ID:RD23A_HUMAN DESCRIPTION: RecName: Full=UV excision repair protein RAD23 homolog A; Short=HR23A; Short=hHR23A; 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: 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. SUBUNIT: Interacts with XPC; the interaction is suggesting the existence of a functional equivalent variant XPC complex. Interacts with PSMD4 and PSMC5. Interacts with ATXN3. Interacts with HIV-1 vpr. Interacts with UBQLN2. INTERACTION: P55036:PSMD4; NbExp=2; IntAct=EBI-746453, EBI-359318; Q13501:SQSTM1; NbExp=2; IntAct=EBI-746453, EBI-307104; Q9UHD9:UBQLN2; NbExp=3; IntAct=EBI-746453, EBI-947187; SUBCELLULAR LOCATION: Nucleus. DOMAIN: The ubiquitin-like domain mediates interaction with ATXN3. DOMAIN: The ubiquitin-like (UBL) and the UBA (ubiquitin- associated) domains interact intramolecularly in a highly dynamic manner, as each UBA domain competes for an overlapping UBL domain surface. Binding of ubiquitin or proteasome subunit PSMD4 disrupt the UBL-UBA domain interactions and drive RAD23A in to an open conformation. PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. SIMILARITY: Belongs to the RAD23 family. SIMILARITY: Contains 2 UBA domains. SIMILARITY: Contains 1 ubiquitin-like domain. WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/rad23a/";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P54725
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0006281 DNA repair GO:0006289 nucleotide-excision repair GO:0006974 cellular response to DNA damage stimulus GO:0016032 viral process GO:0016579 protein deubiquitination GO:0031648 protein destabilization GO:0032434 regulation of proteasomal ubiquitin-dependent protein catabolic process GO:0032436 positive regulation of proteasomal ubiquitin-dependent protein catabolic process GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process GO:0045070 positive regulation of viral genome replication GO:0045787 positive regulation of cell cycle
US Server
Sequence and Links to Tools and Databases 
Common Gene Haplotype Alleles 
