RPA1 | ENSG00000132383 | NCBI 6117

Details for: RPA1

Gene ID: 6117

Symbol: RPA1

Ensembl ID: ENSG00000132383

Description: replication protein A1

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 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)
Metabolism of proteins
(R-HSA-392499)
Mismatch repair
(R-HSA-5358508)
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)
Post-translational protein modification
(R-HSA-597592)
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)
Sumo e3 ligases sumoylate target proteins
(R-HSA-3108232)
Sumoylation
(R-HSA-2990846)
Sumoylation of dna damage response and repair proteins
(R-HSA-3108214)
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)
Chromatin-protein adaptor activity
(GO:0140463)
Damaged dna binding
(GO:0003684)
Dna-templated dna replication
(GO:0006261)
Dna repair
(GO:0006281)
Dna replication
(GO:0006260)
Double-strand break repair via homologous recombination
(GO:0000724)
G-rich strand telomeric dna binding
(GO:0098505)
Metal ion binding
(GO:0046872)
Nucleotide-excision repair
(GO:0006289)
Protein binding
(GO:0005515)
Single-stranded dna binding
(GO:0003697)
Single-stranded telomeric dna binding
(GO:0043047)
Telomere maintenance
(GO:0000723)

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: embryonic stem cell (CL0002322)
Fold Change: 80.5442
Cell Significance Index: -33.1800
Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 68.5415
Cell Significance Index: -32.3600
Cell Name: mucosal type mast cell (CL0000485)
Fold Change: 65.9435
Cell Significance Index: -26.7900
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 58.8081
Cell Significance Index: -30.2500
Cell Name: ciliated cell of the bronchus (CL0002332)
Fold Change: 28.4160
Cell Significance Index: -27.1300
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 9.9632
Cell Significance Index: -26.6900
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 8.2339
Cell Significance Index: -25.2900
Cell Name: epidermal Langerhans cell (CL0002457)
Fold Change: 5.8896
Cell Significance Index: -12.8900
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: 1.2151
Cell Significance Index: 141.6100
Cell Name: gut absorptive cell (CL0000677)
Fold Change: 1.1167
Cell Significance Index: 67.0400
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: 1.0969
Cell Significance Index: 315.6000
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: 0.9663
Cell Significance Index: 105.1100
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 0.9172
Cell Significance Index: 828.1500
Cell Name: neoplastic cell (CL0001063)
Fold Change: 0.9154
Cell Significance Index: 181.6600
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 0.8177
Cell Significance Index: 132.9900
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: 0.8161
Cell Significance Index: 11.1400
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 0.8045
Cell Significance Index: 94.8700
Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
Fold Change: 0.7548
Cell Significance Index: 26.2300
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 0.6464
Cell Significance Index: 129.6700
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: 0.4817
Cell Significance Index: 333.1800
Cell Name: colon goblet cell (CL0009039)
Fold Change: 0.4745
Cell Significance Index: 46.9400
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: 0.4684
Cell Significance Index: 13.0900
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 0.3983
Cell Significance Index: 142.8800
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: 0.3853
Cell Significance Index: 26.6500
Cell Name: cell in vitro (CL0001034)
Fold Change: 0.3583
Cell Significance Index: 195.7000
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 0.3524
Cell Significance Index: 48.3900
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 0.3412
Cell Significance Index: 61.5100
Cell Name: lung endothelial cell (CL1001567)
Fold Change: 0.3348
Cell Significance Index: 17.4400
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: 0.3329
Cell Significance Index: 8.8900
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: 0.3283
Cell Significance Index: 25.2000
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 0.3261
Cell Significance Index: 144.1700
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 0.2854
Cell Significance Index: 35.1000
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 0.2823
Cell Significance Index: 13.1600
Cell Name: odontoblast (CL0000060)
Fold Change: 0.2529
Cell Significance Index: 32.4200
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: 0.2496
Cell Significance Index: 6.2400
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: 0.2437
Cell Significance Index: 5.2800
Cell Name: early pro-B cell (CL0002046)
Fold Change: 0.2381
Cell Significance Index: 15.3600
Cell Name: abnormal cell (CL0001061)
Fold Change: 0.2158
Cell Significance Index: 22.0400
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: 0.1885
Cell Significance Index: 10.5800
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.1698
Cell Significance Index: 319.7700
Cell Name: fibroblast of dermis (CL0002551)
Fold Change: 0.1581
Cell Significance Index: 3.3100
Cell Name: mesenchymal cell (CL0008019)
Fold Change: 0.1353
Cell Significance Index: 2.2700
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: 0.1159
Cell Significance Index: 3.3400
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.1110
Cell Significance Index: 21.1300
Cell Name: glycinergic neuron (CL1001509)
Fold Change: 0.0932
Cell Significance Index: 4.9000
Cell Name: sebum secreting cell (CL0000317)
Fold Change: 0.0865
Cell Significance Index: 6.1200
Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
Fold Change: 0.0834
Cell Significance Index: 2.4500
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: 0.0440
Cell Significance Index: 1.4100
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: 0.0431
Cell Significance Index: 19.5400
Cell Name: anterior lens cell (CL0002223)
Fold Change: 0.0369
Cell Significance Index: 68.1200
Cell Name: lens epithelial cell (CL0002224)
Fold Change: 0.0340
Cell Significance Index: 52.2800
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: 0.0313
Cell Significance Index: 19.8600
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: 0.0140
Cell Significance Index: 0.8800
Cell Name: secondary lens fiber (CL0002225)
Fold Change: 0.0015
Cell Significance Index: 2.0900
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: -0.0026
Cell Significance Index: -0.1200
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: -0.0028
Cell Significance Index: -0.1000
Cell Name: lactocyte (CL0002325)
Fold Change: -0.0087
Cell Significance Index: -1.1300
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: -0.0125
Cell Significance Index: -0.6500
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: -0.0198
Cell Significance Index: -14.9600
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: -0.0302
Cell Significance Index: -22.1600
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0453
Cell Significance Index: -33.5300
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.0559
Cell Significance Index: -31.5300
Cell Name: leptomeningeal cell (CL0000708)
Fold Change: -0.0578
Cell Significance Index: -1.2400
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0593
Cell Significance Index: -37.0400
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: -0.0695
Cell Significance Index: -3.1500
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: -0.0835
Cell Significance Index: -14.2600
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.1140
Cell Significance Index: -11.8700
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.1178
Cell Significance Index: -17.1300
Cell Name: transit amplifying cell of small intestine (CL0009012)
Fold Change: -0.1721
Cell Significance Index: -3.5700
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: -0.1728
Cell Significance Index: -12.8800
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.1778
Cell Significance Index: -37.4400
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: -0.1782
Cell Significance Index: -10.9500
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: -0.1849
Cell Significance Index: -12.4300
Cell Name: pro-T cell (CL0000827)
Fold Change: -0.1875
Cell Significance Index: -4.7900
Cell Name: granulosa cell (CL0000501)
Fold Change: -0.1882
Cell Significance Index: -4.9500
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: -0.1943
Cell Significance Index: -5.2900
Cell Name: skeletal muscle myoblast (CL0000515)
Fold Change: -0.1959
Cell Significance Index: -2.1300
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.2050
Cell Significance Index: -23.4900
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: -0.2216
Cell Significance Index: -9.8000
Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: -0.2225
Cell Significance Index: -5.7200
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: -0.2860
Cell Significance Index: -6.0900
Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: -0.3075
Cell Significance Index: -11.6400
Cell Name: cerebellar granule cell (CL0001031)
Fold Change: -0.3285
Cell Significance Index: -5.6300
Cell Name: fibro/adipogenic progenitor cell (CL0009099)
Fold Change: -0.3470
Cell Significance Index: -17.5400
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: -0.3478
Cell Significance Index: -9.3200
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.3501
Cell Significance Index: -27.7300
Cell Name: Hofbauer cell (CL3000001)
Fold Change: -0.4427
Cell Significance Index: -3.6100
Cell Name: retinal rod cell (CL0000604)
Fold Change: -0.4522
Cell Significance Index: -5.3900
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -0.5203
Cell Significance Index: -31.9000
Cell Name: preadipocyte (CL0002334)
Fold Change: -0.5267
Cell Significance Index: -10.2800
Cell Name: kidney epithelial cell (CL0002518)
Fold Change: -0.5602
Cell Significance Index: -16.5000
Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: -0.5834
Cell Significance Index: -15.6100
Cell Name: peg cell (CL4033014)
Fold Change: -0.6791
Cell Significance Index: -15.6900
Cell Name: hippocampal pyramidal neuron (CL1001571)
Fold Change: -0.6865
Cell Significance Index: -19.5900
Cell Name: medium spiny neuron (CL1001474)
Fold Change: -0.6966
Cell Significance Index: -9.4000
Cell Name: interstitial cell of ovary (CL0002094)
Fold Change: -0.7067
Cell Significance Index: -9.0500
Cell Name: stratified epithelial cell (CL0000079)
Fold Change: -0.7336
Cell Significance Index: -26.9300
Cell Name: type I muscle cell (CL0002211)
Fold Change: -0.7890
Cell Significance Index: -19.2500
Cell Name: corticothalamic-projecting glutamatergic cortical neuron (CL4023013)
Fold Change: -0.8295
Cell Significance Index: -26.4200
Cell Name: L5 extratelencephalic projecting glutamatergic cortical neuron (CL4023041)
Fold Change: -0.8360
Cell Significance Index: -29.2900

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** RPA1 exhibits several key characteristics that contribute to its role in maintaining genome stability: 1. **DNA binding**: RPA1 binds to ssDNA and dsDNA, forming a complex that stabilizes the DNA molecule and facilitates its replication, repair, and recombination. 2. **Single-stranded DNA binding**: RPA1 binds to ssDNA, protecting it from degradation and facilitating its interaction with other proteins involved in DNA repair and replication. 3. **Double-stranded DNA binding**: RPA1 also binds to dsDNA, influencing chromatin remodeling and transcriptional regulation. 4. **Cell cycle regulation**: RPA1 regulates the cell cycle by modulating the activity of the pre-replicative complex and the G1/S transition. 5. **DNA damage response**: RPA1 plays a critical role in the DNA damage response by facilitating the recognition and repair of DNA damage. **Pathways and Functions** RPA1 is involved in various cellular pathways and functions, including: 1. **DNA replication**: RPA1 facilitates the unwinding of double-stranded DNA and the synthesis of new DNA strands during replication. 2. **DNA repair**: RPA1 regulates the repair of DNA damage by facilitating the recognition and repair of single-stranded breaks and other lesions. 3. **Chromatin remodeling**: RPA1 influences chromatin remodeling by regulating the activity of chromatin-modifying enzymes. 4. **Transcriptional regulation**: RPA1 modulates transcriptional regulation by influencing the activity of transcription factors and chromatin-modifying enzymes. 5. **Cell cycle regulation**: RPA1 regulates the cell cycle by modulating the activity of the pre-replicative complex and the G1/S transition. **Clinical Significance** Dysregulation of RPA1 has been implicated in several human diseases, including: 1. **Cancer**: RPA1 mutations or overexpression have been linked to various types of cancer, including breast, ovarian, and lung cancer. 2. **Neurodegenerative disorders**: RPA1 mutations have been associated with neurodegenerative disorders, including Huntington's disease and amyotrophic lateral sclerosis (ALS). 3. **DNA damage response disorders**: RPA1 mutations have been linked to disorders of DNA damage response, including Fanconi anemia and Bloom syndrome. 4. **Genomic instability**: RPA1 dysfunction has been implicated in genomic instability, leading to chromosomal instability and an increased risk of cancer. In conclusion, RPA1 is a critical component of the replication protein A complex, playing a central role in maintaining genome stability by facilitating DNA replication, repair, and recombination. Dysregulation of RPA1 has been implicated in several human diseases, highlighting the importance of this gene in maintaining genome integrity.

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 70 kDa DNA-binding subunit

Genular Protein ID: 1382693081

Symbol: RFA1_HUMAN

Name: Replication protein A 70 kDa DNA-binding subunit

UniProtKB Accession Codes:

P27694 A8K0Y9 Q59ES9

Database IDs:

Citations:

PubMed ID: 2050703

Title: Characterization of a cDNA encoding the 70-kDa single-stranded DNA-binding subunit of human replication protein A and the role of the protein in DNA replication.

PubMed ID: 2050703

DOI: 10.1016/s0021-9258(18)99069-1

PubMed ID: 8420996

Title: Type I human complement C2 deficiency. A 28-base pair gene deletion causes skipping of exon 6 during RNA splicing.

