Reviewed,
UniProtKB/Swiss-Prot P16862 (K6PF2_YEAST)
Last modified
November 3, 2009.
Version 103.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 6-phosphofructokinase subunit beta EC=2.7.1.11 Alternative name(s): Phosphofructokinase 2 Phosphohexokinase 6PF-1-K subunit beta | ||||||
| Gene names |
| ||||||
| Organism | Saccharomyces cerevisiae (Baker's yeast) [Complete proteome] | ||||||
| Taxonomic identifier | 4932 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces |
Protein attributes
| Sequence length | 959 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. |
| Enzyme regulation | Allosterically inhibited by ATP and activated by AMP and fructose 2,6-bisphosphate By similarity. |
| Pathway | |
| Subunit structure | Heterooctamer of 4 alpha and 4 beta chains. |
| Subcellular location | |
| Miscellaneous | Present with 90200 molecules/cell in log phase SD medium. Ref.5 |
| Sequence similarities | Belongs to the phosphofructokinase family. Two domains subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Cytoplasm |
| Domain | Repeat |
| Ligand | ATP-binding Magnesium Nucleotide-binding |
| Molecular function | Kinase Transferase |
| PTM | Methylation Phosphoprotein |
| Technical term | Allosteric enzyme Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | glycolysis Inferred from direct assay. Source: SGD proton transportInferred from genetic interaction. Source: UniProtKB |
| Cellular component | 6-phosphofructokinase complex Inferred from mutant phenotype. Source: SGD mitochondrionInferred from direct assay. Source: SGD |
| Molecular function | 6-phosphofructokinase activity Inferred from mutant phenotype. Source: SGD ATP bindingInferred from electronic annotation. Source: UniProtKB-KW magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW protein bindingInferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| GIS4 | Q04233 | 1 | EBI-9435,EBI-27721 | |
| PFK1 | P16861 | 1 | EBI-9435,EBI-9428 | |
| PRP40 | P33203 | 1 | EBI-9435,EBI-701 | |
| RSP5 | P39940 | 1 | EBI-9435,EBI-16219 | |
| SSM4 | P40318 | 1 | EBI-9435,EBI-18208 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.3 | ||||||
| Chain | 2 – 959 | 958 | 6-phosphofructokinase subunit beta | PRO_0000112046 | |||||
Regions | |||||||||
| Nucleotide binding | 216 – 220 | 5 | ATP By similarity | ||||||
| Nucleotide binding | 375 – 379 | 5 | ATP By similarity | ||||||
| Nucleotide binding | 392 – 408 | 17 | ATP By similarity | ||||||
Sites | |||||||||
| Active site | 348 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 383 | 1 | Substrate By similarity | ||||||
| Binding site | 481 | 1 | Substrate By similarity | ||||||
| Binding site | 484 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 41 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 42 | 1 | Phosphoserine Ref.11 Ref.7 | ||||||
| Modified residue | 152 | 1 | Phosphothreonine Ref.11 | ||||||
| Modified residue | 160 | 1 | Phosphoserine Ref.11 Ref.7 Ref.6 | ||||||
| Modified residue | 163 | 1 | Phosphoserine Ref.11 Ref.8 Ref.10 | ||||||
| Modified residue | 166 | 1 | Phosphoserine Ref.11 Ref.10 | ||||||
| Modified residue | 167 | 1 | Phosphoserine Ref.11 Ref.10 | ||||||
| Modified residue | 171 | 1 | Phosphoserine Ref.11 Ref.7 Ref.6 Ref.8 Ref.10 Ref.4 Ref.9 | ||||||
| Modified residue | 172 | 1 | Phosphotyrosine Ref.11 | ||||||
| Modified residue | 173 | 1 | Phosphothreonine Ref.11 Ref.10 Ref.9 | ||||||
| Modified residue | 177 | 1 | Phosphotyrosine Ref.11 | ||||||
| Modified residue | 180 | 1 | N6-methyllysine Ref.9 | ||||||
| Modified residue | 184 | 1 | Phosphothreonine Ref.11 | ||||||
| Modified residue | 514 | 1 | Phosphothreonine Ref.11 | ||||||
| Modified residue | 803 | 1 | Phosphoserine Ref.11 | ||||||
Experimental info | |||||||||
| Sequence conflict | 137 | 1 | V → G in AAA34860. Ref.1 | ||||||
| Sequence conflict | 880 | 1 | K → E in AAA34860. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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: 2528496] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. Barrell B.G.Nature 387:90-93(1997) [PubMed: 9169872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972. |
| [3] | "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: 8223596] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-12; 181-185 AND 193-197. |
| [4] | "Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171, MASS SPECTROMETRY. |
| [5] | "Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. |
| [6] | "A proteomics approach to understanding protein ubiquitination." Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P. Nat. Biotechnol. 21:921-926(2003) [PubMed: 12872131] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160 AND SER-171, MASS SPECTROMETRY. |
| [7] | "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: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-160 AND SER-171, MASS SPECTROMETRY. |
| [8] | "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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND SER-171, MASS SPECTROMETRY. |
| [9] | "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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171 AND THR-173, METHYLATION AT LYS-180, MASS SPECTROMETRY. |
| [10] | "Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163; SER-166; SER-167; SER-171 AND THR-173, MASS SPECTROMETRY. |
| [11] | "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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-42; THR-152; SER-160; SER-163; SER-166; SER-167; SER-171; TYR-172; THR-173; TYR-177; THR-184; THR-514 AND SER-803, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| M26944 Genomic DNA. Translation: AAA34860.1. Z48755 Genomic DNA. Translation: CAA88646.1. | |
| PIR | JQ0017. S59446. |
| RefSeq | NP_013932.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 3PFK based on UniProtKB P00512. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:2619N. |
| IntAct | P16862. 39 interactions. |
| STRING | P16862. |
Proteomic databases | |
| PeptideAtlas | P16862. |
| PRIDE | P16862. |
Genome annotation databases | |
| Ensembl | YMR205C; YMR205C; YMR205C; Saccharomyces cerevisiae. [Genome view] |
| GeneID | 855245. |
| GenomeReviews | Gene locus YMR205C in contig Z71257_GR. |
| KEGG | sce:YMR205C. |
| NMPDR | fig|4932.3.peg.4985. |
Organism-specific databases | |
| CYGD | YMR205c. |
| SGD | S000004818. PFK2. |
Phylogenomic databases | |
| HOGENOM | P16862. |
| OMA | ANSHSRA. |
Enzyme and pathway databases | |
| BRENDA | 2.7.1.11. 250. |
Gene expression databases | |
| ArrayExpress | P16862. |
| Genevestigator | P16862. |
| GermOnline | YMR205C. Saccharomyces cerevisiae. |
Family and domain databases | |
| InterPro | IPR009161. 6-phosphofructokinase_euk. IPR000023. Phosphofructokinase. IPR015912. Phosphofructokinase_CS. [Graphical view] |
| Pfam | PF00365. PFK. 2 hits. [Graphical view] |
| PIRSF | PIRSF000533. ATP_PFK_euk. 1 hit. |
| PRINTS | PR00476. PHFRCTKINASE. |
| ProDom | PD000707. Ppfruckinase. 2 hits. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR02478. 6PF1K_euk. 1 hit. |
| PROSITE | PS00433. PHOSPHOFRUCTOKINASE. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 978807. |
Entry information
| Entry name | K6PF2_YEAST | ||||||||
| Accession | Primary (citable) accession number: P16862 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome XIII Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names |

Clusters with


