Detail Information for IndEnz0002013355
IED ID IndEnz0002013355
Enzyme Type ID protease013355
Protein Name UBX domain-containing protein 1
Protein 2B28
SAPK substrate protein 1
UBA/UBX 33.3 kDa protein
mY33K
Gene Name Ubxn1 D19Ertd721e Saks1
Organism Mus musculus (Mouse)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MAELTALESLIEMGFPRGRAEKALALTGNQGIEAAMDWLMEHEDDPDVDEPLETPLSHVLGREPTPSEQVGPEGSGSAAGESRPILTEEERQEQTKRMLELVAQKQREREEREEREALEREKQRRRQGQELSVARQKLQEDEMRRAAEERRREKAEELAARQRVREKIERDKAERAKKYGGSVGSRSSPPATDPGPVPSSPSQEPPTKREYDQCRIQVRLPDGTSLTQTFRAREQLAAVRLYVELHRGEEPGQDQDPVQLLSGFPRRAFSEADMERPLQELGLVPSAVLIVAKKCPS
Enzyme Length 297
Uniprot Accession Number Q922Y1
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Ubiquitin-binding protein that plays a role in the modulation of innate immune response. Blocks both the RIG-I-like receptors (RLR) and NF-kappa-B pathways. Following viral infection, UBXN1 is induced and recruited to the RLR component MAVS. In turn, interferes with MAVS oligomerization, and disrupts the MAVS/TRAF3/TRAF6 signalosome. This function probably serves as a brake to prevent excessive RLR signaling. Interferes with the TNFalpha-triggered NF-kappa-B pathway by interacting with cellular inhibitors of apoptosis proteins (cIAPs) and thereby inhibiting their recruitment to TNFR1. Prevents also the activation of NF-kappa-B by associating with CUL1 and thus inhibiting NF-kappa-B inhibitor alpha/NFKBIA degradation that remains bound to NF-kappa-B. Interacts with the BRCA1-BARD1 heterodimer and regulates its activity. Specifically binds 'Lys-6'-linked polyubiquitin chains. Interaction with autoubiquitinated BRCA1 leads to the inhibition of the E3 ubiquitin-protein ligase activity of the BRCA1-BARD1 heterodimer. Component of a complex required to couple deglycosylation and proteasome-mediated degradation of misfolded proteins in the endoplasmic reticulum that are retrotranslocated in the cytosol. {ECO:0000250|UniProtKB:Q04323, ECO:0000269|PubMed:16709668}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Compositional bias (1); Domain (2); Helix (3); Initiator methionine (1); Modified residue (6); Region (2); Turn (1)
Keywords 3D-structure;Acetylation;Coiled coil;Cytoplasm;Phosphoprotein;Reference proteome
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15944415}.
Modified Residue MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000250|UniProtKB:Q04323; MOD_RES 199; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 200; /note=Phosphoserine; by MAPK12; /evidence=ECO:0000250|UniProtKB:Q04323; MOD_RES 207; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q04323; MOD_RES 229; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q04323; MOD_RES 270; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q04323
Post Translational Modification
Signal Peptide
Structure 3D NMR spectroscopy (1)
Cross Reference PDB 1WHC;
Mapped Pubmed ID 10725249; 11217851; 12466851; 12477932; 14610273; 15761153; 18554416; 18799693; 21311561;
Motif
Gene Encoded By
Mass 33,573
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda