| IED ID | IndEnz0002013848 |
| Enzyme Type ID | protease013848 |
| Protein Name |
UV excision repair protein RAD23 homolog A HR23A hHR23A |
| Gene Name | RAD23A |
| 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 | MAVTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIRDYRIDEKNFVVVMVTKTKAGQGTSAPPEASPTAAPESSTSFPPAPTSGMSHPPPAAREDKSPSEESAPTTSPESVSGSVPSSGSSGREEDAASTLVTGSEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLTGIPGSPEPEHGSVQESQVSEQPATEAAGENPLEFLRDQPQFQNMRQVIQQNPALLPALLQQLGQENPQLLQQISRHQEQFIQMLNEPPGELADISDVEGEVGAIGEEAPQMNYIQVTPQEKEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQNFDDE |
| Enzyme Length | 363 |
| Uniprot Accession Number | P54725 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to 'Lys-48'-linked polyubiquitin chains in a length-dependent manner and with a lower affinity to 'Lys-63'-linked polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome.; FUNCTION: Involved in nucleotide excision repair and is thought to be functional equivalent for RAD23B in global genome nucleotide excision repair (GG-NER) by association with XPC. In vitro, the XPC:RAD23A dimer has NER activity. Can stabilize XPC.; FUNCTION: (Microbial infection) Involved in Vpr-dependent replication of HIV-1 in non-proliferating cells and primary macrophages. Required for the association of HIV-1 Vpr with the host proteasome. {ECO:0000269|PubMed:20614012}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Beta strand (12); Chain (1); Compositional bias (3); Cross-link (1); Domain (3); Erroneous initiation (1); Frameshift (1); Helix (13); Modified residue (8); Mutagenesis (14); Natural variant (3); Region (3); Turn (8) |
| Keywords | 3D-structure;Alternative splicing;DNA damage;DNA repair;Host-virus interaction;Isopeptide bond;Nucleus;Phosphoprotein;Proteasome;Reference proteome;Repeat;Ubl conjugation |
| Interact With | Q6AI12; Q9NP61; P54253; P54252; Q4VBR4; Q8N137; P48730-2; Q15038; P68104; P26378-2; B7ZLH0; P42858; P06756; P59991; Q9H8M7; Q9UHC7; Q15843; Q96IV0; Q8TBJ4; Q07869; Q13200; P55036; Q9UJ41-4; Q04864-2; Q6NTF9-3; Q9H4P4; P62979; Q16586; Q8NCS7; Q13501; O43463; P21580; Q12933; Q13114; Q9Y228; O00463; Q9Y4K3; Q9HCM9-2; Q86XT4; Q9BYV2; Q9BYV6-2; Q9BZR9; Q15654; P62987; Q9UHD9; Q04323-2; Q96RL1-2; Q9UHP3; P25490; Q9HCK0; Q8NCP5; Q96BR9; Q6FIF0; Q9JI78 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus. |
| Modified Residue | MOD_RES 123; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"; MOD_RES 128; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 133; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"; MOD_RES 136; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 138; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P54726"; MOD_RES 205; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569"; MOD_RES 295; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569"; MOD_RES 357; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (9); X-ray crystallography (5) |
| Cross Reference PDB | 1DV0; 1F4I; 1IFY; 1OQY; 1P98; 1P9D; 1QZE; 1TP4; 2WYQ; 5XBO; 6W2G; 6W2H; 6W2I; 6XQI; |
| Mapped Pubmed ID | 10391953; 10526214; 10734143; 11007478; 11141066; 11278856; 11279143; 11511374; 11788722; 12080057; 12732143; 12815074; 12944386; 14517266; 14645509; 14742321; 15220921; 15811629; 15882621; 15964821; 16030353; 16105547; 16189514; 16223728; 16430867; 16473935; 16491090; 16678110; 16713569; 16924240; 16990800; 17353931; 17408689; 17466626; 17882165; 18614043; 18654987; 19056823; 19109893; 19161404; 19609301; 19615732; 19661379; 19713942; 19724136; 19913121; 19941824; 20368362; 20496165; 20522537; 20628086; 20711500; 20855601; 20876134; 21047872; 21135142; 21163940; 21388382; 21900206; 21911578; 22081108; 22118460; 22575648; 23038248; 23045548; 23319653; 23352696; 23357418; 23751493; 24318982; 24811749; 25154395; 25260751; 25277244; 25311859; 25416956; 26042670; 26151477; 26296656; 27613096; 27771451; 28365903; 31487504; 32209475; 34824204; 8692841; 9130708; 9771713; |
| Motif | |
| Gene Encoded By | |
| Mass | 39,609 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |