P54725 · RD23A_HUMAN
- ProteinUV excision repair protein RAD23 homolog A
- GeneRAD23A
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids363 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
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.
(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.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameUV excision repair protein RAD23 homolog A
- Short namesHR23A; hHR23A
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP54725
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 8 | No effect on interaction with EEF1A1. | ||||
Sequence: K → A | ||||||
Mutagenesis | 9 | Abolishes interaction with PSMD4; when associated with T-49. | ||||
Sequence: T → A | ||||||
Mutagenesis | 10 | Impairs UBL-UBA domain interaction and enhances ubiquitin-binding; when associated with Glu-47. | ||||
Sequence: L → E | ||||||
Mutagenesis | 47 | No effect on UBL-UBA domain interaction. | ||||
Sequence: K → A | ||||||
Mutagenesis | 47 | Impairs UBL-UBA domain interaction and enhances ubiquitin-binding; when associated with Glu-10. | ||||
Sequence: K → E | ||||||
Mutagenesis | 47 | Impairs UBL-UBA domain interaction and enhances ubiquitin-binding; when associated with Glu-77. | ||||
Sequence: K → E | ||||||
Mutagenesis | 49 | Impairs interaction with PSMD4. | ||||
Sequence: I → A | ||||||
Mutagenesis | 49 | Abolishes interaction with PSMD4; when associated with A-9. | ||||
Sequence: I → T | ||||||
Mutagenesis | 54 | Impairs interaction with PSMD4. | ||||
Sequence: I → A | ||||||
Mutagenesis | 71 | Impairs interaction with PSMD4. | ||||
Sequence: F → A | ||||||
Mutagenesis | 77 | Impairs UBL-UBA domain interaction and enhances ubiquitin-binding; when associated with Glu-47. | ||||
Sequence: T → E | ||||||
Mutagenesis | 77 | No effect on interaction with PSMD4. | ||||
Sequence: T → S | ||||||
Mutagenesis | 79 | Increases interaction with PSMD1 and PSMC1. | ||||
Sequence: T → P | ||||||
Natural variant | VAR_016251 | 131 | in dbSNP:rs11558955 | |||
Sequence: T → A | ||||||
Natural variant | VAR_020377 | 179 | in dbSNP:rs4987203 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_016252 | 200 | in dbSNP:rs4987202 | |||
Sequence: T → M | ||||||
Mutagenesis | 333 | Abolishes interaction with HIV-1 vpr. | ||||
Sequence: P → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 346 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), cross-link, modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000114904 | 1-363 | UniProt | UV excision repair protein RAD23 homolog A | |||
Sequence: MAVTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIRDYRIDEKNFVVVMVTKTKAGQGTSAPPEASPTAAPESSTSFPPAPTSGMSHPPPAAREDKSPSEESAPTTSPESVSGSVPSSGSSGREEDAASTLVTGSEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLTGIPGSPEPEHGSVQESQVSEQPATEAAGENPLEFLRDQPQFQNMRQVIQQNPALLPALLQQLGQENPQLLQQISRHQEQFIQMLNEPPGELADISDVEGEVGAIGEEAPQMNYIQVTPQEKEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQNFDDE | |||||||
Modified residue (large scale data) | 92 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 122 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue | 123 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 123 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 125 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 128 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 128 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 131 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 132 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 133 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 133 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 136 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 136 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 138 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 140 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 205 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 295 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 357 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 357 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
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
Interacts with UBQLN2
(Microbial infection) Interacts with HIV-1 Vpr.
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-81 | Ubiquitin-like | ||||
Sequence: MAVTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIRDYRIDEKNFVVVMVTKTKA | ||||||
Compositional bias | 81-107 | Polar residues | ||||
Sequence: AGQGTSAPPEASPTAAPESSTSFPPAP | ||||||
Region | 81-160 | Disordered | ||||
Sequence: AGQGTSAPPEASPTAAPESSTSFPPAPTSGMSHPPPAAREDKSPSEESAPTTSPESVSGSVPSSGSSGREEDAASTLVTG | ||||||
Compositional bias | 127-160 | Polar residues | ||||
Sequence: ESAPTTSPESVSGSVPSSGSSGREEDAASTLVTG | ||||||
Domain | 161-201 | UBA 1 | ||||
Sequence: SEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLTG | ||||||
Region | 203-227 | Disordered | ||||
Sequence: PGSPEPEHGSVQESQVSEQPATEAA | ||||||
Compositional bias | 210-224 | Polar residues | ||||
Sequence: HGSVQESQVSEQPAT | ||||||
Domain | 318-358 | UBA 2 | ||||
Sequence: PQEKEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQ | ||||||
Region | 319-363 | HIV-1 vpr binding | ||||
Sequence: QEKEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQNFDDE |
Domain
The ubiquitin-like domain mediates interaction with ATXN3.
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.
Sequence similarities
Belongs to the RAD23 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P54725-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length363
- Mass (Da)39,609
- Last updated1996-10-01 v1
- ChecksumC4E47E9313BB47B5
P54725-2
- Name2
- Differences from canonical
- 272-326: Missing
P54725-3
- Name3
- Differences from canonical
- 226-226: Missing
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A494C0B4 | A0A494C0B4_HUMAN | RAD23A | 282 | ||
K7ELU6 | K7ELU6_HUMAN | RAD23A | 62 | ||
K7ELW1 | K7ELW1_HUMAN | RAD23A | 142 | ||
K7ENJ0 | K7ENJ0_HUMAN | RAD23A | 139 | ||
K7EQ16 | K7EQ16_HUMAN | RAD23A | 150 |
Sequence caution
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 81-107 | Polar residues | ||||
Sequence: AGQGTSAPPEASPTAAPESSTSFPPAP | ||||||
Compositional bias | 127-160 | Polar residues | ||||
Sequence: ESAPTTSPESVSGSVPSSGSSGREEDAASTLVTG | ||||||
Compositional bias | 210-224 | Polar residues | ||||
Sequence: HGSVQESQVSEQPAT | ||||||
Alternative sequence | VSP_054694 | 226 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_047565 | 272-326 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D21235 EMBL· GenBank· DDBJ | BAA04767.1 EMBL· GenBank· DDBJ | mRNA | ||
AF549209 EMBL· GenBank· DDBJ | AAN39383.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BX448989 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
AB209713 EMBL· GenBank· DDBJ | BAD92950.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC092069 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AD000092 EMBL· GenBank· DDBJ | AAB51177.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC014026 EMBL· GenBank· DDBJ | AAH14026.1 EMBL· GenBank· DDBJ | mRNA | ||
BC088364 EMBL· GenBank· DDBJ | AAH88364.1 EMBL· GenBank· DDBJ | mRNA |