Search by BoMiProt ID - Bomi2478


Primary Information

BoMiProt ID Bomi2478
Protein Name Phosphoglycerate kinase 1
Organism Bos taurus
Uniprot IDQ3T0P6
Milk FractionMFGM, Exosome
Ref Sequence ID NP_001029471.1
Aminoacid Length 417
Molecular Weight 44538
FASTA Sequence Download
Gene Name PGK1
Gene ID 507476
Protein Existence Status Reveiwed:Experimental evidence at transcript level

Secondary Information

Protein Function Phosphoglycerate kinase 1 (PGK1) is the first critical enzyme to produce ATP in the glycolytic pathway. PGK1 is not only a metabolic enzyme but also a protein kinase, which mediates the tumor growth, migration and invasion through phosphorylation of some important substrates. 
Biochemical Properties PGK exists in all organisms and contains 2–3 isozymes in most organisms. There are two subtypes of PGK1 and PGK2 in human genome, with similar structure and function, and more than 80% of similar amino acid sequences.PGK is a bilobed enzyme with two functional domains, including the nucleotide binding domain (NBD) and the catalytic domain (CD). 3-phosphoglyceric acid binds to the N domain, and Mg-complex nucleotides bind to the C domain, increasing the structural stability of the whole PGK1 molecule.
PTMs N6-acetylation at Lysine, Hydroxylation, Phosphorylation at Ser/Tyr
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
Predicted Disorder Regions (372-386)
DisProt Annotation
TM Helix Prediction No TM helices
Bibliography 1.Fu Q, Yu Z. Phosphoglycerate kinase 1 (PGK1) in cancer: A promising target for diagnosis and therapy. Life Sci. 2020 Sep 1;256:117863. doi: 10.1016/j.lfs.2020.117863. Epub 2020 May 30. PMID: 32479953. 2.J.R. McCarrey, W.M. Berg, S.J. Paragioudakis, P.L. Zhang, D.D. Dilworth, B.L. Arnold, J.J. Rossi.Differential transcription of Pgk genes during spermatogenesis in the mouse.Dev. Biol., 154 (1992), pp. 160-168. 3.A. Varga, B. Flachner, E. Graczer, S. Osvath, A.N. Szilagyi, M. Vas.Correlation between conformational stability of the ternary enzyme-substrate complex and domain closure of 3-phosphoglycerate kinase.FEBS J., 272 (2005), pp. 1867-1885.