Basic Information
Name | [Pyruvate dehydrogenase (acetyl-transferring)] kinase 2, mitochondrial (PDK 2) (Pyruvate dehydrogenase kinase 2) (EC 2.7.11.2) (Protein kinase of PDH protein 2) (Pyruvate dehydrogenase complex kinase 2) (PDC kinase 2) ([Pyruvate dehydrogenase [lipoamide]] kinase 2) |
Uniprot ID | P53170 |
Systematic gene name | YGL059W |
Standard gene name | PKP2 |
Gene names | PKP2 YGL059W |
Description from SGD | YGL059W PKP2 SGDID:S000003027, Chr VII from 392223-393698, Genome Release 64-3-1, Verified ORF, "Mitochondrial protein kinase; negatively regulates activity of the pyruvate dehydrogenase complex by phosphorylating the ser-133 residue of the Pda1p subunit; acts in concert with kinase Pkp1p and phosphatases Ptc5p and Ptc6p; relocalizes from mitochondrion to cytoplasm upon DNA replication stress" |
Protein length | 491 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MSKYQINCIR YRHFLRTSNI SQIPDFTKYC IGPVNEELAP YIMETMKAYP
SNSEYINPQH YYHNRTVLVE NYLKRSPNPV SLTQLAQYYD DSTKLTRTKI
INSGKFVKEE LVIRIAHKLN QLQQLPFNVV NNFHFVQVYE SYYNIFESFR
KYPTIRTLED ASQFADFIKN MLEGFNTLNL PHLIMGALEC TILDLYPREK
MDQLLSDLLR ARISRRLIVE EHVSITANYT SGKEENTLVL GDIFQECSAK
KYLLEASEES QKFIQDMYFK DIPMPEFIIE GDTQLSFYFL PTHLKYLLGE
ILRNTYEATM KHYIRKGLEK PEPIIVTVVS NDESYLFRIS DKAGGVLHDD
ENLWSFGKSK ERAQESLNNF HKLPGLQTVS IYDEVHSHTK YNSKLKSLQS
ITLKPYMHTS LEPMSYPSII NGHIKYETPL IELLKRSFRY KLGIGLAMCK
VYAEYWNGDL SLHSMPGYGT DVVLKLGNLM KHTKKLQLDK V
SNSEYINPQH YYHNRTVLVE NYLKRSPNPV SLTQLAQYYD DSTKLTRTKI
INSGKFVKEE LVIRIAHKLN QLQQLPFNVV NNFHFVQVYE SYYNIFESFR
KYPTIRTLED ASQFADFIKN MLEGFNTLNL PHLIMGALEC TILDLYPREK
MDQLLSDLLR ARISRRLIVE EHVSITANYT SGKEENTLVL GDIFQECSAK
KYLLEASEES QKFIQDMYFK DIPMPEFIIE GDTQLSFYFL PTHLKYLLGE
ILRNTYEATM KHYIRKGLEK PEPIIVTVVS NDESYLFRIS DKAGGVLHDD
ENLWSFGKSK ERAQESLNNF HKLPGLQTVS IYDEVHSHTK YNSKLKSLQS
ITLKPYMHTS LEPMSYPSII NGHIKYETPL IELLKRSFRY KLGIGLAMCK
VYAEYWNGDL SLHSMPGYGT DVVLKLGNLM KHTKKLQLDK V
Legend
- X Phoshorylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[252, 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) |
[252, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[327, 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) |
[327, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[330, 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) |
[330, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[334, 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) |
[334, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[335, 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) |
[335, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[340, 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) |
[340, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[355, 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) |
[355, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[359, 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) |