Search by BoMiProt ID - Bomi74


Primary Information

BoMiProt ID Bomi74
Protein Name Proteasome activator complex subunit 1
Organism Bos taurus
Uniprot IDQ4U5R3
Milk FractionExosome
Aminoacid Length 249
Molecular Weight 28663
FASTA Sequence Download
Gene Name PSME1
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondary Information

Presence in other biological fluids/tissue/cells PA28 family members, which are found in higher eukaryotes; identified in soluble extracts of bovine red blood cells; PA28a and b subunits are expressed in many organs, they are particularly abundant in immune tissues and are virtually absent from the brain
Protein Function Also known as PA28, activator of 20s proteasome complex; active PA28 binds to the proteasome to form a protease-activator complex; activators that bind to proteasomes and stimulate the hydrolysis of peptides
Biochemical Properties exist as homo- or heteromeric complexes; presence of three PA28 homologs, called α,ß and ɣ; α and ß subunits form a heteroheptamer, whereas ɣ forms a homoheptamer; PA28 was purified from extracts of rat liver, which had high levels of PA28 protein but no PA28 activity; Carboxypeptidase inactivates PA28; bovine PA28 contain a 'KEKE motif', which is characterized by a high content of alternating lysine and glutamic acid residues;
Significance in milk Higher expression indicate enhanced mammary protein catabolism in cows
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
Predicted Disorder Regions 55-102
DisProt Annotation
TM Helix Prediction No TM helices
Linking IDs
Bibliography 1. Piccinini, M., Tazartes, O., Mostert, M., Musso, A., DeMarchi, M., & Rinaudo, M. T. (2000). Structural and functional characterization of 20S and 26S proteasomes from bovine brain. Brain Research. Molecular Brain Research, 76(1), 103–114. https://doi.org/10.1016/s0169-328x(99)00337-x.
2. Sharon, M., Taverner, T., Ambroggio, X. I., Deshaies, R. J., & Robinson, C. V. (2006). Structural organization of the 19S proteasome lid: Insights from MS of intact complexes. PLoS Biology, 4(8), 1314–1323. https://doi.org/10.1371/journal.pbio.0040267.
3. Wei, S.-J., Williams, J. G., Dang, H., Darden, T. A., Betz, B. L., Humble, M. M., … Tennant, R. W. (2008). Identification of a specific motif of the DSS1 protein required for proteasome interaction and p53 protein degradation. Journal of Molecular Biology, 383(3), 693–712. https://doi.org/10.1016/j.jmb.2008.08.044.