RPA2 | ENSG00000117748 | NCBI 6118

Details for: RPA2

Gene ID: 6118

Symbol: RPA2

Ensembl ID: ENSG00000117748

Description: replication protein A2

Associated with

Activation of atr in response to replication stress
(R-HSA-176187)
Activation of the pre-replicative complex
(R-HSA-68962)
Base excision repair
(R-HSA-73884)
Cell cycle
(R-HSA-1640170)
Cell cycle, mitotic
(R-HSA-69278)
Cell cycle checkpoints
(R-HSA-69620)
Cellular responses to stimuli
(R-HSA-8953897)
Cellular responses to stress
(R-HSA-2262752)
Cellular response to heat stress
(R-HSA-3371556)
Chromosome maintenance
(R-HSA-73886)
Defective homologous recombination repair (hrr) due to brca2 loss of function
(R-HSA-9701190)
Disease
(R-HSA-1643685)
Diseases of dna double-strand break repair
(R-HSA-9675136)
Diseases of dna repair
(R-HSA-9675135)
Dna damage bypass
(R-HSA-73893)
Dna double-strand break repair
(R-HSA-5693532)
Dna repair
(R-HSA-73894)
Dna replication pre-initiation
(R-HSA-69002)
Dna strand elongation
(R-HSA-69190)
Dual incision in gg-ner
(R-HSA-5696400)
Dual incision in tc-ner
(R-HSA-6782135)
Extension of telomeres
(R-HSA-180786)
Fanconi anemia pathway
(R-HSA-6783310)
Formation of incision complex in gg-ner
(R-HSA-5696395)
G1/s transition
(R-HSA-69206)
G2/m checkpoints
(R-HSA-69481)
G2/m dna damage checkpoint
(R-HSA-69473)
Gap-filling dna repair synthesis and ligation in gg-ner
(R-HSA-5696397)
Gap-filling dna repair synthesis and ligation in tc-ner
(R-HSA-6782210)
Gene expression (transcription)
(R-HSA-74160)
Generic transcription pathway
(R-HSA-212436)
Global genome nucleotide excision repair (gg-ner)
(R-HSA-5696399)
Hdr through homologous recombination (hrr)
(R-HSA-5685942)
Hdr through homologous recombination (hrr) or single strand annealing (ssa)
(R-HSA-5693567)
Hdr through single strand annealing (ssa)
(R-HSA-5685938)
Homologous dna pairing and strand exchange
(R-HSA-5693579)
Homology directed repair
(R-HSA-5693538)
Hsf1 activation
(R-HSA-3371511)
Impaired brca2 binding to rad51
(R-HSA-9709570)
Lagging strand synthesis
(R-HSA-69186)
Meiosis
(R-HSA-1500620)
Meiotic recombination
(R-HSA-912446)
Mismatch repair (mmr) directed by msh2:msh3 (mutsbeta)
(R-HSA-5358606)
Mismatch repair (mmr) directed by msh2:msh6 (mutsalpha)
(R-HSA-5358565)
Mitotic g1 phase and g1/s transition
(R-HSA-453279)
Nucleotide excision repair
(R-HSA-5696398)
Pcna-dependent long patch base excision repair
(R-HSA-5651801)
Presynaptic phase of homologous dna pairing and strand exchange
(R-HSA-5693616)
Processing of dna double-strand break ends
(R-HSA-5693607)
Processive synthesis on the c-strand of the telomere
(R-HSA-174414)
Processive synthesis on the lagging strand
(R-HSA-69183)
Recognition of dna damage by pcna-containing replication complex
(R-HSA-110314)
Regulation of hsf1-mediated heat shock response
(R-HSA-3371453)
Regulation of tp53 activity
(R-HSA-5633007)
Regulation of tp53 activity through phosphorylation
(R-HSA-6804756)
Removal of the flap intermediate
(R-HSA-69166)
Removal of the flap intermediate from the c-strand
(R-HSA-174437)
Reproduction
(R-HSA-1474165)
Resolution of abasic sites (ap sites)
(R-HSA-73933)
Resolution of ap sites via the multiple-nucleotide patch replacement pathway
(R-HSA-110373)
Rna polymerase ii transcription
(R-HSA-73857)
S phase
(R-HSA-69242)
Synthesis of dna
(R-HSA-69239)
Telomere c-strand (lagging strand) synthesis
(R-HSA-174417)
Termination of translesion dna synthesis
(R-HSA-5656169)
Transcription-coupled nucleotide excision repair (tc-ner)
(R-HSA-6781827)
Transcriptional regulation by tp53
(R-HSA-3700989)
Translesion synthesis by polh
(R-HSA-110320)
Translesion synthesis by poli
(R-HSA-5656121)
Translesion synthesis by polk
(R-HSA-5655862)
Translesion synthesis by rev1
(R-HSA-110312)
Translesion synthesis by y family dna polymerases bypasses lesions on dna template
(R-HSA-110313)
Base-excision repair
(GO:0006284)
Damaged dna binding
(GO:0003684)
Dna replication
(GO:0006260)
Double-strand break repair via homologous recombination
(GO:0000724)
Enzyme binding
(GO:0019899)
G-rich strand telomeric dna binding
(GO:0098505)
Mismatch repair
(GO:0006298)
Mitotic g1 dna damage checkpoint signaling
(GO:0031571)
Nucleotide-excision repair
(GO:0006289)
Protein binding
(GO:0005515)
Protein localization to chromosome
(GO:0034502)
Protein phosphatase binding
(GO:0019903)
Regulation of dna damage checkpoint
(GO:2000001)
Regulation of double-strand break repair via homologous recombination
(GO:0010569)
Single-stranded dna binding
(GO:0003697)
Telomere maintenance
(GO:0000723)
Telomeric dna binding
(GO:0042162)
Ubiquitin protein ligase binding
(GO:0031625)

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 69.5794
Cell Significance Index: -32.8500
Cell Name: mucosal type mast cell (CL0000485)
Fold Change: 67.5188
Cell Significance Index: -27.4300
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 61.5298
Cell Significance Index: -31.6500
Cell Name: ileal goblet cell (CL1000326)
Fold Change: 48.9999
Cell Significance Index: -32.8800
Cell Name: ciliated cell of the bronchus (CL0002332)
Fold Change: 28.7302
Cell Significance Index: -27.4300
Cell Name: epithelial cell of pancreas (CL0000083)
Fold Change: 13.7384
Cell Significance Index: 226.3900
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 8.5009
Cell Significance Index: -26.1100
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 5.9951
Cell Significance Index: -16.0600
Cell Name: epidermal Langerhans cell (CL0002457)
Fold Change: 4.1122
Cell Significance Index: -9.0000
Cell Name: germ cell (CL0000586)
Fold Change: 2.3382
Cell Significance Index: 17.6600
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: 1.4079
Cell Significance Index: 97.3700
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 1.2056
Cell Significance Index: 1088.5800
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: 1.1641
Cell Significance Index: 135.6700
Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
Fold Change: 1.1444
Cell Significance Index: 33.6100
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: 1.1262
Cell Significance Index: 23.9900
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 0.8922
Cell Significance Index: 145.1100
Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
Fold Change: 0.8662
Cell Significance Index: 30.1000
Cell Name: early pro-B cell (CL0002046)
Fold Change: 0.8036
Cell Significance Index: 51.8500
Cell Name: colon goblet cell (CL0009039)
Fold Change: 0.6698
Cell Significance Index: 66.2600
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 0.6653
Cell Significance Index: 78.4600
Cell Name: abnormal cell (CL0001061)
Fold Change: 0.6346
Cell Significance Index: 64.8300
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 0.5668
Cell Significance Index: 69.6900
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 0.5641
Cell Significance Index: 101.6900
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 0.5330
Cell Significance Index: 73.2000
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 0.4834
Cell Significance Index: 213.7300
Cell Name: odontoblast (CL0000060)
Fold Change: 0.4712
Cell Significance Index: 60.4100
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: 0.4681
Cell Significance Index: 29.5100
Cell Name: granulosa cell (CL0000501)
Fold Change: 0.4543
Cell Significance Index: 11.9500
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: 0.4416
Cell Significance Index: 6.0300
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 0.4365
Cell Significance Index: 87.5700
Cell Name: neoplastic cell (CL0001063)
Fold Change: 0.4282
Cell Significance Index: 84.9700
Cell Name: glycinergic neuron (CL1001509)
Fold Change: 0.3983
Cell Significance Index: 20.9100
Cell Name: cell in vitro (CL0001034)
Fold Change: 0.3350
Cell Significance Index: 182.9300
Cell Name: sebum secreting cell (CL0000317)
Fold Change: 0.3347
Cell Significance Index: 23.6700
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: 0.2669
Cell Significance Index: 12.5500
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 0.2554
Cell Significance Index: 13.2700
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 0.2448
Cell Significance Index: 87.8200
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: 0.2288
Cell Significance Index: 6.1100
Cell Name: skeletal muscle myoblast (CL0000515)
Fold Change: 0.1573
Cell Significance Index: 1.7100
Cell Name: fibroblast of dermis (CL0002551)
Fold Change: 0.0836
Cell Significance Index: 1.7500
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 0.0751
Cell Significance Index: 3.5000
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.0649
Cell Significance Index: 12.3500
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: 0.0614
Cell Significance Index: 1.3300
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: 0.0566
Cell Significance Index: 9.6600
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: 0.0437
Cell Significance Index: 1.2600
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: 0.0404
Cell Significance Index: 3.0100
Cell Name: mesenchymal cell (CL0008019)
Fold Change: 0.0287
Cell Significance Index: 0.4800
Cell Name: lactocyte (CL0002325)
Fold Change: 0.0209
Cell Significance Index: 2.7100
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.0006
Cell Significance Index: 1.1300
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0096
Cell Significance Index: -6.0200
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: -0.0101
Cell Significance Index: -0.4600
Cell Name: anterior lens cell (CL0002223)
Fold Change: -0.0103
Cell Significance Index: -18.9700
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: -0.0118
Cell Significance Index: -8.6600
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.0123
Cell Significance Index: -3.5400
Cell Name: lens epithelial cell (CL0002224)
Fold Change: -0.0140
Cell Significance Index: -21.5600
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0157
Cell Significance Index: -11.6200
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: -0.0167
Cell Significance Index: -12.6700
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: -0.0184
Cell Significance Index: -11.6900
Cell Name: secondary lens fiber (CL0002225)
Fold Change: -0.0237
Cell Significance Index: -32.2800
Cell Name: pro-T cell (CL0000827)
Fold Change: -0.0317
Cell Significance Index: -0.8100
Cell Name: thyroid follicular cell (CL0002258)
Fold Change: -0.0367
Cell Significance Index: -0.3900
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.0385
Cell Significance Index: -21.6900
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: -0.0459
Cell Significance Index: -20.8200
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: -0.0501
Cell Significance Index: -1.7600
Cell Name: Hofbauer cell (CL3000001)
Fold Change: -0.0552
Cell Significance Index: -0.4500
Cell Name: interstitial cell of ovary (CL0002094)
Fold Change: -0.0582
Cell Significance Index: -0.7500
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: -0.0594
Cell Significance Index: -1.6600
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.0721
Cell Significance Index: -15.1900
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: -0.0769
Cell Significance Index: -4.3200
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: -0.0960
Cell Significance Index: -2.4000
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.1152
Cell Significance Index: -13.2000
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.1327
Cell Significance Index: -19.2900
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -0.1506
Cell Significance Index: -4.8200
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: -0.1590
Cell Significance Index: -9.7700
Cell Name: Sertoli cell (CL0000216)
Fold Change: -0.1797
Cell Significance Index: -2.5200
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: -0.1932
Cell Significance Index: -5.2600
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: -0.2040
Cell Significance Index: -13.7200
Cell Name: basal cell of epidermis (CL0002187)
Fold Change: -0.2074
Cell Significance Index: -3.1500
Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: -0.2264
Cell Significance Index: -25.8400
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: -0.2317
Cell Significance Index: -17.7800
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.3068
Cell Significance Index: -31.9400
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.3080
Cell Significance Index: -24.3900
Cell Name: peg cell (CL4033014)
Fold Change: -0.3367
Cell Significance Index: -7.7800
Cell Name: cerebellar granule cell (CL0001031)
Fold Change: -0.3997
Cell Significance Index: -6.8500
Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: -0.4090
Cell Significance Index: -10.9400
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: -0.4971
Cell Significance Index: -21.9900
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: -0.5111
Cell Significance Index: -14.6500
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: -0.5281
Cell Significance Index: -9.7600
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -0.5332
Cell Significance Index: -32.6900
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: -0.5479
Cell Significance Index: -14.6800
Cell Name: retinal rod cell (CL0000604)
Fold Change: -0.5713
Cell Significance Index: -6.8100
Cell Name: kidney epithelial cell (CL0002518)
Fold Change: -0.5921
Cell Significance Index: -17.4400
Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: -0.6087
Cell Significance Index: -23.0500
Cell Name: hippocampal pyramidal neuron (CL1001571)
Fold Change: -0.6872
Cell Significance Index: -19.6100
Cell Name: melanocyte of skin (CL1000458)
Fold Change: -0.6913
Cell Significance Index: -9.6900
Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: -0.7084
Cell Significance Index: -18.2100
Cell Name: CD4-positive, alpha-beta thymocyte (CL0000810)
Fold Change: -0.7176
Cell Significance Index: -12.3700
Cell Name: stratified epithelial cell (CL0000079)
Fold Change: -0.7205
Cell Significance Index: -26.4500
Cell Name: transit amplifying cell of small intestine (CL0009012)
Fold Change: -0.7303
Cell Significance Index: -15.1500
Cell Name: fibro/adipogenic progenitor cell (CL0009099)
Fold Change: -0.7505
Cell Significance Index: -37.9300

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**Key Characteristics:** RPA2 is a 32-kDa protein that belongs to the RPA complex, which is composed of three subunits: RPA1, RPA2, and RPA3. RPA2 is responsible for binding to single-stranded DNA (ssDNA) and regulating the replication process. It is also involved in the repair of DNA double-strand breaks (DSBs) through homologous recombination (HR) and non-homologous end joining (NHEJ). RPA2 has been shown to interact with various proteins, including BRCA2, PCNA, and TP53, which are involved in DNA repair and cell cycle regulation. Its expression is tightly regulated, and its dysregulation has been linked to various diseases, including cancer. **Pathways and Functions:** RPA2 plays a crucial role in several cellular processes, including: 1. **DNA Replication:** RPA2 binds to ssDNA and regulates the replication process, ensuring accurate and efficient DNA replication. 2. **DNA Repair:** RPA2 is involved in the repair of DNA DSBs through HR and NHEJ, which are essential for maintaining genome stability. 3. **Cell Cycle Regulation:** RPA2 interacts with PCNA and TP53 to regulate the cell cycle, ensuring proper cell division and preventing genomic instability. 4. **Transcriptional Regulation:** RPA2 has been shown to regulate transcriptional activity, particularly in the context of DNA damage response. 5. **Homologous Recombination:** RPA2 is involved in the repair of DNA DSBs through HR, which is essential for maintaining genome stability. **Clinical Significance:** Dysregulation of RPA2 has been implicated in various diseases, including: 1. **Cancer:** RPA2 mutations and overexpression have been linked to various types of cancer, including breast, ovarian, and lung cancer. 2. **Genetic Disorders:** RPA2 mutations have been associated with genetic disorders, such as Fanconi anemia and Bloom syndrome. 3. **DNA Damage Response:** RPA2 plays a crucial role in the DNA damage response, and its dysregulation can lead to genomic instability and tumorigenesis. 4. **Reproductive Health:** RPA2 has been implicated in reproductive health, particularly in the context of oogonial cell development and meiotic recombination. In conclusion, RPA2 is a crucial protein involved in maintaining genome stability and responding to DNA damage. Its dysregulation has been implicated in various diseases, including cancer, genetic disorders, and reproductive health issues. Further research is needed to understand the mechanisms by which RPA2 regulates cellular processes and to develop therapeutic strategies for targeting RPA2 in disease prevention and treatment.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Replication protein A 32 kDa subunit
B4DUL2_HUMAN

Genular Protein ID: 3411609379

Symbol: RFA2_HUMAN

Name: Replication protein A 32 kDa subunit

UniProtKB Accession Codes:

P15927 Q52II0 Q5TEI9 Q5TEJ5

Database IDs:

Citations:

PubMed ID: 2406247

Title: The primary structure of the 32-kDa subunit of human replication protein A.

PubMed ID: 2406247

DOI: 10.1016/s0021-9258(19)39750-9

PubMed ID: 16710414

Title: The DNA sequence and biological annotation of human chromosome 1.

PubMed ID: 16710414

DOI: 10.1038/nature04727

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 2200738

Title: Cell-cycle-regulated phosphorylation of DNA replication factor A from human and yeast cells.

PubMed ID: 2200738

DOI: 10.1101/gad.4.6.968

PubMed ID: 1318195

Title: cdc2 family kinases phosphorylate a human cell DNA replication factor, RPA, and activate DNA replication.

PubMed ID: 1318195

DOI: 10.1002/j.1460-2075.1992.tb05278.x

PubMed ID: 8246944

Title: The ionizing radiation-induced replication protein A phosphorylation response differs between ataxia telangiectasia and normal human cells.

PubMed ID: 8246944

DOI: 10.1128/mcb.13.12.7222-7231.1993

PubMed ID: 7697716

Title: Mammalian DNA nucleotide excision repair reconstituted with purified protein components.

PubMed ID: 7697716

DOI: 10.1016/0092-8674(95)90289-9

PubMed ID: 7700386

Title: RPA involvement in the damage-recognition and incision steps of nucleotide excision repair.

PubMed ID: 7700386

DOI: 10.1038/374566a0

PubMed ID: 8702565

Title: Physical interaction between human RAD52 and RPA is required for homologous recombination in mammalian cells.

PubMed ID: 8702565

DOI: 10.1074/jbc.271.31.18996

PubMed ID: 9139719

Title: Mapping of amino acid residues in the p34 subunit of human single-stranded DNA-binding protein phosphorylated by DNA-dependent protein kinase and Cdc2 kinase in vitro.

PubMed ID: 9139719

DOI: 10.1074/jbc.272.19.12634

PubMed ID: 9295339

Title: Sites of UV-induced phosphorylation of the p34 subunit of replication protein A from HeLa cells.

PubMed ID: 9295339

DOI: 10.1074/jbc.272.38.23896

PubMed ID: 9430682

Title: The evolutionarily conserved zinc finger motif in the largest subunit of human replication protein A is required for DNA replication and mismatch repair but not for nucleotide excision repair.

PubMed ID: 9430682

DOI: 10.1074/jbc.273.3.1453

PubMed ID: 9765279

Title: Replication protein A stimulates long patch DNA base excision repair.

PubMed ID: 9765279

DOI: 10.1074/jbc.273.42.27492

PubMed ID: 10982866

Title: RBT1, a novel transcriptional co-activator, binds the second subunit of replication protein A.

PubMed ID: 10982866

DOI: 10.1093/nar/28.18.3478

PubMed ID: 12814551

Title: ATR kinase activity regulates the intranuclear translocation of ATR and RPA following ionizing radiation.

PubMed ID: 12814551

DOI: 10.1016/s0960-9822(03)00376-2

PubMed ID: 15205463

Title: Coordinated regulation of replication protein A activities by its subunits p14 and p32.

PubMed ID: 15205463

DOI: 10.1074/jbc.m403825200

PubMed ID: 17596542

Title: FANCJ (BACH1) helicase forms DNA damage inducible foci with replication protein A and interacts physically and functionally with the single-stranded DNA-binding protein.

PubMed ID: 17596542

DOI: 10.1182/blood-2006-11-057273

PubMed ID: 17141802

Title: Mammalian TIMELESS and Tipin are evolutionarily conserved replication fork-associated factors.

PubMed ID: 17141802

DOI: 10.1016/j.jmb.2006.10.097

PubMed ID: 17765923

Title: RPA mediates recombination repair during replication stress and is displaced from DNA by checkpoint signalling in human cells.

PubMed ID: 17765923

DOI: 10.1016/j.jmb.2007.07.068

PubMed ID: 17296725

Title: The human Tim/Tipin complex coordinates an Intra-S checkpoint response to UV that slows replication fork displacement.

PubMed ID: 17296725

DOI: 10.1128/mcb.02190-06

PubMed ID: 17959650

Title: Replication protein A prevents accumulation of single-stranded telomeric DNA in cells that use alternative lengthening of telomeres.

PubMed ID: 17959650

DOI: 10.1093/nar/gkm738

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19793863

Title: The annealing helicase HARP is recruited to DNA repair sites via an interaction with RPA.

PubMed ID: 19793863

DOI: 10.1101/gad.1831509

PubMed ID: 19793861

Title: The annealing helicase SMARCAL1 maintains genome integrity at stalled replication forks.

PubMed ID: 19793861

DOI: 10.1101/gad.1839909

PubMed ID: 19793862

Title: The SIOD disorder protein SMARCAL1 is an RPA-interacting protein involved in replication fork restart.

PubMed ID: 19793862

DOI: 10.1101/gad.1832309

PubMed ID: 19116208

Title: An alternative form of replication protein a prevents viral replication in vitro.

PubMed ID: 19116208

DOI: 10.1074/jbc.m808963200

PubMed ID: 19996105

Title: An alternative form of replication protein a expressed in normal human tissues supports DNA repair.

PubMed ID: 19996105

DOI: 10.1074/jbc.m109.079418

PubMed ID: 20154705

Title: A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombination.

PubMed ID: 20154705

DOI: 10.1038/nsmb.1769

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21504906

Title: E3 ligase RFWD3 participates in replication checkpoint control.

PubMed ID: 21504906

DOI: 10.1074/jbc.m111.222869

PubMed ID: 21558276

Title: RING finger and WD repeat domain 3 (RFWD3) associates with replication protein A (RPA) and facilitates RPA-mediated DNA damage response.

PubMed ID: 21558276

DOI: 10.1074/jbc.m111.222802

PubMed ID: 21731742

Title: DNA-PK-dependent RPA2 hyperphosphorylation facilitates DNA repair and suppresses sister chromatid exchange.

PubMed ID: 21731742

DOI: 10.1371/journal.pone.0021424

PubMed ID: 22684010

Title: 4E-BP3 regulates eIF4E-mediated nuclear mRNA export and interacts with replication protein A2.

PubMed ID: 22684010

DOI: 10.1016/j.febslet.2012.05.059

PubMed ID: 23393223

Title: Translational regulation of RPA2 via internal ribosomal entry site and by eIF3a.

PubMed ID: 23393223

DOI: 10.1093/carcin/bgt052

PubMed ID: 23319600

Title: FBH1 promotes DNA double-strand breakage and apoptosis in response to DNA replication stress.

PubMed ID: 23319600

DOI: 10.1083/jcb.201209002

PubMed ID: 24332808

Title: PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and drives ATR activation via a ubiquitin-mediated circuitry.

PubMed ID: 24332808

DOI: 10.1016/j.molcel.2013.11.002

PubMed ID: 26474068

Title: RFWD3-dependent ubiquitination of RPA regulates repair at stalled replication forks.

PubMed ID: 26474068

DOI: 10.1016/j.molcel.2015.09.011

PubMed ID: 27601467

Title: Ewing Tumor-associated Antigen 1 interacts with replication protein A to promote restart of stalled replication forks.

PubMed ID: 27601467

DOI: 10.1074/jbc.c116.747758

PubMed ID: 27723720

Title: ETAA1 acts at stalled replication forks to maintain genome integrity.

PubMed ID: 27723720

DOI: 10.1038/ncb3415

PubMed ID: 27723717

Title: Activation of the ATR kinase by the RPA-binding protein ETAA1.

PubMed ID: 27723717

DOI: 10.1038/ncb3422

PubMed ID: 28575657

Title: RPA-mediated recruitment of the E3 ligase RFWD3 is vital for interstrand crosslink repair and human health.

PubMed ID: 28575657

DOI: 10.1016/j.molcel.2017.04.021

PubMed ID: 29290612

Title: Removal of RTF2 from Stalled Replisomes Promotes Maintenance of Genome Integrity.

PubMed ID: 29290612

DOI: 10.1016/j.molcel.2017.11.035

PubMed ID: 10449415

Title: The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding.

PubMed ID: 10449415

DOI: 10.1093/emboj/18.16.4498

PubMed ID: 11081631

Title: Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA.

PubMed ID: 11081631

DOI: 10.1016/s0092-8674(00)00136-7

PubMed ID: 11927569

Title: Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA.

PubMed ID: 11927569

DOI: 10.1093/emboj/21.7.1855

Sequence Information:

Length: 270
Mass: 29247
Checksum: 61A563EA7B34A9B1
Sequence:

MWNSGFESYG SSSYGGAGGY TQSPGGFGSP APSQAEKKSR ARAQHIVPCT ISQLLSATLV 
DEVFRIGNVE ISQVTIVGII RHAEKAPTNI VYKIDDMTAA PMDVRQWVDT DDTSSENTVV 
PPETYVKVAG HLRSFQNKKS LVAFKIMPLE DMNEFTTHIL EVINAHMVLS KANSQPSAGR 
APISNPGMSE AGNFGGNSFM PANGLTVAQN QVLNLIKACP RPEGLNFQDL KNQLKHMSVS 
SIKQAVDFLS NEGHIYSTVD DDHFKSTDAE

Genular Protein ID: 691535472

Symbol: B4DUL2_HUMAN

Name: N/A

UniProtKB Accession Codes:

B4DUL2

Database IDs:

Sequence Information:

Length: 174
Mass: 19062
Checksum: 3F936D7AF6B63159
Sequence:

MTAAPMDVRQ WVDTDDTSSE NTVVPPETYV KVAGHLRSFQ NKKSLVAFKI MPLEDMNEFT 
THILEVINAH MVLSKANSQP SAGRAPISNP GMSEAGNFGG NSFMPANGLT VAQNQVLNLI 
KACPRPEGLN FQDLKNQLKH MSVSSIKQAV DFLSNEGHIY STVDDDHFKS TDAE

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: RPA2

Associated with

Cells (max top 100)

Other Information

The primary structure of the 32-kDa subunit of human replication protein A. PubMed ID: 2406247

The DNA sequence and biological annotation of human chromosome 1. PubMed ID: 16710414

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Cell-cycle-regulated phosphorylation of DNA replication factor A from human and yeast cells. PubMed ID: 2200738

cdc2 family kinases phosphorylate a human cell DNA replication factor, RPA, and activate DNA replication. PubMed ID: 1318195

The ionizing radiation-induced replication protein A phosphorylation response differs between ataxia telangiectasia and normal human cells. PubMed ID: 8246944

Mammalian DNA nucleotide excision repair reconstituted with purified protein components. PubMed ID: 7697716

RPA involvement in the damage-recognition and incision steps of nucleotide excision repair. PubMed ID: 7700386

Physical interaction between human RAD52 and RPA is required for homologous recombination in mammalian cells. PubMed ID: 8702565

Mapping of amino acid residues in the p34 subunit of human single-stranded DNA-binding protein phosphorylated by DNA-dependent protein kinase and Cdc2 kinase in vitro. PubMed ID: 9139719

Sites of UV-induced phosphorylation of the p34 subunit of replication protein A from HeLa cells. PubMed ID: 9295339

The evolutionarily conserved zinc finger motif in the largest subunit of human replication protein A is required for DNA replication and mismatch repair but not for nucleotide excision repair. PubMed ID: 9430682

Replication protein A stimulates long patch DNA base excision repair. PubMed ID: 9765279

RBT1, a novel transcriptional co-activator, binds the second subunit of replication protein A. PubMed ID: 10982866

ATR kinase activity regulates the intranuclear translocation of ATR and RPA following ionizing radiation. PubMed ID: 12814551

Coordinated regulation of replication protein A activities by its subunits p14 and p32. PubMed ID: 15205463

FANCJ (BACH1) helicase forms DNA damage inducible foci with replication protein A and interacts physically and functionally with the single-stranded DNA-binding protein. PubMed ID: 17596542

Mammalian TIMELESS and Tipin are evolutionarily conserved replication fork-associated factors. PubMed ID: 17141802

RPA mediates recombination repair during replication stress and is displaced from DNA by checkpoint signalling in human cells. PubMed ID: 17765923

The human Tim/Tipin complex coordinates an Intra-S checkpoint response to UV that slows replication fork displacement. PubMed ID: 17296725

Replication protein A prevents accumulation of single-stranded telomeric DNA in cells that use alternative lengthening of telomeres. PubMed ID: 17959650

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

The annealing helicase HARP is recruited to DNA repair sites via an interaction with RPA. PubMed ID: 19793863

The annealing helicase SMARCAL1 maintains genome integrity at stalled replication forks. PubMed ID: 19793861

The SIOD disorder protein SMARCAL1 is an RPA-interacting protein involved in replication fork restart. PubMed ID: 19793862

An alternative form of replication protein a prevents viral replication in vitro. PubMed ID: 19116208

An alternative form of replication protein a expressed in normal human tissues supports DNA repair. PubMed ID: 19996105

A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombination. PubMed ID: 20154705

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

E3 ligase RFWD3 participates in replication checkpoint control. PubMed ID: 21504906

RING finger and WD repeat domain 3 (RFWD3) associates with replication protein A (RPA) and facilitates RPA-mediated DNA damage response. PubMed ID: 21558276

DNA-PK-dependent RPA2 hyperphosphorylation facilitates DNA repair and suppresses sister chromatid exchange. PubMed ID: 21731742

4E-BP3 regulates eIF4E-mediated nuclear mRNA export and interacts with replication protein A2. PubMed ID: 22684010

Translational regulation of RPA2 via internal ribosomal entry site and by eIF3a. PubMed ID: 23393223

FBH1 promotes DNA double-strand breakage and apoptosis in response to DNA replication stress. PubMed ID: 23319600

PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and drives ATR activation via a ubiquitin-mediated circuitry. PubMed ID: 24332808

RFWD3-dependent ubiquitination of RPA regulates repair at stalled replication forks. PubMed ID: 26474068

Ewing Tumor-associated Antigen 1 interacts with replication protein A to promote restart of stalled replication forks. PubMed ID: 27601467

ETAA1 acts at stalled replication forks to maintain genome integrity. PubMed ID: 27723720

Activation of the ATR kinase by the RPA-binding protein ETAA1. PubMed ID: 27723717

RPA-mediated recruitment of the E3 ligase RFWD3 is vital for interstrand crosslink repair and human health. PubMed ID: 28575657

Removal of RTF2 from Stalled Replisomes Promotes Maintenance of Genome Integrity. PubMed ID: 29290612

The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding. PubMed ID: 10449415

Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA. PubMed ID: 11081631

Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA. PubMed ID: 11927569