UniProt functional annotation for P54725



	UniProt functional annotation for P54725

UniProt code: P54725.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

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}.

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 (PubMed:30455355). Interacts with UBQLN2. {ECO:0000269|PubMed:10488153, ECO:0000269|PubMed:10915768, ECO:0000269|PubMed:12970176, ECO:0000269|PubMed:14557549, ECO:0000269|PubMed:16712842, ECO:0000269|PubMed:17098253, ECO:0000269|PubMed:30455355}.

Subunit: (Microbial infection) Interacts with HIV-1 Vpr. {ECO:0000269|PubMed:11087358, ECO:0000269|PubMed:9371639}.

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.

Similarity: Belongs to the RAD23 family. {ECO:0000305}.

Sequence caution: Sequence=BAD92950.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; Sequence=BX448989; Type=Frameshift; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



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}.


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 (PubMed:30455355). Interacts with UBQLN2. {ECO:0000269\|PubMed:10488153, ECO:0000269\|PubMed:10915768, ECO:0000269\|PubMed:12970176, ECO:0000269\|PubMed:14557549, ECO:0000269\|PubMed:16712842, ECO:0000269\|PubMed:17098253, ECO:0000269\|PubMed:30455355}.
Subunit:		(Microbial infection) Interacts with HIV-1 Vpr. {ECO:0000269\|PubMed:11087358, ECO:0000269\|PubMed:9371639}.
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.
Similarity:		Belongs to the RAD23 family. {ECO:0000305}.
Sequence caution:		Sequence=BAD92950.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; Sequence=BX448989; Type=Frameshift; Evidence={ECO:0000305};