Detail Information for IndEnz0002011572
IED ID IndEnz0002011572
Enzyme Type ID protease011572
Protein Name Proteasome activator complex subunit 3
Activator of multicatalytic protease subunit 3
Proteasome activator 28 subunit gamma
PA28g
PA28gamma
Gene Name PSME3 RCJMB04_15e19 RCJMB04_5i13
Organism Gallus gallus (Chicken)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Archelosauria Archosauria Dinosauria Saurischia Theropoda Coelurosauria Aves Neognathae Galloanserae Galliformes Phasianidae (turkeys) Phasianinae Gallus Gallus gallus (Chicken)
Enzyme Sequence MASLLKVDPEVKLKVDSFRERITSEAEDLVANFFPKKLLELDGFLKEPILNIHDLTQIHSDMNLPVPDPILLTNSHDGLDGPNMKKRKLEDREETFQGTKVFVMPNGMLKSNQQLVDIIEKVKPEIRLLIEKCNTVKMWVQLLIPRIEDGNNFGVSIQEETVAELRTVESEAASYLDQISRYYITRAKLVSKIAKYPHVEDYRRTVTEIDEKEYISLRLIISELRNQYVTLHDMILKNIEKIKRPRSSNAETLY
Enzyme Length 254
Uniprot Accession Number Q5F3J5
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Implicated in immunoproteasome assembly and required for efficient antigen processing. The PA28 activator complex enhances the generation of class I binding peptides by altering the cleavage pattern of the proteasome (By similarity). {ECO:0000250|UniProtKB:P61290}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Modified residue (3); Sequence conflict (1)
Keywords Acetylation;Proteasome;Reference proteome
Interact With
Induction
Subcellular Location
Modified Residue MOD_RES 6; /note=N6-acetyllysine; /evidence=ECO:0000250; MOD_RES 14; /note=N6-acetyllysine; /evidence=ECO:0000250; MOD_RES 195; /note=N6-acetyllysine; by P300/CBP; /evidence=ECO:0000250
Post Translational Modification PTM: Acetylation at the major site Lys-195 is important for oligomerization and ability to degrade its target substrates. Deacetylated by SIRT1 (By similarity). {ECO:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 29,481
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda