Detail Information for IndEnz0002008590
IED ID IndEnz0002008590
Enzyme Type ID protease008590
Protein Name 26S proteasome non-ATPase regulatory subunit 4 homolog
26S proteasome regulatory subunit RPN10
AtRPN10
26S proteasome regulatory subunit S5A homolog
Multiubiquitin chain-binding protein 1
AtMCB1
Gene Name RPN10 MBP1 MCB1 At4g38630 F20M13.190 T9A14.7
Organism Arabidopsis thaliana (Mouse-ear cress)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress)
Enzyme Sequence MVLEATMICIDNSEWMRNGDYSPSRLQAQTEAVNLLCGAKTQSNPENTVGILTMAGKGVRVLTTPTSDLGKILACMHGLDVGGEINLTAAIQIAQLALKHRQNKNQRQRIIVFAGSPIKYEKKALEIVGKRLKKNSVSLDIVNFGEDDDEEKPQKLEALLTAVNNNDGSHIVHVPSGANALSDVLLSTPVFTGDEGASGYVSAAAAAAAAGGDFDFGVDPNIDPELALALRVSMEEERARQEAAAKKAADEAGQKDKDGDTASASQETVARTTDKNAEPMDEDSALLDQAIAMSVGDVNMSEAADEDQDLALALQMSMSGEESSEATGAGNNLLGNQAFISSVLSSLPGVDPNDPAVKELLASLPDESKRTEEEESSSKKGEDEKK
Enzyme Length 386
Uniprot Accession Number P55034
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Plays a role in maintaining the structural integrity of the 19S regulatory particle (RP), subcomplex of the 26S proteasome. Plays a major role in both the direct and indirect recognition of ubiquitinated substrates of ubiquitin/26S proteasome-mediated proteolysis (UPP). Binds and presumably selects ubiquitin-conjugates for destruction. Prefers multiubiquitin chains rather than single ubiquitins, with a binding affinity for 'Lys-48'-linked ubiquitin chains. Acts as a potential docking subunit for both ubiquitin receptors RAD23s and DSK2s. Plays a role in the growth and development via the proteasome-dependent degradation of the ABA-signaling protein ABI5/DPBF1. Plays an important role for balancing cell expansion with cell proliferation rates during shoot development. {ECO:0000269|PubMed:12671091, ECO:0000269|PubMed:17971041, ECO:0000269|PubMed:19321709, ECO:0000269|PubMed:20059542, ECO:0000269|PubMed:21764993, ECO:0000269|PubMed:22751321, ECO:0000269|PubMed:8530351, ECO:0000269|PubMed:8570648, ECO:0000269|PubMed:9442033, ECO:0000269|PubMed:9741626}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Compositional bias (2); Domain (4); Modified residue (1); Region (2); Sequence conflict (2)
Keywords Phosphoprotein;Proteasome;Reference proteome;Repeat
Interact With Q9SII8; Q9SFT9; P0CG48
Induction
Subcellular Location
Modified Residue MOD_RES 263; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:18433157
Post Translational Modification PTM: Phosphorylated by PI4KG4 in vitro. {ECO:0000269|PubMed:17880284}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10363660; 17432890; 17825468; 18420596; 18650403; 18775970; 19874541; 20087596; 20118269; 20687615; 22323770; 23952686; 25620024; 26004230; 26291247; 27477278; 27733337; 30955882; 8641424; 8887631;
Motif
Gene Encoded By
Mass 40,757
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda