Detail Information for IndEnz0002013849
IED ID IndEnz0002013849
Enzyme Type ID protease013849
Protein Name UV excision repair protein RAD23 homolog A
HR23A
mHR23A
Gene Name Rad23a Mhr23a
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 MAVTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIKEYHIDEKNFVVVMVTKAKAGQGIPAPPEASPTAVPEPSTPFPPVLASGMSHPPPTSREDKSPSEESTTTTSPESISGSVPSSGSSGREEDAASTLVTGSEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLTGIPGSPEPEHGSVQESQAPEQPATEAAGENPLEFLRDQPQFQNMRQVIQQNPALLPALLQQLGQENPQLLQQISRHQEQFIQMLNEPPGELADISDVEGEVGAIGEEAPQMNYIQVTPQEKEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQNFDDE
Enzyme Length 363
Uniprot Accession Number P54726
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 (By similarity). {ECO:0000250}.; 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. Reported differences to Rad23b in regard to NER activity and Xpc stabilization are probably due to differences in expression levels with Rad23a being much less expressed than Rad23b. {ECO:0000269|PubMed:12815074, ECO:0000269|PubMed:15336624}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Compositional bias (2); Cross-link (1); Domain (3); Modified residue (8); Region (2); Sequence conflict (3)
Keywords DNA damage;DNA repair;Isopeptide bond;Nucleus;Phosphoprotein;Proteasome;Reference proteome;Repeat;Ubl conjugation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
Modified Residue MOD_RES 123; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"; MOD_RES 128; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P54725"; MOD_RES 133; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 136; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 138; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 205; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P54725"; MOD_RES 295; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P54725"; MOD_RES 357; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17525332"
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11217851; 12466851; 14610273; 16141072; 17662948; 18369441; 21677750; 21706023; 22431748; 25217174; 26998601; 8858346;
Motif
Gene Encoded By
Mass 39,706
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda