Primary Information |
---|
BoMiProt ID | Bomi2478 |
---|
Protein Name | Phosphoglycerate kinase 1 |
---|
Organism | Bos taurus |
---|
Uniprot ID | Q3T0P6 |
---|
Milk Fraction | MFGM, 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. |