PubMed ID: 8420996

DOI: 10.1016/s0021-9258(18)53993-4

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

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: 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: 7760808

Title: Rpa4, a homolog of the 34-kilodalton subunit of the replication protein A complex.

PubMed ID: 7760808

DOI: 10.1128/mcb.15.6.3119

PubMed ID: 9214288

Title: Role of protein-protein interactions in the function of replication protein A (RPA): RPA modulates the activity of DNA polymerase alpha by multiple mechanisms.

PubMed ID: 9214288

DOI: 10.1021/bi970473r

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: 9699634

Title: Solution structure of the DNA- and RPA-binding domain of the human repair factor XPA.

PubMed ID: 9699634

DOI: 10.1038/1400

PubMed ID: 10563794

Title: Interactions of human nucleotide excision repair protein XPA with DNA and RPA70 Delta C327: chemical shift mapping and 15N NMR relaxation studies.

PubMed ID: 10563794

DOI: 10.1021/bi991755p

PubMed ID: 14654843

Title: Proteomic characterization of the human centrosome by protein correlation profiling.

PubMed ID: 14654843

DOI: 10.1038/nature02166

PubMed ID: 12791985

Title: Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes.

PubMed ID: 12791985

DOI: 10.1126/science.1083430

PubMed ID: 16135809

Title: Sumoylation of the novel protein hRIPbeta is involved in replication protein A deposition in PML nuclear bodies.

PubMed ID: 16135809

DOI: 10.1128/mcb.25.18.8202-8214.2005

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: 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: 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: 17525332

Title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.

PubMed ID: 17525332

DOI: 10.1126/science.1140321

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: 19116208

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

PubMed ID: 19116208

DOI: 10.1074/jbc.m808963200

PubMed ID: 19010961

Title: Evidence for direct contact between the RPA3 subunit of the human replication protein A and single-stranded DNA.

PubMed ID: 19010961

DOI: 10.1093/nar/gkn895

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

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: 20705237

Title: Regulation of DNA repair through desumoylation and sumoylation of replication protein A complex.

PubMed ID: 20705237

DOI: 10.1016/j.molcel.2010.07.021

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: 22194613

Title: Human DNA helicase B (HDHB) binds to replication protein A and facilitates cellular recovery from replication stress.

PubMed ID: 22194613

DOI: 10.1074/jbc.m111.324582

PubMed ID: 22223895

Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

PubMed ID: 22223895

DOI: 10.1074/mcp.m111.015131

PubMed ID: 24126761

Title: hPrimpol1/CCDC111 is a human DNA primase-polymerase required for the maintenance of genome integrity.

PubMed ID: 24126761

DOI: 10.1038/embor.2013.159

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

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: 24906880

Title: PARG is dispensable for recovery from transient replicative stress but required to prevent detrimental accumulation of poly(ADP-ribose) upon prolonged replicative stress.

PubMed ID: 24906880

DOI: 10.1093/nar/gku505

PubMed ID: 25550423

Title: Human PrimPol is a highly error-prone polymerase regulated by single-stranded DNA binding proteins.

PubMed ID: 25550423

DOI: 10.1093/nar/gku1321

PubMed ID: 26774285

Title: HELB is a feedback inhibitor of DNA end resection.

PubMed ID: 26774285

DOI: 10.1016/j.molcel.2015.12.013

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: 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: 35597237

Title: A PARylation-phosphorylation cascade promotes TOPBP1 loading and RPA-RAD51 exchange in homologous recombination.

PubMed ID: 35597237

DOI: 10.1016/j.molcel.2022.04.031

PubMed ID: 8990123

Title: Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA.

PubMed ID: 8990123

DOI: 10.1038/385176a0

PubMed ID: 28534480

Title: Molecular basis for PrimPol recruitment to replication forks by RPA.

PubMed ID: 28534480

DOI: 10.1038/ncomms15222

PubMed ID: 34767620

Title: Gain-of-function mutations in RPA1 cause a syndrome with short telomeres and somatic genetic rescue.

PubMed ID: 34767620

DOI: 10.1182/blood.2021011980

Sequence Information:

Length: 616
Mass: 68138
Checksum: FE038F40F5886CD1
Sequence:

MVGQLSEGAI AAIMQKGDTN IKPILQVINI RPITTGNSPP RYRLLMSDGL NTLSSFMLAT 
QLNPLVEEEQ LSSNCVCQIH RFIVNTLKDG RRVVILMELE VLKSAEAVGV KIGNPVPYNE 
GLGQPQVAPP APAASPAASS RPQPQNGSSG MGSTVSKAYG ASKTFGKAAG PSLSHTSGGT 
QSKVVPIASL TPYQSKWTIC ARVTNKSQIR TWSNSRGEGK LFSLELVDES GEIRATAFNE 
QVDKFFPLIE VNKVYYFSKG TLKIANKQFT AVKNDYEMTF NNETSVMPCE DDHHLPTVQF 
DFTGIDDLEN KSKDSLVDII GICKSYEDAT KITVRSNNRE VAKRNIYLMD TSGKVVTATL 
WGEDADKFDG SRQPVLAIKG ARVSDFGGRS LSVLSSSTII ANPDIPEAYK LRGWFDAEGQ 
ALDGVSISDL KSGGVGGSNT NWKTLYEVKS ENLGQGDKPD YFSSVATVVY LRKENCMYQA 
CPTQDCNKKV IDQQNGLYRC EKCDTEFPNF KYRMILSVNI ADFQENQWVT CFQESAEAIL 
GQNAAYLGEL KDKNEQAFEE VFQNANFRSF IFRVRVKVET YNDESRIKAT VMDVKPVDYR 
EYGRRLVMSI RRSALM

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: RPA1

Associated with

Cells (max top 100)

Other Information

Characterization of a cDNA encoding the 70-kDa single-stranded DNA-binding subunit of human replication protein A and the role of the protein in DNA replication. PubMed ID: 2050703

Type I human complement C2 deficiency. A 28-base pair gene deletion causes skipping of exon 6 during RNA splicing. PubMed ID: 8420996

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

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

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

Rpa4, a homolog of the 34-kilodalton subunit of the replication protein A complex. PubMed ID: 7760808

Role of protein-protein interactions in the function of replication protein A (RPA): RPA modulates the activity of DNA polymerase alpha by multiple mechanisms. PubMed ID: 9214288

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

Solution structure of the DNA- and RPA-binding domain of the human repair factor XPA. PubMed ID: 9699634

Interactions of human nucleotide excision repair protein XPA with DNA and RPA70 Delta C327: chemical shift mapping and 15N NMR relaxation studies. PubMed ID: 10563794

Proteomic characterization of the human centrosome by protein correlation profiling. PubMed ID: 14654843

Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes. PubMed ID: 12791985

Sumoylation of the novel protein hRIPbeta is involved in replication protein A deposition in PML nuclear bodies. PubMed ID: 16135809

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

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

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

ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. PubMed ID: 17525332

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

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

Evidence for direct contact between the RPA3 subunit of the human replication protein A and single-stranded DNA. PubMed ID: 19010961

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

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

Regulation of DNA repair through desumoylation and sumoylation of replication protein A complex. PubMed ID: 20705237

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

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

Human DNA helicase B (HDHB) binds to replication protein A and facilitates cellular recovery from replication stress. PubMed ID: 22194613

Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features. PubMed ID: 22223895

hPrimpol1/CCDC111 is a human DNA primase-polymerase required for the maintenance of genome integrity. PubMed ID: 24126761

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

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

PARG is dispensable for recovery from transient replicative stress but required to prevent detrimental accumulation of poly(ADP-ribose) upon prolonged replicative stress. PubMed ID: 24906880

Human PrimPol is a highly error-prone polymerase regulated by single-stranded DNA binding proteins. PubMed ID: 25550423

HELB is a feedback inhibitor of DNA end resection. PubMed ID: 26774285

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

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

A PARylation-phosphorylation cascade promotes TOPBP1 loading and RPA-RAD51 exchange in homologous recombination. PubMed ID: 35597237

Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA. PubMed ID: 8990123

Molecular basis for PrimPol recruitment to replication forks by RPA. PubMed ID: 28534480

Gain-of-function mutations in RPA1 cause a syndrome with short telomeres and somatic genetic rescue. PubMed ID: 34767620