Detailed entry information

Protein Information (annotations from UniProt)

Database IDHIV0002425
UniProt IDP54727
Primary gene name(s)RAD23B
Synonym gene name(s)unknown
Protein nameUV excision repair protein RAD23 homolog B
Protein functionMultiubiquitin 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.; FUNCTION: 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.; FUNCTION: 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.
Subcellular locationNucleus. Cytoplasm. Note=The intracellular distribution is cell cycle dependent. Localized to the nucleus and the cytoplasm during G1 phase. Nuclear levels decrease during S-phase;
upon entering mitosis, relocalizes in the cytoplasm without association with chromatin.
ECO codeClick here for more information.
Amino acid sequence
FASTA format: P54727
Gene Ontology
(Biological Process)
Complete annatation
embryonic organ development [GO:0048568];
global genome nucleotide-excision repair [GO:0070911];
nucleotide-excision repair [GO:0006289];
nucleotide-excision repair, DNA damage recognition [GO:0000715];
nucleotide-excision repair, DNA duplex unwinding [GO:0000717];
nucleotide-excision repair, preincision complex assembly [GO:0006294];
proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161];
regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032434];
spermatogenesis [GO:0007283]
Gene Ontology
(Molecular Function)
Complete annatation
damaged DNA binding [GO:0003684];
polyubiquitin binding [GO:0031593];
single-stranded DNA binding [GO:0003697]
Gene Ontology
(Cellular Component)
Complete annatation
cytoplasm [GO:0005737];
nucleoplasm [GO:0005654];
nucleus [GO:0005634];
proteasome complex [GO:0000502];
XPC complex [GO:0071942]
Protein-protein interaction111824
Phylogenetic treeP54727
HIV replication factor status Zhou et al., Cell. Host. Microbe., 2008
Brass et al., Science, 2008
Smith et al., J. Immunol, 2010
gene status
Lu et al., J. Virol., 2011
      Folds changes 8h: unknown; Folds changes 16h: unknown; Tested: unknown;
Schoggins JW and Rice CM, Curr. Opin. Virol., 2011
      Targeted viruses: unknown
      Viral life cycle: unknown
      Mechanism related to antiviral activity: unknown
Anti-viral restriction factor Liu et al., Retrovirology, 2011
      unknown (Triplicates)

Gene Expression Profile       top

            Up-regulated;            Down-regulated

For brief introduction to each study, please go to the help page.

Gene expression during HIV latency

(1). Mohammadi et al., PLoS Pathog., 2014

Differentially expressed transcripts (Pairwise) during latency and subsequent viral reactivation using several agents - Primary CD4+ T-cell based model

DMSO: Dimethyl suloxyde (negative control) - 0.0033% final
SAHA: Vorinostat (Histone deacetylase inhibitor) - 0.5 μM
CD3: TCR Stimulation by IL-2+ antiCD3/anti-CD28 antibodies
IL7: Interleukin-7 based stimulation
DISU: Disulfiram (alcohol dehydrogenase inhibitor) - 0.5 μM
AZA: 5-azacytidine (AZA; DNA methylation inhibitor) - 1 μM
Experimental Condition Log2 Fold Change P value Adjusted P value
AZA vs. CD31.56284998833163.18547340816266e-062.21149033661113e-05
AZA vs. DISU0.2314818267520.3599968719320150.893849883358823
AZA vs. IL70.2250328909052340.2419786585792510.993092391402121
AZA vs. SAHA-0.06931205524739480.7762105813233230.941353350035522
DISU vs. CD3-1.344063257475330.0002666268136187750.00133260364339835
DISU vs. IL7-0.01520813209979560.9518046136042310.991495507719781
DISU vs. SAHA-0.3001535249359370.3030627809126330.687451442937339
DMSO vs. AZA-0.0952287256818720.569921179342141
DMSO vs. CD3-1.669227860038793.68765129765691e-072.86806746511107e-06
DMSO vs. DISU-0.328688750284380.1779889555676160.690311335740057
DMSO vs. IL70.3275649021726540.06869545421616440.501008211083057
DMSO vs. SAHA0.01813226381264160.9386783341807190.985064509878897
HIV vs. Mock in Activation-0.05368176811088440.9311426805033010.999983755607037
HIV vs. Mock in Latency0.08056820888028890.6254202831816110.999834320637052
IL7 vs. CD3-1.328902645918754.68387186893793e-050.000300340353487958
SAHA vs. CD3-1.658216320040564.98335835308339e-063.40277346538136e-05
SAHA vs. IL7-0.2986338661535770.2205051109660830.459927223288051
(2). Iglesias-Ussel et al., J. Virol., 2013

Up and Downregulated transcripts during Latency (Latently infected CD4+ T cells vs Uninfected)- Primary CD4+Tcell based model
Log2 Fold Change P Value
unknown unknown

Gene expression during HIV infection and replication

(1). Imbeault et al., PloS Pathog., 2012

Transcriptomic profiling of HIV-1 infected CD4+ T cells - Primary CD4+ T cells
Experiment type Log2 Fold Change P Value Adjusted P Value
Infected vs. Mock unknown unknown unknown
Infected vs. Bystander unknown unknown unknown
(2). Lefebvre et al., J. Virol., 2011

Transcriptome analysis of T-cell line (Sup T1)
Log2 Fold Change unknown
(3). Li et al., J. Immunol., 2013

Lymphatic tissue
Acute Fold Change Acute P Value Asymt Fold Change Asypt P Value AIDS Fold Change AIDS P Value
unknown unknown unknown unknown unknown unknown
(4). Chang et al., MBio., 2011

Transcriptome analysis of T-cell line (Sup T1)

Derived from Sherrill-Mix et al., BMC Retrovirol., 2015 cross validation
Up-regulated (True) FALSE
(5). Sherrill-Mix et al., BMC Retrovirol., 2015

Deep RNA-seq analysis of primary human T cell infected with low passage HIV isolate HIV89.6 - Primary CD4+ T cell based
Test Status Log2 Fold Change P Value
OK 0.0805154 0.6294
(6). Rotger et al., PLoS Pathog., 2010

Genome-wide mRNA expression of CD4+ T cells from HIV-infected patient
(Genes differentially expressed (at adjusted p<0.01) according to the empirical Bayes approach)
Log2 Fold Change P Value
unknown unknown

Proteomic/Transcriptomics studies indicating differentially expressed genes mediated by HIV

(1). Greenwood et al., Elife, 2016

Activated (CD3/CD28) Primary human CD4+ T cells infected with pNL4-3-dE-EGFP. The table shows the complete (unfiltered) TMT (tandem mass tag)-based proteomic time course dataset
6 h 24 h 48 h 72 h RTi
1.01 0.943 1.04 0.986 0.936
(2). Navare et al., Virology, 2012

SUP-T1 cell line
FC-4hpi P-value FC-8hpi P-value FC-20hpi P-value Category
unknown unknown unknown unknown unknown unknown unknown
(3). Hyrcza et al., J. Virolo., 2007

Primary human CD4+ and CD8+ T Cells
Affymetrix Prob ID Fold Change In CD8? Category
unknown unknown unknown unknown

Protein Overview       top

Drug-protein Interaction       (annotations from DrugBank)      top

not found

Protein Secondary Structure       (annotations from PDB)      top

PDB Accession Method Resolution Chain Structure Preview
1P1A NMR - A=1-82.
1PVE NMR - A=275-342.
1UEL NMR - A=1-87.

HIV-1 Interaction       (annotations from NCBI HIV-1 Interaction Database)      top

HIV Partner Interaction Type PubMed
HIV-1 virus replication enhanced by expression of human gene 20174665

Metabolic/Signalling Pathway       (annotations from KEGG database)      top

Pathway Accession Number Description
hsa03420 Nucleotide excision repair - Homo sapiens (human)
hsa04141 Protein processing in endoplasmic reticulum - Homo sapiens (human)