVRAIVR SAIFKGCRAF VVMEGYEGLV RGGPEYIKEF
260 270 280 290 300
HWEDVRGWSA EGGTNIGTAR CMEFKKREGR LLGAQHLIEA GVDALIVCGG
310 320 330 340 350
DGSLTGADLF RSEWPSLIEE LLKTNRISNE QYERMKHLNI CGTVGSIDND
360 370 380 390 400
MSTTDATIGA YSALDRICKA IDYVEATANS HSRAFVVEVM GRNCGWLALL
410 420 430 440 450
AGIATSADYI FIPEKPATSS EWQDQMCDIV SKHRSRGKRT TIVVVAEGAI
460 470 480 490 500
AADLTPISPS DVHKVLVDRL GLDTRITTLG HVQRGGTAVA YDRILATLQG
510 520 530 540 550
LEAVNAVLES TPDTPSPLIA VNENKIVRKP LMESVKLTKA VAEAIQAKDF
560 570 580 590 600
KRAMSLRDTE FIEHLNNFMA INSADHNEPK LPKDKRLKIA IVNVGAPAGG
610 620 630 640 650
INSAVYSMAT YCMSQGHRPY AIYNGWSGLA RHESVRSLNW KDMLGWQSRG
660 670 680 690 700
GSEIGTNRVT PEEADLGMIA YYFQKYEFDG LIIVGGFEAF ESLHQLERAR
710 720 730 740 750
ESYPAFRIPM VLIPATLSNN VPGTEYSLGS DTALNALMEY CDVVKQSASS
760 770 780 790 800
TRGRAFVVDC QGGNSGYLAT YASLAVGAQV SYVPEEGISL EQLSEDIEYL
810 820 830 840 850
AQSFEKAEGR GRFGKLILKS TNASKALSAT KLAEVITAEA DGRFDAKPAY
860 870 880 890 900
PGHVQQGGLP SPIDRTRATR MAIKAVGFIK DNQAAIAEAR AAEENFNADD
910 920 930 940 950
KTISDTAAVV GVKGSHVVYN SIRQLYDYET EVSMRMPKVI HWQATRLIAD

HLVGRKRVD
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. 171 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.
InParanoidi P16862.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 150 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