Detailed entry information

Protein Information (annotations from UniProt)

Database IDHIV0002531
UniProt IDP15927
Primary gene name(s)RPA2
Synonym gene name(s)REPA2, RPA32, RPA34
Protein nameReplication protein A 32 kDa subunit
Protein functionAs part of the heterotrimeric replication protein A complex, RPA/RP-A, binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair, BER probably through interaction with UNG. Through RFWD3 may activate CHEK1 and play a role in replication checkpoint control. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. {ECO:0000269|PubMed:15205463, ECO:0000269|PubMed:17765923, ECO:0000269|PubMed:17959650, ECO:0000269|PubMed:19116208, ECO:0000269|PubMed:20154705, ECO:0000269|PubMed:21504906, ECO:0000269|PubMed:2406247, ECO:0000269|PubMed:24332808, ECO:0000269|PubMed:7697716, ECO:0000269|PubMed:7700386, ECO:0000269|PubMed:8702565, ECO:0000269|PubMed:9430682, ECO:0000269|PubMed:9765279}.
Subcellular locationNucleus {ECO:0000269|PubMed:10982866, ECO:0000269|PubMed:12814551, ECO:0000269|PubMed:20154705, ECO:0000269|PubMed:21504906}. Nucleus, PML body {ECO:0000269|PubMed:12814551}. Note=Redistributes to discrete nuclear foci upon DNA damage in an ATR-dependent manner. {ECO:0000269|PubMed:12814551}.
ECO codeClick here for more information.
Amino acid sequence
FASTA format: P15927
Gene Ontology
(Biological Process)
Complete annatation
base-excision repair [GO:0006284];
DNA damage response, detection of DNA damage [GO:0042769];
DNA replication [GO:0006260];
double-strand break repair via homologous recombination [GO:0000724];
error-free translesion synthesis [GO:0070987];
error-prone translesion synthesis [GO:0042276];
G1/S transition of mitotic cell cycle [GO:0000082];
interstrand cross-link repair [GO:0036297];
mismatch repair [GO:0006298];
mitotic G1 DNA damage checkpoint [GO:0031571];
nucleotide-excision repair [GO:0006289];
nucleotide-excision repair, DNA gap filling [GO:0006297];
nucleotide-excision repair, DNA incision [GO:0033683];
nucleotide-excision repair, DNA incision, 3'-to lesion [GO:0006295];
nucleotide-excision repair, DNA incision, 5'-to lesion [GO:0006296];
nucleotide-excision repair, preincision complex assembly [GO:0006294];
nucleotide-excision repair, preincision complex stabilization [GO:0006293];
regulation of cellular response to heat [GO:1900034];
regulation of DNA damage checkpoint [GO:2000001];
regulation of double-strand break repair via homologous recombination [GO:0010569];
regulation of signal transduction by p53 class mediator [GO:1901796];
telomere maintenance [GO:0000723];
telomere maintenance via recombination [GO:0000722];
transcription-coupled nucleotide-excision repair [GO:0006283];
translesion synthesis [GO:0019985]
Gene Ontology
(Molecular Function)
Complete annatation
damaged DNA binding [GO:0003684];
enzyme binding [GO:0019899];
protein phosphatase binding [GO:0019903];
single-stranded DNA binding [GO:0003697];
ubiquitin protein ligase binding [GO:0031625]
Gene Ontology
(Cellular Component)
Complete annatation
chromatin [GO:0000785];
DNA replication factor A complex [GO:0005662];
nuclear chromosome, telomeric region [GO:0000784];
nucleoplasm [GO:0005654];
nucleus [GO:0005634];
PML body [GO:0016605]
Protein-protein interaction112038
Phylogenetic treeP15927
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. CD30.7723667356482350.02016320774539840.0469126068444959
AZA vs. DISU-0.03820542743907630.8799066530683850.991771899371402
AZA vs. IL70.07540811372047880.6948451075411620.999311006273513
AZA vs. SAHA-0.3993796621883920.1022160164718960.404571990674691
DISU vs. CD3-0.8232782116208310.02598423615535730.0636371041114306
DISU vs. IL70.1040405761683550.6796849044479120.913457246550082
DISU vs. SAHA-0.3588909059980970.2191535462102520.594023031531609
DMSO vs. AZA-0.03181656933610510.8493958830017531
DMSO vs. CD3-0.8150805581879970.01214832864282640.0294235644701255
DMSO vs. DISU0.004687697114145770.9846640586397920.997438150413502
DMSO vs. IL70.1143319556760560.5248914546434050.892975060233746
DMSO vs. SAHA-0.3733022292259390.1139223877398590.4012640059523
HIV vs. Mock in Activation-0.1481767999801940.8115605180439620.999983755607037
HIV vs. Mock in Latency0.08197405227158670.6198238263241040.999834320637052
IL7 vs. CD3-0.690396941223660.03354366007325520.0795724879263731
SAHA vs. CD3-1.195237508036280.0009030115108349390.00328229220170828
SAHA vs. IL7-0.4769703887919040.05058436188499180.185751198795217
(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 0.0279289 0.891302
(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
1.018 0.975 1.082 1.058 0.998
(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
1DPU NMR - A=172-270.
1L1O X-ray 2.8Å B/E=44-171.
1QUQ X-ray 2.5Å A/C=43-171.
1Z1D NMR - A=172-270.
2PI2 X-ray 2.0Å A/B/C/D=1-270.
2PQA X-ray 2.5Å A/C=42-172.
2Z6K X-ray 3.0Å A/B=1-270.
3KDF X-ray 1.9Å B/D=41-172.
4MQV X-ray 1.9Å A/C=202-270.
4OU0 X-ray 1.4Å A=202-270.

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

HIV Partner Interaction Type PubMed
Vpr co-localizes with 20824083
Vpr induces phosphorylation of 16956949
Vif inhibited by 18596088
reverse transcriptase inhibited by 9084803
HIV-1 virus replication enhanced by expression of human gene 22171270

Metabolic/Signalling Pathway       (annotations from KEGG database)      top

Pathway Accession Number Description
hsa03030 DNA replication - Homo sapiens (human)
hsa03420 Nucleotide excision repair - Homo sapiens (human)
hsa03430 Mismatch repair - Homo sapiens (human)
hsa03440 Homologous recombination - Homo sapiens (human)
hsa03460 Fanconi anemia pathway - Homo sapiens (human)