P54727 · RD23B_HUMAN
- ProteinUV excision repair protein RAD23 homolog B
- GeneRAD23B
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids409 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to 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. May play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome.
Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with CETN2 appears to stabilize XPC. May protect XPC from proteasomal degradation.
The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | proteasome complex | |
Cellular Component | XPC complex | |
Molecular Function | damaged DNA binding | |
Molecular Function | DNA damage sensor activity | |
Molecular Function | polyubiquitin modification-dependent protein binding | |
Molecular Function | proteasome binding | |
Molecular Function | RNA polymerase II cis-regulatory region sequence-specific DNA binding | |
Molecular Function | RNA polymerase II-specific DNA-binding transcription factor binding | |
Molecular Function | single-stranded DNA binding | |
Molecular Function | ubiquitin binding | |
Biological Process | cellular response to interleukin-7 | |
Biological Process | embryonic organ development | |
Biological Process | nucleotide-excision repair | |
Biological Process | proteasome-mediated ubiquitin-dependent protein catabolic process | |
Biological Process | regulation of proteasomal ubiquitin-dependent protein catabolic process | |
Biological Process | spermatogenesis |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameUV excision repair protein RAD23 homolog B
- Short namesHR23B; hHR23B
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP54727
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 6 | Impairs interaction with EEF1A1. | ||||
Sequence: K → A | ||||||
Natural variant | VAR_014350 | 249 | in dbSNP:rs1805329 | |||
Sequence: A → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 355 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, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000114906 | 1-409 | UniProt | UV excision repair protein RAD23 homolog B | |||
Sequence: MQVTLKTLQQQTFKIDIDPEETVKALKEKIESEKGKDAFPVAGQKLIYAGKILNDDTALKEYKIDEKNFVVVMVTKPKAVSTPAPATTQQSAPASTTAVTSSTTTTVAQAPTPVPALAPTSTPASITPASATASSEPAPASAAKQEKPAEKPAETPVATSPTATDSTSGDSSRSNLFEDATSALVTGQSYENMVTEIMSMGYEREQVIAALRASFNNPDRAVEYLLMGIPGDRESQAVVDPPQAASTGAPQSSAVAAAAATTTATTTTTSSGGHPLEFLRNQPQFQQMRQIIQQNPSLLPALLQQIGRENPQLLQQISQHQEHFIQMLNEPVQEAGGQGGGGGGGSGGIAEAGSGHMNYIQVTPQEKEAIERLKALGFPEGLVIQAYFACEKNENLAANFLLQQNFDED | |||||||
Modified residue | 155 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 155 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 159 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 160 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 160 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 162 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 164 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 166 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 168 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 171 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 174 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 186 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 199 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 202 | UniProt | Phosphotyrosine | ||||
Sequence: Y |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Interaction
Subunit
Component of the XPC complex composed of XPC, RAD23B and CETN2. Interacts with NGLY1 and PSMC1. Interacts with ATXN3 (PubMed:30455355).
Interacts with PSMD4 and PSMC5. Interacts with AMFR. Interacts with VCP; the interaction is indirect and mediated by NGLY1 (By similarity).
Interacts with PSMD4 and PSMC5. Interacts with AMFR. Interacts with VCP; the interaction is indirect and mediated by NGLY1 (By similarity).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-79 | Ubiquitin-like | ||||
Sequence: MQVTLKTLQQQTFKIDIDPEETVKALKEKIESEKGKDAFPVAGQKLIYAGKILNDDTALKEYKIDEKNFVVVMVTKPKA | ||||||
Region | 80-175 | Disordered | ||||
Sequence: VSTPAPATTQQSAPASTTAVTSSTTTTVAQAPTPVPALAPTSTPASITPASATASSEPAPASAAKQEKPAEKPAETPVATSPTATDSTSGDSSRSN | ||||||
Compositional bias | 81-111 | Polar residues | ||||
Sequence: STPAPATTQQSAPASTTAVTSSTTTTVAQAP | ||||||
Compositional bias | 119-139 | Polar residues | ||||
Sequence: PTSTPASITPASATASSEPAP | ||||||
Compositional bias | 157-175 | Polar residues | ||||
Sequence: VATSPTATDSTSGDSSRSN | ||||||
Domain | 188-228 | UBA 1 | ||||
Sequence: QSYENMVTEIMSMGYEREQVIAALRASFNNPDRAVEYLLMG | ||||||
Region | 236-276 | Disordered | ||||
Sequence: QAVVDPPQAASTGAPQSSAVAAAAATTTATTTTTSSGGHPL | ||||||
Compositional bias | 240-276 | Polar residues | ||||
Sequence: DPPQAASTGAPQSSAVAAAAATTTATTTTTSSGGHPL | ||||||
Domain | 274-317 | STI1 | ||||
Sequence: HPLEFLRNQPQFQQMRQIIQQNPSLLPALLQQIGRENPQLLQQI | ||||||
Domain | 364-404 | UBA 2 | ||||
Sequence: PQEKEAIERLKALGFPEGLVIQAYFACEKNENLAANFLLQQ |
Domain
The ubiquitin-like domain mediates interaction with ATXN3.
Sequence similarities
Belongs to the RAD23 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P54727-1
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
- Length409
- Mass (Da)43,171
- Last updated1996-10-01 v1
- ChecksumC026C78273BCB289
P54727-2
- Name2
- NoteHighly expressed in the testis and in ejaculated spermatozoa.
- Differences from canonical
- 1-72: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_045606 | 1-72 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 81-111 | Polar residues | ||||
Sequence: STPAPATTQQSAPASTTAVTSSTTTTVAQAP | ||||||
Compositional bias | 119-139 | Polar residues | ||||
Sequence: PTSTPASITPASATASSEPAP | ||||||
Compositional bias | 157-175 | Polar residues | ||||
Sequence: VATSPTATDSTSGDSSRSN | ||||||
Compositional bias | 240-276 | Polar residues | ||||
Sequence: DPPQAASTGAPQSSAVAAAAATTTATTTTTSSGGHPL |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D21090 EMBL· GenBank· DDBJ | BAA04652.1 EMBL· GenBank· DDBJ | mRNA | ||
AY313777 EMBL· GenBank· DDBJ | AAP81008.1 EMBL· GenBank· DDBJ | mRNA | ||
AY165178 EMBL· GenBank· DDBJ | AAN47194.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK125226 EMBL· GenBank· DDBJ | BAG54170.1 EMBL· GenBank· DDBJ | mRNA | ||
AL137852 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471105 EMBL· GenBank· DDBJ | EAW59016.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471105 EMBL· GenBank· DDBJ | EAW59017.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC020973 EMBL· GenBank· DDBJ | AAH20973.1 EMBL· GenBank· DDBJ | mRNA |