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RPA2 (replication protein A2, 32kDa)

Written2010-04Anar KZ Murphy, James A Borowiec
Dept of Biochemistry, New York University Cancer Institute, New York University School of Medicine, New York, New York 10016, USA

(Note : for Links provided by Atlas : click)

Identity

Alias_namesreplication protein A2 (32kD)
replication protein A2, 32kDa
Other aliasREPA2
RPA32
HGNC (Hugo) RPA2
LocusID (NCBI) 6118
Atlas_Id 42146
Location 1p35.3  [Link to chromosome band 1p35]
Location_base_pair Starts at 27891526 and ends at 27914797 bp from pter ( according to hg19-Feb_2009)  [Mapping RPA2.png]
Local_order The human RPA2 gene maps on 1p35.3 between the SMPDL3B (sphingomyelin phosphodiesterase, acid-like 3B) and C1orf38 (interferon-gamma inducible gene ICB-1 (induced by contact to basement membrane)).
Fusion genes
(updated 2016)
RPA2 (1p35.3) / EPB41 (1p35.3)RPA2 (1p35.3) / HN1L (16p13.3)RPA2 (1p35.3) / SERPING1 (11q12.1)
TOM1L1 (17q22) / RPA2 (1p35.3)

DNA/RNA

 
  The sequence numbering corresponds to EMBL locus DQ001128 (26.6 kb). Exon are indicated as boxes (yellow = 5' UTR, blue = CDS, red = 3' UTR), and introns with orange lines. Two lengthy introns have been truncated (indicated with parallel diagonal lines) to improve viewability.
Description The RPA2 gene is contained within 24.5 kb of chromosome 1. The coding sequence is contained within nine exons. There is no confirmed alternative splicing of the RPA2 gene, or differential promoter usage.
Transcription The RPA2 mRNA transcript is 1.5 kb. The RPA2 promoter contains four E2F consensus sequences within the region about 400 bp upstream of the mRNA start site, and putative binding sites for ATF-1 and SP-1 transcription factors. Expression is upregulated 2 to 3-fold by E2F, with mutation of the three start site-proximal E2F sites causing a loss of E2F responsiveness (Kalma et al., 2001).
Pseudogene RPA2 does not have known pseudogenes.

Protein

 
  Upper panel: Schematic showing the key domains of RPA2. Lower panel: RPA2 phosphorylation sites are shown in bold, with the primary responsible kinases indicated above each site. Some sites can be phosphorylated by more than one kinase (e.g., T21 by ATM and DNA-PK).
Description RPA2 is the middle subunit of the heterotrimeric Replication Protein A (RPA; (reviewed in Binz et al., 2004)). The subunit is composed of 270 residues, and has a nominal molecular weight of 29.2 kDa. RPA2 contains an N-terminal phosphorylation region with 7 phosphorylation sites, a central DNA-binding domain (termed DBD-D), and a C-terminal region that can form a three-helix bundle. One helix of the three helix bundle is contributed by each RPA subunit, with this structure responsible for supporting heterotrimerization of the RPA complex (Bochkareva et al., 2002). At least in the non-phosphorylated state, the N-terminal region is unstructured. DBD-D is constructed from an oligonucleotide/oligosaccharide binding (OB) fold (Bochkarev et al., 1999), one of six OB folds found with the RPA heterotrimer (four OB folds are located in RPA1, and one within RPA3).
Expression RPA is an essential factor for DNA replication and repair, and hence is expressed in all tissues.
Localisation Nuclear.
Function General function: RPA is a heterotrimeric single-stranded DNA (ssDNA) binding protein that is essential for chromosomal DNA replication, homologous recombination, and particular DNA repair reactions (nucleotide excision repair). The apparent association constant of the RPA: ssDNA complex is 109 - 1011 M-1 (Kim et al., 1992). While RPA2 contains a central DBD (Philipova et al., 1996), the major effect of mutating DBD-D is to decrease the size of the ssDNA occluded by RPA binding, with only minor effects on RPA: ssDNA affinity (Bastin-Shanower and Brill, 2001). A key function of the RPA2 subunit is to regulate RPA activity in DNA replication and repair reactions, through the RPA2 phosphorylation state (see below).

1) RPA2 phosphorylation. The N-terminal 33 residues of RPA2 contain seven phosphorylation sites. In interphase cells, genotoxic stress (e.g., caused by chromosomal double-strand DNA breaks or DNA replication stress) induces RPA2 phosphorylation by members of the phosphatidylinositol 3-kinase-like kinase (PIKK; ATM, ATR, and DNA-PK) and cyclin-dependent kinases (CDK) families (reviewed in Binz et al., 2004). Mutation of particular RPA2 phosphorylation sites causes defects in homologous recombination (Lee et al., 2010), and Rad51 recruitment to nuclear repair foci (Anantha et al., 2008; Lee et al., 2010). Mutation of these sites also causes genomic instability in response to DNA replication stress induced by cellular treatment with hydroxyurea (Vassin et al., 2009). RPA phosphorylation also increases cell viability in response to DNA damage arising during mitosis (Anantha et al., 2008). Modification of sites in the phosphorylation region of RPA2 proceeds in a favored order in response to genotoxic stress (Anantha et al., 2007). The phosphorylation of individual RPA2 residues is dependent on the type of DNA damage or replication stress encountered (Anantha et al., 2007; Vassin et al., 2009). RPA2 is a substrate both for PP2A and PP4 phosphatases (Feng et al., 2009; Lee et al., 2010).

2) Involvement of RPA2 in protein-protein interactions. RPA2 interacts with the nucleotide excision repair factor XPA (He et al., 1995), base excision repair enzyme UNG2 (Mer et al., 2000), homologous recombination (HR) factor Rad52 (Mer et al., 2000), replication checkpoint protein Tipin (Unsal-Kacmaz et al., 2007), and the annealing helicase HARP/SMARCAL1 (Bansbach et al., 2009; Ciccia et al., 2009; Yuan et al., 2009). These interactions likely aid the multiple roles of RPA in facilitating DNA repair.

Homology A close homolog of RPA2, termed RPA4, is located on Xq21.33 (Haring et al., 2010).

Mutations

Note Naturally-occurring mutations of human RPA2 have not yet been described. A small number of genetic polymorphisms have been described in SNP datasets (Y14S, G15R, and N203S), but these have not yet been reported to have any biological effects (NIEHS SNPs program).

Implicated in

Note
  
Entity Colorectal adenocarcinoma
Disease Overexpression of the RPA2 (and RPA1) proteins have been found to be prognostic indicator of colon cancer. Strong associations between RPA2 expression and disease stage, lymph node metastasis, and the histological grade of carcinomas have been observed.
Prognosis In addition, RPA2 protein expression correlates with poor survival of stage II and III patients (Givalos et al., 2007).
  
  
Entity Ductal breast carcinoma
Disease Levels of anti-RPA2 antibodies was observed to be significantly higher in sera from breast cancer patients (10.9%; n = 801) as compared to normal controls (0.0%; n = 221). Examining individuals with early stage intraductal in situ carcinomas, 10.3% (n = 39) similarly showed the presence of high levels of anti-RPA2 antibodies. Even so, follow-up studies indicated that there were no apparent differences in mean survival, occurrences of a second primary tumor, or metastasis frequency between breast cancer patients that were positive or negative for anti-RPA2 sera. Although RPA is a nuclear protein, RPA was seen to be localized to both nuclei and cytoplasm in the cells of at least one breast tumor, with RPA also over-expressed (Tomkiel et al., 2002).
  
  
Entity Non-small cell carcinoma
Disease A fraction of individuals with squamous cell lung cancer were found to have significant levels of anti-RPA2 antibodies (9.1%; n = 22) (Tomkiel et al., 2002).
  
  
Entity Laryngeal tumors
Disease One patient (out of 35; 2.9%) with head and neck tumors tested positive for the presence of anti-RPA2 sera (Tomkiel et al., 2002).
  
  
Entity Promyelocytic leukemia
Disease A derivative of the human HL-60 promyelocytic leukemia cell line (HL-60/P1), selected for its decreased sensitivity to undergo apoptosis in response to TNF-related apoptosis-inducing ligand (TRAIL), was found to have decreased (2-fold) expression of RPA2 (Petrak et al., 2009).
  
  
Entity Sjögren syndrome
Disease Serum from a patient with Sjögren syndrome was found to have high levels of anti-RPA2 antibodies. A higher rate of non-Hodgkin lymphoma, and lymphoid malignancies, is seen in individuals with Sjögren syndrome, compared to normal individuals (Garcia-Lozano et al., 1995).
  
  
Entity Systemic lupus erythematosus (SLE)
Disease One out of 55 individuals with autoimmune disorders was found to test positive for anti-RPA2 antibodies (1.8%). This individual had SLE, and secondary Sjögren syndrome (Garcia-Lozano et al., 1995).
  
  
Entity Rheumatoid arthritis (RA)
Note Fibroblast-like synoviocytes (FLSs) are a cell type whose invasive properties provide an indicator of RA severity. Microarray studies from FLSs in DA rats (arthritis-susceptible inbred model) show a modest increase in the level of RPA2 mRNA, compared to back-crossed arthritis-resistant DA.F344 (Cia5d) congenic strains (Laragione et al., 2008).
  

Bibliography

RPA phosphorylation facilitates mitotic exit in response to mitotic DNA damage.
Anantha RW, Sokolova E, Borowiec JA.
Proc Natl Acad Sci U S A. 2008 Sep 2;105(35):12903-8. Epub 2008 Aug 22.
PMID 18723675
 
The annealing helicase SMARCAL1 maintains genome integrity at stalled replication forks.
Bansbach CE, Betous R, Lovejoy CA, Glick GG, Cortez D.
Genes Dev. 2009 Oct 15;23(20):2405-14. Epub 2009 Sep 30.
PMID 19793861
 
Functional analysis of the four DNA binding domains of replication protein A. The role of RPA2 in ssDNA binding.
Bastin-Shanower SA, Brill SJ.
J Biol Chem. 2001 Sep 28;276(39):36446-53. Epub 2001 Jul 30.
PMID 11479296
 
Replication protein A phosphorylation and the cellular response to DNA damage.
Binz SK, Sheehan AM, Wold MS.
DNA Repair (Amst). 2004 Aug-Sep;3(8-9):1015-24. (REVIEW)
PMID 15279788
 
The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding.
Bochkarev A, Bochkareva E, Frappier L, Edwards AM.
EMBO J. 1999 Aug 16;18(16):4498-504.
PMID 10449415
 
Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA.
Bochkareva E, Korolev S, Lees-Miller SP, Bochkarev A.
EMBO J. 2002 Apr 2;21(7):1855-63.
PMID 11927569
 
The SIOD disorder protein SMARCAL1 is an RPA-interacting protein involved in replication fork restart.
Ciccia A, Bredemeyer AL, Sowa ME, Terret ME, Jallepalli PV, Harper JW, Elledge SJ.
Genes Dev. 2009 Oct 15;23(20):2415-25. Epub 2009 Sep 30.
PMID 19793862
 
Protein phosphatase 2A-dependent dephosphorylation of replication protein A is required for the repair of DNA breaks induced by replication stress.
Feng J, Wakeman T, Yong S, Wu X, Kornbluth S, Wang XF.
Mol Cell Biol. 2009 Nov;29(21):5696-709. Epub 2009 Aug 24.
PMID 19704001
 
Presence of antibodies to different subunits of replication protein A in autoimmune sera.
Garcia-Lozano R, Gonzalez-Escribano F, Sanchez-Roman J, Wichmann I, Nunez-Roldan A.
Proc Natl Acad Sci U S A. 1995 May 23;92(11):5116-20.
PMID 7761458
 
Replication protein A is an independent prognostic indicator with potential therapeutic implications in colon cancer.
Givalos N, Gakiopoulou H, Skliri M, Bousboukea K, Konstantinidou AE, Korkolopoulou P, Lelouda M, Kouraklis G, Patsouris E, Karatzas G.
Mod Pathol. 2007 Feb;20(2):159-66.
PMID 17361204
 
A naturally occurring human RPA subunit homolog does not support DNA replication or cell-cycle progression.
Haring SJ, Humphreys TD, Wold MS.
Nucleic Acids Res. 2010 Jan 1;38(3):846-58. Epub 2009 Nov 26.
PMID 19942684
 
RPA involvement in the damage-recognition and incision steps of nucleotide excision repair.
He Z, Henricksen LA, Wold MS, Ingles CJ.
Nature. 1995 Apr 6;374(6522):566-9.
PMID 7700386
 
Expression analysis using DNA microarrays demonstrates that E2F-1 up-regulates expression of DNA replication genes including replication protein A2.
Kalma Y, Marash L, Lamed Y, Ginsberg D.
Oncogene. 2001 Mar 15;20(11):1379-87.
PMID 11313881
 
Binding properties of replication protein A from human and yeast cells.
Kim C, Snyder RO, Wold MS.
Mol Cell Biol. 1992 Jul;12(7):3050-9.
PMID 1320195
 
Cia5d regulates a new fibroblast-like synoviocyte invasion-associated gene expression signature.
Laragione T, Brenner M, Li W, Gulko PS.
Arthritis Res Ther. 2008;10(4):R92. Epub 2008 Aug 15.
PMID 18706093
 
A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombination.
Lee DH, Pan Y, Kanner S, Sung P, Borowiec JA, Chowdhury D.
Nat Struct Mol Biol. 2010 Mar;17(3):365-72. Epub 2010 Feb 14.
PMID 20154705
 
Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA.
Mer G, Bochkarev A, Gupta R, Bochkareva E, Frappier L, Ingles CJ, Edwards AM, Chazin WJ.
Cell. 2000 Oct 27;103(3):449-56.
PMID 11081631
 
Identification of molecular targets for selective elimination of TRAIL-resistant leukemia cells. From spots to in vitro assays using TOP15 charts.
Petrak J, Toman O, Simonova T, Halada P, Cmejla R, Klener P, Zivny J.
Proteomics. 2009 Nov;9(22):5006-15.
PMID 19834905
 
A hierarchy of SSB protomers in replication protein A.
Philipova D, Mullen JR, Maniar HS, Lu J, Gu C, Brill SJ.
Genes Dev. 1996 Sep 1;10(17):2222-33.
PMID 8804316
 
Autoimmunity to the M(r) 32,000 subunit of replication protein A in breast cancer.
Tomkiel JE, Alansari H, Tang N, Virgin JB, Yang X, VandeVord P, Karvonen RL, Granda JL, Kraut MJ, Ensley JF, Fernandez-Madrid F.
Clin Cancer Res. 2002 Mar;8(3):752-8.
PMID 11895905
 
The human Tim/Tipin complex coordinates an Intra-S checkpoint response to UV that slows replication fork displacement.
Unsal-Kacmaz K, Chastain PD, Qu PP, Minoo P, Cordeiro-Stone M, Sancar A, Kaufmann WK.
Mol Cell Biol. 2007 Apr;27(8):3131-42. Epub 2007 Feb 12.
PMID 17296725
 
Human RPA phosphorylation by ATR stimulates DNA synthesis and prevents ssDNA accumulation during DNA-replication stress.
Vassin VM, Anantha RW, Sokolova E, Kanner S, Borowiec JA.
J Cell Sci. 2009 Nov 15;122(Pt 22):4070-80. Epub 2009 Oct 20.
PMID 19843584
 
The annealing helicase HARP protects stalled replication forks.
Yuan J, Ghosal G, Chen J.
Genes Dev. 2009 Oct 15;23(20):2394-9. Epub 2009 Sep 30.
PMID 19793864
 

Citation

This paper should be referenced as such :
Murphy, AKZ ; Borowiec, JA
RPA2 (replication protein A2, 32kDa)
Atlas Genet Cytogenet Oncol Haematol. 2011;15(1):55-58.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/RPA2ID42146ch1p35.html


External links

Nomenclature
HGNC (Hugo)RPA2   10290
Cards
AtlasRPA2ID42146ch1p35
Entrez_Gene (NCBI)RPA2  6118  replication protein A2
AliasesREPA2; RP-A; RP-A; RPA32
GeneCards (Weizmann)RPA2
Ensembl hg19 (Hinxton)ENSG00000117748 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000117748 [Gene_View]  chr1:27891526-27914797 [Contig_View]  RPA2 [Vega]
ICGC DataPortalENSG00000117748
TCGA cBioPortalRPA2
AceView (NCBI)RPA2
Genatlas (Paris)RPA2
WikiGenes6118
SOURCE (Princeton)RPA2
Genetics Home Reference (NIH)RPA2
Genomic and cartography
GoldenPath hg38 (UCSC)RPA2  -     chr1:27891526-27914797 -  1p35.3   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)RPA2  -     1p35.3   [Description]    (hg19-Feb_2009)
EnsemblRPA2 - 1p35.3 [CytoView hg19]  RPA2 - 1p35.3 [CytoView hg38]
Mapping of homologs : NCBIRPA2 [Mapview hg19]  RPA2 [Mapview hg38]
OMIM179836   
Gene and transcription
Genbank (Entrez)AK298759 AK300691 AK312956 BC001630 BC012157
RefSeq transcript (Entrez)NM_001286076 NM_001297558 NM_002946
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)RPA2
Cluster EST : UnigeneHs.79411 [ NCBI ]
CGAP (NCI)Hs.79411
Alternative Splicing GalleryENSG00000117748
Gene ExpressionRPA2 [ NCBI-GEO ]   RPA2 [ EBI - ARRAY_EXPRESS ]   RPA2 [ SEEK ]   RPA2 [ MEM ]
Gene Expression Viewer (FireBrowse)RPA2 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)6118
GTEX Portal (Tissue expression)RPA2
Protein : pattern, domain, 3D structure
UniProt/SwissProtP15927   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP15927  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP15927
Splice isoforms : SwissVarP15927
PhosPhoSitePlusP15927
Domains : Interpro (EBI)NA-bd_OB-fold    Rfa2/RPA32    RPA_C    WHTH_DNA-bd_dom   
Domain families : Pfam (Sanger)RPA_C (PF08784)   
Domain families : Pfam (NCBI)pfam08784   
Conserved Domain (NCBI)RPA2
DMDM Disease mutations6118
Blocks (Seattle)RPA2
PDB (SRS)1DPU    1L1O    1QUQ    1Z1D    2PI2    2PQA    2Z6K    3KDF    4MQV    4OU0   
PDB (PDBSum)1DPU    1L1O    1QUQ    1Z1D    2PI2    2PQA    2Z6K    3KDF    4MQV    4OU0   
PDB (IMB)1DPU    1L1O    1QUQ    1Z1D    2PI2    2PQA    2Z6K    3KDF    4MQV    4OU0   
PDB (RSDB)1DPU    1L1O    1QUQ    1Z1D    2PI2    2PQA    2Z6K    3KDF    4MQV    4OU0   
Structural Biology KnowledgeBase1DPU    1L1O    1QUQ    1Z1D    2PI2    2PQA    2Z6K    3KDF    4MQV    4OU0   
SCOP (Structural Classification of Proteins)1DPU    1L1O    1QUQ    1Z1D    2PI2    2PQA    2Z6K    3KDF    4MQV    4OU0   
CATH (Classification of proteins structures)1DPU    1L1O    1QUQ    1Z1D    2PI2    2PQA    2Z6K    3KDF    4MQV    4OU0   
SuperfamilyP15927
Human Protein AtlasENSG00000117748
Peptide AtlasP15927
HPRD01566
IPIIPI00013939   IPI00647667   IPI00646500   IPI00642145   IPI00646957   
Protein Interaction databases
DIP (DOE-UCLA)P15927
IntAct (EBI)P15927
FunCoupENSG00000117748
BioGRIDRPA2
STRING (EMBL)RPA2
ZODIACRPA2
Ontologies - Pathways
QuickGOP15927
Ontology : AmiGOG1/S transition of mitotic cell cycle  telomere maintenance via recombination  telomere maintenance  telomere maintenance  double-strand break repair via homologous recombination  chromosome, telomeric region  nuclear chromosome, telomeric region  chromatin  damaged DNA binding  single-stranded DNA binding  single-stranded DNA binding  single-stranded DNA binding  protein binding  nucleus  nucleoplasm  nucleoplasm  DNA replication factor A complex  DNA replication factor A complex  DNA replication  DNA replication  DNA replication  transcription-coupled nucleotide-excision repair  base-excision repair  nucleotide-excision repair  nucleotide-excision repair, preincision complex stabilization  nucleotide-excision repair, preincision complex assembly  nucleotide-excision repair, DNA incision, 3'-to lesion  nucleotide-excision repair, DNA incision, 5'-to lesion  nucleotide-excision repair, DNA gap filling  mismatch repair  mismatch repair  regulation of double-strand break repair via homologous recombination  nuclear body  PML body  PML body  enzyme binding  protein phosphatase binding  translesion synthesis  mitotic G1 DNA damage checkpoint  ubiquitin protein ligase binding  nucleotide-excision repair, DNA incision  protein localization to chromosome  site of double-strand break  interstrand cross-link repair  error-prone translesion synthesis  DNA damage response, detection of DNA damage  protein N-terminus binding  error-free translesion synthesis  G-rich strand telomeric DNA binding  regulation of cellular response to heat  regulation of signal transduction by p53 class mediator  regulation of DNA damage checkpoint  
Ontology : EGO-EBIG1/S transition of mitotic cell cycle  telomere maintenance via recombination  telomere maintenance  telomere maintenance  double-strand break repair via homologous recombination  chromosome, telomeric region  nuclear chromosome, telomeric region  chromatin  damaged DNA binding  single-stranded DNA binding  single-stranded DNA binding  single-stranded DNA binding  protein binding  nucleus  nucleoplasm  nucleoplasm  DNA replication factor A complex  DNA replication factor A complex  DNA replication  DNA replication  DNA replication  transcription-coupled nucleotide-excision repair  base-excision repair  nucleotide-excision repair  nucleotide-excision repair, preincision complex stabilization  nucleotide-excision repair, preincision complex assembly  nucleotide-excision repair, DNA incision, 3'-to lesion  nucleotide-excision repair, DNA incision, 5'-to lesion  nucleotide-excision repair, DNA gap filling  mismatch repair  mismatch repair  regulation of double-strand break repair via homologous recombination  nuclear body  PML body  PML body  enzyme binding  protein phosphatase binding  translesion synthesis  mitotic G1 DNA damage checkpoint  ubiquitin protein ligase binding  nucleotide-excision repair, DNA incision  protein localization to chromosome  site of double-strand break  interstrand cross-link repair  error-prone translesion synthesis  DNA damage response, detection of DNA damage  protein N-terminus binding  error-free translesion synthesis  G-rich strand telomeric DNA binding  regulation of cellular response to heat  regulation of signal transduction by p53 class mediator  regulation of DNA damage checkpoint  
Pathways : KEGGDNA replication    Nucleotide excision repair    Mismatch repair    Homologous recombination    Fanconi anemia pathway   
REACTOMEP15927 [protein]
REACTOME PathwaysR-HSA-912446 [pathway]   
NDEx NetworkRPA2
Atlas of Cancer Signalling NetworkRPA2
Wikipedia pathwaysRPA2
Orthology - Evolution
OrthoDB6118
GeneTree (enSembl)ENSG00000117748
Phylogenetic Trees/Animal Genes : TreeFamRPA2
HOVERGENP15927
HOGENOMP15927
Homologs : HomoloGeneRPA2
Homology/Alignments : Family Browser (UCSC)RPA2
Gene fusions - Rearrangements
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerRPA2 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)RPA2
dbVarRPA2
ClinVarRPA2
1000_GenomesRPA2 
Exome Variant ServerRPA2
ExAC (Exome Aggregation Consortium)RPA2 (select the gene name)
Genetic variants : HAPMAP6118
Genomic Variants (DGV)RPA2 [DGVbeta]
DECIPHERRPA2 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisRPA2 
Mutations
ICGC Data PortalRPA2 
TCGA Data PortalRPA2 
Broad Tumor PortalRPA2
OASIS PortalRPA2 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICRPA2  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDRPA2
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch RPA2
DgiDB (Drug Gene Interaction Database)RPA2
DoCM (Curated mutations)RPA2 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)RPA2 (select a term)
intoGenRPA2
NCG5 (London)RPA2
Cancer3DRPA2(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM179836   
Orphanet
MedgenRPA2
Genetic Testing Registry RPA2
NextProtP15927 [Medical]
TSGene6118
GENETestsRPA2
Target ValidationRPA2
Huge Navigator RPA2 [HugePedia]
snp3D : Map Gene to Disease6118
BioCentury BCIQRPA2
ClinGenRPA2
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD6118
Chemical/Pharm GKB GenePA34652
Clinical trialRPA2
Miscellaneous
canSAR (ICR)RPA2 (select the gene name)
Other databaseNIEHS SNPs program
Probes
Litterature
PubMed141 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineRPA2
EVEXRPA2
GoPubMedRPA2
iHOPRPA2
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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