| IED ID | IndEnz0002016379 |
| Enzyme Type ID | protease016379 |
| Protein Name |
Proteasomal ubiquitin receptor ADRM1 110 kDa cell membrane glycoprotein Gp110 Adhesion-regulating molecule 1 ARM-1 Rpn13 homolog |
| Gene Name | Adrm1 Gp110 |
| 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 | MTTSGALFPSLVPGSRGSSTKYLVEFRAGKMSLKGTTVTPDKRKGLVYIQQTDDSLIHFCWKDRTSGTVEDDLIIFPDDCEFKRVPQCPSGRVYVLKFKAGSKRLFFWMQEPKTDQDEEHCRKVNECLNNPPMPGSLGASGSSGHELSALGGEGGLQSLLGNMSHSQLMQLIGPAGLGGLGGLGALTGPGLASLLGSSGPPASSSSSSSRSQSAAVTPSSSTSSARATPAPSAPAAASATSPSPAPSSGNGTSTAASPTQPIQLSDLQSILATMNVPAGPGGSQQVDLASVLTPEIMAPILANADVQERLLPYLPSGESLPQTADEIQNTLTSPQFQQALGMFSAALASGQLGPLMCQFGLPAEAVEAANKGDVEAFAKAMQNNAKSDPKEGDTKDKKDEEEDMSLD |
| Enzyme Length | 407 |
| Uniprot Accession Number | Q9JKV1 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins (PubMed:18497827). This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required (PubMed:18497827). Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair (PubMed:18497827). Within the complex, functions as a proteasomal ubiquitin receptor (PubMed:18497827). Engages and thus activates 19S-associated deubiquitinases UCHL5 and PSMD14 during protein degradation (By similarity). UCHL5 reversibly associate with the 19S regulatory particle whereas PSMD14 is an intrinsic subunit of the proteasome lid subcomplex (By similarity). {ECO:0000250|UniProtKB:Q16186, ECO:0000269|PubMed:18497827}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (9); Chain (1); Compositional bias (2); Cross-link (1); Domain (2); Helix (1); Initiator methionine (1); Modified residue (6); Region (3); Sequence conflict (4); Turn (2) |
| Keywords | 3D-structure;Acetylation;Cytoplasm;Isopeptide bond;Nucleus;Phosphoprotein;Proteasome;Reference proteome;Ubl conjugation |
| Interact With | Q99460-1 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15819879}. Nucleus {ECO:0000250|UniProtKB:Q16186}. |
| Modified Residue | MOD_RES 2; /note=N-acetylthreonine; /evidence=ECO:0000250|UniProtKB:Q16186; MOD_RES 15; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q16186; MOD_RES 140; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q16186; MOD_RES 211; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q16186; MOD_RES 217; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q16186; MOD_RES 405; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9JMB5 |
| Post Translational Modification | PTM: Not N-glycosylated. {ECO:0000269|PubMed:15819879}.; PTM: Not O-glycosylated. {ECO:0000269|PubMed:15819879}.; PTM: Ubiquitinated by UBE3C in response to proteotoxic stress. {ECO:0000250|UniProtKB:Q16186}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (1); X-ray crystallography (1) |
| Cross Reference PDB | 2R2Y; 2Z59; |
| Mapped Pubmed ID | 10725249; 11217851; 12466851; 14610273; 18497817; 19818731; 20498273; 20634424; 21048919; 21267068; 23706739; 26222436; |
| Motif | |
| Gene Encoded By | |
| Mass | 42,060 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |