Detail Information for IndEnz0002010037
IED ID IndEnz0002010037
Enzyme Type ID protease010037
Protein Name UBX domain-containing protein 1
SAPK substrate protein 1
UBA/UBX 33.3 kDa protein
Gene Name UBXN1 SAKS1
Organism Homo sapiens (Human)
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MAELTALESLIEMGFPRGRAEKALALTGNQGIEAAMDWLMEHEDDPDVDEPLETPLGHILGREPTSSEQGGLEGSGSAAGEGKPALSEEERQEQTKRMLELVAQKQREREEREEREALERERQRRRQGQELSAARQRLQEDEMRRAAEERRREKAEELAARQRVREKIERDKAERAKKYGGSVGSQPPPVAPEPGPVPSSPSQEPPTKREYDQCRIQVRLPDGTSLTQTFRAREQLAAVRLYVELHRGEELGGGQDPVQLLSGFPRRAFSEADMERPLQELGLVPSAVLIVAKKCPS
Enzyme Length 297
Uniprot Accession Number Q04323
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 (PubMed:23545497). 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 (PubMed:25681446). 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 (PubMed:28152074). 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 (PubMed:20351172). 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:0000269|PubMed:20351172, ECO:0000269|PubMed:23545497, ECO:0000269|PubMed:25681446, ECO:0000269|PubMed:28152074}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (1); Chain (1); Coiled coil (1); Compositional bias (2); Domain (2); Initiator methionine (1); Modified residue (6); Mutagenesis (2); Natural variant (1); Region (2); Sequence conflict (3)
Keywords Acetylation;Alternative splicing;Coiled coil;Cytoplasm;Direct protein sequencing;Host-virus interaction;Phosphoprotein;Reference proteome
Interact With V9HW80; Q9Y263; Q9HCM9; Q7KZS0; Q9UMX0; Q9UMX0-2; Q8WU02; O00154-4; Q14203-5; Q08426; P04792; Q9UBY9; O60333-2; P02545; Q9Y263; Q9BUI4; O60260-5; P54725; Q9Y3C5; P37840; Q9UHD9; O76024
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23545497}.
Modified Residue MOD_RES 2; /note="N-acetylalanine"; /evidence="ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712"; MOD_RES 199; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648"; MOD_RES 200; /note="Phosphoserine; by MAPK12"; /evidence="ECO:0000269|PubMed:15362974"; MOD_RES 207; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 229; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 270; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 15215856; 15358861; 15944415; 16055502; 16168377; 17353931; 18847512; 19367725; 19615732; 20195357; 21135095; 25416956; 26611529; 27785701; 29685906; 33754075; 34246306;
Motif
Gene Encoded By
Mass 33,325
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda