Basic Information
Name | Pyruvate kinase 2 (PK 2) (EC 2.7.1.40) |
Uniprot ID | P52489 |
Systematic gene name | YOR347C |
Standard gene name | PYK2 |
Gene names | PYK2 YOR347C O6342 |
Description from SGD | YOR347C PYK2 SGDID:S000005874, Chr XV from 986462-984942, Genome Release 64-3-1, reverse complement, Verified ORF, "Pyruvate kinase; appears to be modulated by phosphorylation; transcription repressed by glucose, and Pyk2p may be active under low glycolytic flux; PYK2 has a paralog, CDC19, that arose from the whole genome duplication" |
Protein length | 506 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MPESRLQRLA NLKIGTPQQL RRTSIIGTIG PKTNSCEAIT ALRKAGLNII
RLNFSHGSYE FHQSVIENAV KSEQQFPGRP LAIALDTKGP EIRTGRTLND
QDLYIPVDHQ MIFTTDASFA NTSNDKIMYI DYANLTKVIV PGRFIYVDDG
ILSFKVLQII DESNLRVQAV NSGYIASHKG VNLPNTDVDL PPLSAKDMKD
LQFGVRNGIH IVFASFIRTS EDVLSIRKAL GSEGQDIKII SKIENQQGLD
NFDEILEVTD GVMIARGDLG IEILAPEVLA IQKKLIAKCN LAGKPVICAT
QMLDSMTHNP RPTRAEVSDV GNAVLDGADC VMLSGETAKG DYPVNAVNIM
AATALIAEST IAHLALYDDL RDATPKPTST TETVAAAATA AILEQDGKAI
VVLSTTGNTA RLLSKYRPSC PIILVTRHAR TARIAHLYRG VFPFLYEPKR
LDDWGEDVHR RLKFGVEMAR SFGMVDNGDT VVSIQGFKGG VGHSNTLRIS
TVGQEF
RLNFSHGSYE FHQSVIENAV KSEQQFPGRP LAIALDTKGP EIRTGRTLND
QDLYIPVDHQ MIFTTDASFA NTSNDKIMYI DYANLTKVIV PGRFIYVDDG
ILSFKVLQII DESNLRVQAV NSGYIASHKG VNLPNTDVDL PPLSAKDMKD
LQFGVRNGIH IVFASFIRTS EDVLSIRKAL GSEGQDIKII SKIENQQGLD
NFDEILEVTD GVMIARGDLG IEILAPEVLA IQKKLIAKCN LAGKPVICAT
QMLDSMTHNP RPTRAEVSDV GNAVLDGADC VMLSGETAKG DYPVNAVNIM
AATALIAEST IAHLALYDDL RDATPKPTST TETVAAAATA AILEQDGKAI
VVLSTTGNTA RLLSKYRPSC PIILVTRHAR TARIAHLYRG VFPFLYEPKR
LDDWGEDVHR RLKFGVEMAR SFGMVDNGDT VVSIQGFKGG VGHSNTLRIS
TVGQEF
Legend
- X Phoshorylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
Use imported representation
Loading structure from server... It may take a while.
If you believe something went wrong, please make sure PDB ID is correct.
Please also make sure that WebGL is enabled in your browser.
- Internet Explorer: sorry. IE doesn't support WebGL.
- Firefox (version 4 or later): try force enable WebGL.
- Chrome: try force enable WebGL.
- Safari: enable WebGL.
References
[16, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[16, Phos] | Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications) |
[16, Phos] | MacGilvray, M.E., Shishkova, E., Place, M., Wagner, E.R., Coon, J.J., Gasch, A.P. (2020). Phosphoproteome response to dithiothreitol reveals unique versus shared features of Saccharomyces cerevisiae stress responses. Journal of Proteome Research 19(8): 3405-3417. (Publication) (All modifications) |
[24, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[24, Phos] | Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications) |
[24, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[24, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[35, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[194, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[318, Phos] | Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications) |
[334, Phos] | Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications) |
[337, Phos] | Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications) |
[405, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[406, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[409, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |