Detail Information for IndEnz0002014542
IED ID IndEnz0002014542
Enzyme Type ID protease014542
Protein Name Proteasomal ubiquitin receptor ADRM1
110 kDa cell membrane glycoprotein
Gp110
Adhesion-regulating molecule 1
ARM-1
Proteasome regulatory particle non-ATPase 13
hRpn13
Rpn13 homolog
Gene Name ADRM1 GP110
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 MTTSGALFPSLVPGSRGASNKYLVEFRAGKMSLKGTTVTPDKRKGLVYIQQTDDSLIHFCWKDRTSGNVEDDLIIFPDDCEFKRVPQCPSGRVYVLKFKAGSKRLFFWMQEPKTDQDEEHCRKVNEYLNNPPMPGALGASGSSGHELSALGGEGGLQSLLGNMSHSQLMQLIGPAGLGGLGGLGALTGPGLASLLGSSGPPGSSSSSSSRSQSAAVTPSSTTSSTRATPAPSAPAAASATSPSPAPSSGNGASTAASPTQPIQLSDLQSILATMNVPAGPAGGQQVDLASVLTPEIMAPILANADVQERLLPYLPSGESLPQTADEIQNTLTSPQFQQALGMFSAALASGQLGPLMCQFGLPAEAVEAANKGDVEAFAKAMQNNAKPEQKEGDTKDKKDEEEDMSLD
Enzyme Length 407
Uniprot Accession Number Q16186
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:16815440, PubMed:16906146, PubMed:16990800, PubMed:17139257, PubMed:18497817, PubMed:24752541, PubMed:25702870, PubMed:25702872). 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:16815440, PubMed:16906146, PubMed:16990800, PubMed:17139257, PubMed:18497817, PubMed:24752541, PubMed:25702870, PubMed:25702872). Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair (PubMed:16815440, PubMed:16906146, PubMed:16990800, PubMed:17139257, PubMed:18497817, PubMed:24752541, PubMed:25702870, PubMed:25702872). Within the complex, functions as a proteasomal ubiquitin receptor (PubMed:18497817). Engages and activates 19S-associated deubiquitinases UCHL5 and PSMD14 during protein degradation (PubMed:16906146, PubMed:16990800, PubMed:17139257, PubMed:24752541). UCHL5 reversibly associate with the 19S regulatory particle whereas PSMD14 is an intrinsic subunit of the proteasome lid subcomplex (PubMed:16906146, PubMed:16990800, PubMed:17139257, PubMed:24752541). {ECO:0000269|PubMed:16815440, ECO:0000269|PubMed:16906146, ECO:0000269|PubMed:16990800, ECO:0000269|PubMed:17139257, ECO:0000269|PubMed:18497817, ECO:0000269|PubMed:24752541, ECO:0000269|PubMed:25702870, ECO:0000269|PubMed:25702872}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (16); Chain (1); Compositional bias (2); Cross-link (1); Domain (2); Helix (14); Initiator methionine (1); Modified residue (7); Region (3); Sequence conflict (1); Turn (4)
Keywords 3D-structure;Acetylation;Cytoplasm;Isopeptide bond;Nucleus;Phosphoprotein;Proteasome;Reference proteome;Ubl conjugation
Interact With Q99460; Q13200; P55036; P54727; P0CG48; Q9UMX0; Q9UHD9; Q9Y5K5; Q9Y5K5-3; P48510; O35593
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16990800}. Nucleus {ECO:0000269|PubMed:16990800}.
Modified Residue MOD_RES 2; /note="N-acetylthreonine"; /evidence="ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"; MOD_RES 15; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 127; /note="Phosphotyrosine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 140; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 211; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648"; MOD_RES 217; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"; MOD_RES 405; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9JMB5"
Post Translational Modification PTM: Ubiquitinated by UBE3C in response to proteotoxic stress. {ECO:0000269|PubMed:24811749, ECO:0000269|PubMed:31375563}.
Signal Peptide
Structure 3D NMR spectroscopy (9); X-ray crystallography (8)
Cross Reference PDB 2KQZ; 2KR0; 2L5V; 2MKZ; 2NBV; 4UEL; 4UEM; 4WLQ; 4WLR; 5IRS; 5V1Y; 5V1Z; 5YMY; 6CO4; 6OI4; 6UYI; 6UYJ;
Mapped Pubmed ID 11566882; 15819879; 16713569; 17353931; 18497827; 18615678; 18922472; 19148532; 19490896; 19615732; 19818731; 20029029; 20059542; 20137344; 20417181; 20634424; 20959455; 21191146; 21432940; 21516116; 21911578; 22057889; 22576803; 23416715; 24429290; 24910440; 24947832; 24968865; 25036637; 25416956; 25609649; 25666615; 26169395; 26496610; 26903513; 26907685; 27827410; 28442575; 28598414; 28784174; 29913454; 30962947; 31064842; 31669266; 32160516; 32278016; 32424294; 32916039; 33441535; 34916494;
Motif
Gene Encoded By
Mass 42,153
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda