RPA1

Summary

RPA1 (replication protein A1, HGNC:10289) is a protein-coding gene on chromosome 17p13.3, encoding Replication protein A 70 kDa DNA-binding subunit (P27694). As 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.

This gene encodes the largest subunit of the heterotrimeric Replication Protein A (RPA) complex, which binds to single-stranded DNA (ssDNA), forming a nucleoprotein complex that plays an important role in DNA metabolism, being involved in DNA replication, repair, recombination, telomere maintenance, and co-ordinating the cellular response to DNA damage through activation of the ataxia telangiectasia and Rad3-related protein (ATR) kinase. The nucleoprotein complex protects the single-stranded DNA from nucleases, prevents formation of secondary structures that would interfere with repair, and co-ordinates the recruitment and departure of different genome maintenance factors. This subunit contains four oligonucleotide/oligosaccharide-binding (OB) domains, though the majority of ssDNA binding occurs in two of these domains. The heterotrimeric complex has two different modes of ssDNA binding, a low-affinity and high-affinity mode, determined by which ssDNA binding domains are utilized. The different binding modes differ in the length of DNA bound and in the proteins with which it interacts, thereby playing a role in regulating different genomic maintenance pathways.

Source: NCBI Gene 6117 — RefSeq curated summary.

At a glance

• Gene–disease (curated): pulmonary fibrosis and/or bone marrow failure, telomere-related, 6 (Strong, GenCC) — +1 more curated relationship
• Clinical variants (ClinVar): 116 total — 2 pathogenic
• Phenotypes (HPO): 17
• Druggable target: yes
• MANE Select transcript: NM_002945

Identifiers

Gene identifiers

Field	Value
HGNC ID	HGNC:10289
Approved symbol	RPA1
Name	replication protein A1
Location	17p13.3
Locus type	gene with protein product
Status	Approved
Aliases	REPA1, RPA70, HSSB, RF-A, RP-A
Ensembl gene	ENSG00000132383
Ensembl biotype	protein_coding
OMIM	179835
Entrez	6117

Gene structure

Transcript identifiers

Ensembl transcripts: 23 — 20 protein_coding, 2 protein_coding_CDS_not_defined, 1 retained_intron

ENST00000254719, ENST00000570451, ENST00000571058, ENST00000571725, ENST00000573924, ENST00000573994, ENST00000574049, ENST00000852055, ENST00000852056, ENST00000852057, ENST00000852058, ENST00000852059, ENST00000852060, ENST00000852061, ENST00000852062, ENST00000852063, ENST00000852064, ENST00000933416, ENST00000933417, ENST00000933418, ENST00000933419, ENST00000933420, ENST00000962481

RefSeq mRNA: 3 — MANE Select: NM_002945 NM_001355120, NM_001355121, NM_002945

CCDS: CCDS11014

Canonical transcript exons

ENST00000254719 — 17 exons

Exon	Start	End
ENSE00000904192	1879215	1879407
ENSE00001116060	1891833	1891940
ENSE00001116065	1888675	1888851
ENSE00001132340	1883812	1883944
ENSE00001197976	1880543	1880691
ENSE00001310575	1879560	1879699
ENSE00002632409	1897071	1900082
ENSE00002669400	1830005	1830126
ENSE00003463656	1877212	1877314
ENSE00003498894	1842803	1842853
ENSE00003509441	1878993	1879061
ENSE00003530312	1872434	1872526
ENSE00003605218	1875661	1875793
ENSE00003610995	1895009	1895095
ENSE00003629134	1843920	1843998
ENSE00003641368	1844578	1844686
ENSE00003662129	1853101	1853189

Expression profiles

Bgee: expression breadth ubiquitous, 300 present calls, max score 99.80.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 32.8200 / max 253.7529, expressed in 1827 samples.

FANTOM5 promoters (5 alternative TSS)

Promoter ID	TPM avg	Samples expressed
158784	28.9416	1826
158783	2.2205	1299
158785	1.0655	635
158786	0.5675	369
158789	0.0249	11

Top tissues by expression

301 total, by Bgee expression score (0-100, higher = more expressed):

Tissue	Anatomy ID	Expression score	Quality
secondary oocyte	CL:0000655	99.80	gold quality
oocyte	CL:0000023	99.42	gold quality
ventricular zone	UBERON:0003053	98.30	gold quality
ganglionic eminence	UBERON:0004023	97.51	gold quality
parietal pleura	UBERON:0002400	97.49	gold quality
embryo	UBERON:0000922	97.08	gold quality
visceral pleura	UBERON:0002401	96.89	gold quality
pleura	UBERON:0000977	96.87	gold quality
germinal epithelium of ovary	UBERON:0001304	96.58	gold quality
gingival epithelium	UBERON:0001949	96.36	gold quality
trabecular bone tissue	UBERON:0002483	96.35	gold quality
tibia	UBERON:0000979	96.11	gold quality
gingiva	UBERON:0001828	95.87	gold quality
esophagus squamous epithelium	UBERON:0006920	95.81	gold quality
parotid gland	UBERON:0001831	95.74	gold quality
palpebral conjunctiva	UBERON:0001812	95.72	gold quality
seminal vesicle	UBERON:0000998	95.53	gold quality
penis	UBERON:0000989	95.48	gold quality
epithelium of esophagus	UBERON:0001976	95.24	gold quality
monocyte	CL:0000576	95.23	gold quality
mononuclear cell	CL:0000842	95.18	gold quality
leukocyte	CL:0000738	95.15	gold quality
squamous epithelium	UBERON:0006914	95.10	gold quality
oral cavity	UBERON:0000167	95.02	gold quality
eye	UBERON:0000970	94.95	gold quality
corpus epididymis	UBERON:0004359	94.93	gold quality
stromal cell of endometrium	CL:0002255	94.92	gold quality
tonsil	UBERON:0002372	94.91	gold quality
gastrocnemius	UBERON:0001388	94.60	gold quality
hindlimb stylopod muscle	UBERON:0004252	94.60	gold quality

Single-cell (SCXA)

Detected in 3 experiment(s), a significant marker in 2.

Experiment	Marker?	Max mean expression
E-MTAB-7052	yes	227.65
E-ANND-3	yes	9.34
E-GEOD-70580	no	725.09

Regulation

Is transcription factor: no

miRNA regulators (miRDB)

92 targeting RPA1, top 30 by miRDB confidence (max_score; target_count = how many genes the miRNA targets in total — lower means more specific):

miRNA	Max score	Avg score	miRNA target_count
HSA-MIR-4476	100.00	68.18	2030
HSA-MIR-6876-5P	100.00	67.68	2126
HSA-MIR-4533	100.00	69.48	2758
HSA-MIR-4481	100.00	66.42	1669
HSA-MIR-4668-3P	100.00	68.74	2635
HSA-MIR-1252-5P	100.00	69.80	2774
HSA-MIR-29A-3P	100.00	73.11	1835
HSA-MIR-29B-3P	100.00	73.18	1833
HSA-MIR-29C-3P	100.00	73.15	1833
HSA-MIR-4745-5P	99.98	65.95	1028
HSA-MIR-4775	99.98	75.00	6394
HSA-MIR-145-5P	99.92	71.13	1836
HSA-MIR-5195-3P	99.92	70.92	1877
HSA-MIR-8063	99.91	69.76	3146
HSA-MIR-5682	99.89	72.56	1005
HSA-LET-7A-2-3P	99.87	70.53	1921
HSA-MIR-4779	99.86	66.50	1583
HSA-LET-7G-3P	99.85	70.43	1929
HSA-MIR-6515-3P	99.82	68.19	1933
HSA-MIR-4760-5P	99.80	69.88	1619
HSA-MIR-556-3P	99.74	68.75	1203
HSA-MIR-10393-3P	99.72	66.56	961
HSA-MIR-6801-5P	99.72	66.50	981
HSA-MIR-4527	99.66	67.43	714
HSA-MIR-452-5P	99.65	69.63	1762
HSA-MIR-4676-3P	99.65	69.31	1733
HSA-MIR-892C-3P	99.65	69.38	1745
HSA-MIR-3177-5P	99.65	70.38	1174
HSA-MIR-10393-5P	99.65	68.01	1368
HSA-MIR-586	99.65	70.40	2051

Literature-anchored findings (GeneRIF, showing 40)

• Sequential model of binding in which DBD-A is responsible for the initial interaction with ssDNA, that domains A, B, and C (RPA1) contact 12-23 nt of ssDNA, and that DBD-D (RPA2) is needed for RPA to interact with substrates that are 23-27 nt in length (PMID:11479296)
• Partial reconstitution of human DNA mismatch repair in vitro: characterization of the role of human replication protein A (PMID:11884592)
• Autoantiboies to replication protein A is highly expressed and aberrantly localized in breast tumor cells (PMID:11895905)
• Human cell DNA replication is mediated by a discrete multiprotein complex. The eluted complex contains DNA polymerase delta, proliferating cell nuclear antigen, and replication protein A. (PMID:11968016)
• Human XPA and RPA DNA repair proteins participate in specific recognition of triplex-induced helical distortions (PMID:11972036)
• interacts with Parvovirus initiator protein NS1 to coordinate replication fork progression in a reconstituted DNA replication system. (PMID:12050365)
• Analysis of the human replication protein A:Rad52 complex: evidence for crosstalk between RPA32, RPA70, Rad52 and DNA (PMID:12139939)
• the multistep process of DNA damage recognition includes initiation by XPC-hHR23B, which is then replaced by the combined action of XPA and RPA (PMID:12486030)
• data suggest that RPA-coated ssDNA is the critical structure at sites of DNA damage that recruits the ATR-ATRIP complex and facilitates its recognition of substrates for phosphorylation and the initiation of checkpoint signaling (PMID:12791985)
• Human replication protein A, by engaging in both protein-protein and protein-DNA interactions, facilitates unwinding catalyzed by WRN helicase during DNA synthetic processes. (PMID:14499497)
• Single-stranded DNA (ssDNA) binding properties of the core domains (DBDs) of RPA are defined: DBD A is responsible for positioning and initial binding of the RPA complex while DBD A together with DBD B direct stable, high-affinity binding to ssDNA. (PMID:14596605)
• replication protein A (RPA) stimulates the binding of the Rad17-Rfc2-5 complex to single-stranded DNA (PMID:14605214)
• Papillomavirus 11 E1 protein interacts with the major ssDNA-binding domain of RPA; the interaction is substantially inhibited by ssDNA dependent on the length of the DNA (PMID:14747526)
• Results suggest that replication protein A (RPA)2 phosphorylation prevents RPA association with replication centers in vivo and potentially serves as a marker for sites of DNA damage. (PMID:14966274)
• RECQ1 alone is able to unwind short DNA duplexes (<110 bp), whereas considerably longer substrates (501 bp) can be unwound only in the presence of human replication protein A (hRPA) (PMID:15096578)
• Replication protein A, Mre11, Rad50 and Nbs1 bind and have roles in DNA repair (PMID:15180989)
• proposal that B-cell-specific AID-RPA complexes preferentially bind to ssDNA of small transcription bubbles at SHM ‘hotspots’, leading to AID-mediated deamination and RPA-mediated recruitment of DNA repair proteins (PMID:15273694)
• the role of RPA phosphorylation in the cellular response to DNA damage is to help regulate DNA metabolism and promote DNA repair [review] (PMID:15279788)
• results obtained in this study demonstrate that a combination of exhaustive proteolysis and MALDI TOF MS can localize the sites of DNA binding to very short sequences of amino acids (PMID:15456284)
• the Mre11/Rad50/Nbs1 (MRN) complex may play a more universal role in the recognition and response to DNA lesions of all types, whereas the role of RPA may be limited to certain subsets of lesions (PMID:15653682)
• CDK2 inhibition modifies the dynamics of chromatin-bound minichromosome maintenance complex and replication protein A (PMID:16082227)
• The results demonstrate that activation of a UV-induced DNA damage response pathway, involving phosphorylation of RPA p34 by DNA-PK, is enhanced in cells lacking poleta. (PMID:16520097)
• DNA polymerase lambda has the ability to create base pair mismatches and human replication protein A can suppress this intrinsic in vitro mutator phenotype. (PMID:16522650)
• phosphorylation alters the DNA binding affinity of RPA to fulfill its differential requirement at the various stages of DNA mismatch repair (PMID:16731533)
• The location of multiple amino acids within the native RPA three-dimensional structure using reactivity of these amino acids toward proteolytic and chemical modification reagents, is studied. (PMID:16893181)
• A mechanistic model is proposed in which the ternary complex is a key intermediate that directly couples origin DNA unwinding to RPA loading on emerging ssDNA. (PMID:17110927)
• an accurate mechanism exists to reduce the deleterious consequences of oxidative DNA damage, with an important role for PCNA and RP-A in determining a functional hierarchy among different DNA pols in lesion bypass (PMID:17507928)
• Determination at single-nucleotide resolution the relative positions of the single-stranded DNA with interacting intrinsic tryptophans of RPA70. (PMID:17583916)
• Data demonstrate that Mre11/Rad50/Nbs1 interacts with replication protein A in unperturbed cells, that the interaction is regulated by cyclin-dependent kinases, and that this interaction is needed for MRN to correctly localize to replication centers. (PMID:17591703)
• transcription-based stress response involving RPA, ATR, and p53 has evolved as a DNA damage-sensing mechanism to safeguard cells against DNA damage-induced mutagenesis (PMID:17616578)
• These data suggest that in response to DNA double-strand breaks, cell cycle-preferred repair pathways differentially engage RPA and the Mre11/Rad50/Nbs1 complex in repair foci. (PMID:17700069)
• These data support a role for RPA as an initial signal/sensor for DNA damage that facilitates recruitment of MRN and ATM/ATR to sites of damage, where they then work together to fully activate the DNA damage response. (PMID:17700070)
• Amino acid sequence conservation is not required for the conservation of dynamic behavior and presumably molecular function. (PMID:17721672)
• Data suggest a direct role of RPA in homologous recombination in assembly of the RAD51 and RAD52 proteins. (PMID:17765923)
• Observations strengthen the original pre-synaptic model, although the visualization of post-synaptic RPA foci may indicate the presence of a different role for this protein during homologous recombination. (PMID:17981954)
• NBS1 mediates ATR-dependent RPA hyperphosphorylation following replication fork stall and collapse. (PMID:18003706)
• RPA plays a regulatory role in DNA damage responses via repression of RFC2 ubiquitylation in human cells. (PMID:18245774)
• Recognition of new DNA nucleotide excision repair (NER) substrate analogs, 48-mer ddsDNA (damaged double-stranded DNA), by human replication protein A (hRPA) has been analyzed using fluorescence spectroscopy and photoaffinity modification. (PMID:18438969)
• as long as a threshold of RPA1-ssDNA binding activity is met, DNA replication can occur and that an RPA1 activity separate from ssDNA binding is essential for function in DNA repair. (PMID:18469000)
• RPA conformation is important for regulating RPA-DNA and RPA-protein interactions (PMID:18515800)

Cross-species orthologs

7 orthologs

Organism	Symbol	Gene ID
danio_rerio	rpa1	ENSDARG00000003938
mus_musculus	Rpa1	ENSMUSG00000000751
rattus_norvegicus	Rpa1	ENSRNOG00000003123
drosophila_melanogaster	RPA1	FBGN0010173
caenorhabditis_elegans		WBGENE00017546
caenorhabditis_elegans		WBGENE00019858
caenorhabditis_elegans		WBGENE00019859

Protein

Protein identifiers

Replication protein A 70 kDa DNA-binding subunit — P27694 (reviewed: P27694)

Alternative names: Replication factor A protein 1, Single-stranded DNA-binding protein

All UniProt accessions (4): P27694, I3L2M5, I3L4R8, I3L524

UniProt curated annotations — full annotation on UniProt →

Function. As 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. Also plays a role in base excision repair (BER) probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. Plays a role in telomere maintenance. As part of the alternative replication protein A complex, aRPA, binds single-stranded DNA and probably plays a role in DNA repair. Compared to the RPA2-containing, canonical RPA complex, may not support chromosomal DNA replication and cell cycle progression through S-phase. The aRPA may not promote efficient priming by DNA polymerase alpha but could support DNA synthesis by polymerase delta in presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange. RPA stimulates 5’-3’ helicase activity of the BRIP1/FANCJ.

Subunit / interactions. Component of the canonical replication protein A complex (RPA), a heterotrimer composed of RPA1, RPA2 and RPA3. Also a component of the aRPA, the alternative replication protein A complex, a trimeric complex similar to the replication protein A complex/RPA but where RPA1 and RPA3 are associated with RPA4 instead of RPA2. The DNA-binding activity may reside exclusively on the RPA1 subunit. Interacts with PRPF19; the PRP19-CDC5L complex is recruited to the sites of DNA repair where it ubiquitinates the replication protein A complex (RPA). Interacts with RIPK1. Interacts with the polymerase alpha subunit POLA1/p180; this interaction stabilizes the replicative complex and reduces the misincorporation rate of DNA polymerase alpha by acting as a fidelity clamp. Interacts with RAD51 and SENP6 to regulate DNA repair. Interacts with HELB; this interaction promotes HELB recruitment to chromatin following DNA damage. Interacts with PRIMPOL; leading to recruit PRIMPOL on chromatin and stimulate its DNA primase activity. Interacts with XPA; the interaction is direct and associates XPA with the RPA complex. Interacts with ETAA1; the interaction is direct and promotes ETAA1 recruitment at stalled replication forks. Interacts with RPA1; this interaction associates HROB with the RPA complex. Interacts (when poly-ADP-ribosylated) with HTATSF1. Interacts with BRIP1/FANCJ via this RPA1 subunit; following DNA damage they colocalize in foci in the nucleus.

Subcellular location. Nucleus. PML body.

Post-translational modifications. DNA damage-induced ‘Lys-63’-linked polyubiquitination by PRPF19 mediates ATRIP recruitment to the RPA complex at sites of DNA damage and activation of ATR. Ubiquitinated by RFWD3 at stalled replication forks in response to DNA damage: ubiquitination by RFWD3 does not lead to degradation by the proteasome and promotes removal of the RPA complex from stalled replication forks, promoting homologous recombination. Sumoylated on lysine residues Lys-449 and Lys-577, with Lys-449 being the major site. Sumoylation promotes recruitment of RAD51 to the DNA damage foci to initiate DNA repair through homologous recombination. Desumoylated by SENP6. Poly-ADP-ribosylated by PARP1; promoting recruitment of HTATSF1.

Disease relevance. Pulmonary fibrosis, and/or bone marrow failure syndrome, telomere-related, 6 (PFBMFT6) [MIM:619767] An autosomal dominant disease associated with shortened telomeres. Pulmonary fibrosis is the most common manifestation. Other manifestations include aplastic anemia due to bone marrow failure, hepatic fibrosis, and increased cancer risk, particularly myelodysplastic syndrome and acute myeloid leukemia. Phenotype, age at onset, and severity are determined by telomere length. The disease is caused by variants affecting the gene represented in this entry.

Similarity. Belongs to the replication factor A protein 1 family.

RefSeq proteins (3): NP_001342049, NP_001342050, NP_002936* (*=MANE)

Domains & families (InterPro)

ID	Name	Type
IPR004365	NA-bd_OB_tRNA	Domain
IPR004591	Rfa1	Family
IPR007199	Rep_factor-A_N	Domain
IPR012340	NA-bd_OB-fold	Homologous_superfamily
IPR013955	Rep_factor-A_C	Domain
IPR031657	REPA_OB_2	Domain
IPR047192	Euk_RPA1_DBD_C	Domain

Pfam: PF01336, PF04057, PF08646, PF16900

UniProt features (100 total): strand 36, helix 17, cross-link 16, modified residue 7, turn 7, mutagenesis site 6, sequence variant 4, chain 2, initiator methionine 1, DNA-binding region 1, zinc finger region 1, region of interest 1, compositionally biased region 1

Structure

Experimental structures (PDB)

42 structures, top 30 by resolution.

PDB	Method	Resolution (Å)
4O0A	X-RAY DIFFRACTION	1.2
5E7N	X-RAY DIFFRACTION	1.21
4IPC	X-RAY DIFFRACTION	1.22
4R4T	X-RAY DIFFRACTION	1.28
5N8A	X-RAY DIFFRACTION	1.28
4R4O	X-RAY DIFFRACTION	1.33
4NB3	X-RAY DIFFRACTION	1.35
4R4Q	X-RAY DIFFRACTION	1.35
4LUV	X-RAY DIFFRACTION	1.4
4R4C	X-RAY DIFFRACTION	1.4
4R4I	X-RAY DIFFRACTION	1.4
8K00	X-RAY DIFFRACTION	1.4
4IJH	X-RAY DIFFRACTION	1.5
7XV0	X-RAY DIFFRACTION	1.5
8JZV	X-RAY DIFFRACTION	1.5
8JZY	X-RAY DIFFRACTION	1.5
4IPD	X-RAY DIFFRACTION	1.51
4LUO	X-RAY DIFFRACTION	1.54
5EAY	X-RAY DIFFRACTION	1.55
9J1S	X-RAY DIFFRACTION	1.55
4IPG	X-RAY DIFFRACTION	1.58
2B29	X-RAY DIFFRACTION	1.6
2B3G	X-RAY DIFFRACTION	1.6
7XUT	X-RAY DIFFRACTION	1.6
7XUV	X-RAY DIFFRACTION	1.6
7XV4	X-RAY DIFFRACTION	1.6
4LWC	X-RAY DIFFRACTION	1.61
4LW1	X-RAY DIFFRACTION	1.63
4IJL	X-RAY DIFFRACTION	1.7
7XUW	X-RAY DIFFRACTION	1.8

Predicted structure (AlphaFold)

Model	pLDDT	Fraction very-high
AF-P27694-F1	84.99	0.63

Functional residue map

Curated UniProt residues grouped by drug-discovery relevance — catalytic, ligand-binding, modification, and mutation-validated positions. Source: UniProtKB sequence features.

Post-translational modifications (23): 180, 191, 259, 384, 22, 88, 163, 167, 183, 220, 244, 259, 267, 331, 410, 431, 449, 458, 553, 577 …

Mutagenesis-validated functional residues (6):

Position	Phenotype
41	loss of helb-binding; when associated with e-43.
43	loss of helb-binding; when associated with e-41.
449	significant reduction of sumoylation. loss of sumoylation; when associated with r-577.
500	loss of function in dna replication and mismatch repair without effect on dna-binding activity; when associated with s-5
503	loss of function in dna replication and mismatch repair without effect on dna-binding activity; when associated with s-5
577	slight sumoylation decrease. loss of sumoylation; when associated with r-449.

Function

Pathways and Gene Ontology

Reactome pathways

30 pathways

ID	Pathway
R-HSA-110312	Translesion synthesis by REV1
R-HSA-110314	Recognition of DNA damage by PCNA-containing replication complex
R-HSA-110320	Translesion Synthesis by POLH
R-HSA-174437	Removal of the Flap Intermediate from the C-strand
R-HSA-176187	Activation of ATR in response to replication stress
R-HSA-3108214	SUMOylation of DNA damage response and repair proteins
R-HSA-3371453	Regulation of HSF1-mediated heat shock response
R-HSA-3371511	HSF1 activation
R-HSA-5358565	Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)
R-HSA-5358606	Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta)
R-HSA-5651801	PCNA-Dependent Long Patch Base Excision Repair
R-HSA-5655862	Translesion synthesis by POLK
R-HSA-5656121	Translesion synthesis by POLI
R-HSA-5656169	Termination of translesion DNA synthesis
R-HSA-5685938	HDR through Single Strand Annealing (SSA)
R-HSA-5685942	HDR through Homologous Recombination (HRR)
R-HSA-5693607	Processing of DNA double-strand break ends
R-HSA-5693616	Presynaptic phase of homologous DNA pairing and strand exchange
R-HSA-5696395	Formation of Incision Complex in GG-NER
R-HSA-5696397	Gap-filling DNA repair synthesis and ligation in GG-NER
R-HSA-5696400	Dual Incision in GG-NER
R-HSA-6782135	Dual incision in TC-NER
R-HSA-6782210	Gap-filling DNA repair synthesis and ligation in TC-NER
R-HSA-6783310	Fanconi Anemia Pathway
R-HSA-6804756	Regulation of TP53 Activity through Phosphorylation
R-HSA-68962	Activation of the pre-replicative complex
R-HSA-69166	Removal of the Flap Intermediate
R-HSA-69473	G2/M DNA damage checkpoint
R-HSA-912446	Meiotic recombination
R-HSA-9709570	Impaired BRCA2 binding to RAD51

MSigDB gene sets: 480 (showing top): PID_FANCONI_PATHWAY, REACTOME_FORMATION_OF_INCISION_COMPLEX_IN_GG_NER, MORF_MTA1, GOBP_RNA_TEMPLATED_DNA_BIOSYNTHETIC_PROCESS, REACTOME_MEIOTIC_RECOMBINATION, GOBP_CHROMOSOME_ORGANIZATION, REACTOME_DNA_REPLICATION, BORCZUK_MALIGNANT_MESOTHELIOMA_UP, GOBP_EMBRYO_DEVELOPMENT_ENDING_IN_BIRTH_OR_EGG_HATCHING, MODULE_451, KAAB_FAILED_HEART_ATRIUM_DN, REACTOME_G2_M_DNA_DAMAGE_CHECKPOINT, MORF_RAD21, REACTOME_ACTIVATION_OF_ATR_IN_RESPONSE_TO_REPLICATION_STRESS, GOBP_TELOMERE_MAINTENANCE_VIA_TELOMERE_LENGTHENING

GO Biological Process (20): telomere maintenance (GO:0000723), double-strand break repair via homologous recombination (GO:0000724), in utero embryonic development (GO:0001701), DNA replication (GO:0006260), DNA-templated DNA replication (GO:0006261), DNA repair (GO:0006281), base-excision repair (GO:0006284), nucleotide-excision repair (GO:0006289), mismatch repair (GO:0006298), DNA recombination (GO:0006310), DNA damage response (GO:0006974), telomere maintenance via telomerase (GO:0007004), positive regulation of cell population proliferation (GO:0008284), hemopoiesis (GO:0030097), protein localization to chromosome (GO:0034502), homeostasis of number of cells within a tissue (GO:0048873), meiotic cell cycle (GO:0051321), protein localization to site of double-strand break (GO:1990166), chromatin organization (GO:0006325), chromosome organization (GO:0051276)

GO Molecular Function (11): chromatin binding (GO:0003682), damaged DNA binding (GO:0003684), single-stranded DNA binding (GO:0003697), zinc ion binding (GO:0008270), single-stranded telomeric DNA binding (GO:0043047), G-rich strand telomeric DNA binding (GO:0098505), chromatin-protein adaptor activity (GO:0140463), nucleic acid binding (GO:0003676), DNA binding (GO:0003677), protein binding (GO:0005515), metal ion binding (GO:0046872)

GO Cellular Component (12): chromosome, telomeric region (GO:0000781), lateral element (GO:0000800), male germ cell nucleus (GO:0001673), nucleus (GO:0005634), nucleoplasm (GO:0005654), DNA replication factor A complex (GO:0005662), PML body (GO:0016605), site of double-strand break (GO:0035861), site of DNA damage (GO:0090734), nuclear chromosome (GO:0000228), condensed chromosome (GO:0000793), condensed nuclear chromosome (GO:0000794)

Reactome top-level categories

Rollup of top-11 pathways:

Category	Pathways
Translesion synthesis by Y family DNA polymerases bypasses lesions on DNA template	5
HDR through Homologous Recombination (HRR) or Single Strand Annealing (SSA)	3
Cellular response to heat stress	2
Mismatch Repair	2
Global Genome Nucleotide Excision Repair (GG-NER)	2
DNA Damage Bypass	1
Processive synthesis on the C-strand of the telomere	1
G2/M Checkpoints	1
SUMO E3 ligases SUMOylate target proteins	1
Resolution of AP sites via the multiple-nucleotide patch replacement pathway	1
Homologous DNA Pairing and Strand Exchange	1

GO top-level categories

Rollup of top GO terms by namespace:

Category	Terms
DNA metabolic process	4
DNA repair	3
binding	3
cellular anatomical structure	3
chromosome	3
DNA binding	2
nuclear lumen	2
nucleus	2
telomere organization	1
recombinational repair	1
double-strand break repair	1
chordate embryonic development	1
DNA biosynthetic process	1
DNA replication	1
DNA damage response	1
cellular response to stress	1
telomerase activity	1
RNA-templated DNA biosynthetic process	1
telomere maintenance via telomere lengthening	1
telomere-telomerase complex assembly	1
cell population proliferation	1
regulation of cell population proliferation	1
positive regulation of cellular process	1
cell development	1
protein localization to organelle	1
tissue homeostasis	1
homeostasis of number of cells	1
cell cycle	1
sexual reproduction	1
reproductive process	1
meiotic nuclear division	1
protein localization to chromosome	1
cellular component organization	1
organelle organization	1
transition metal ion binding	1
telomeric repeat DNA binding	1
sequence-specific single stranded DNA binding	1
single-stranded telomeric DNA binding	1
chromatin binding	1
chromatin organization	1

Protein interactions and networks

STRING

2901 interactions, top by confidence (×1000):

Protein A	Protein B	Partner UniProt	Score
RPA1	RPA2	P15927	999
RPA1	RPA3	P35244	997
RPA1	STN1	Q9H668	997
RPA1	ATRIP	Q8WXE1	983
RPA1	TP53	P04637	932
RPA1	RAD9A	Q99638	899
RPA1	RAD51	Q06609	838
RPA1	XPA	P23025	808
RPA1	RAD17	O75943	797
RPA1	EXO1	Q9UQ84	785
RPA1	DNA2	P51530	782
RPA1	BRIP1	Q9BX63	773
RPA1	XRCC6	P12956	749
RPA1	WRN	Q14191	749
RPA1	RBBP8	Q99708	733

IntAct

266 interactions, top by confidence:

A	B	Type	Score
RPA2	RPA1	psi-mi:“MI:0914”(association)	0.960
RPA1	RPA2	psi-mi:“MI:0915”(physical association)	0.960
RPA1	RPA2	psi-mi:“MI:0914”(association)	0.960
RPA2	RPA1	psi-mi:“MI:0915”(physical association)	0.960
RPA3	RPA2	psi-mi:“MI:0914”(association)	0.930
XPA	ERCC1	psi-mi:“MI:0914”(association)	0.930
XPA	RPA2	psi-mi:“MI:0914”(association)	0.920
RPA1	RPA3	psi-mi:“MI:0914”(association)	0.920
RPA1	RPA3	psi-mi:“MI:0915”(physical association)	0.920
RB1CC1	ATG13	psi-mi:“MI:0914”(association)	0.820
RNF146	TNKS	psi-mi:“MI:0914”(association)	0.790
RPA1	RPA4	psi-mi:“MI:0915”(physical association)	0.740
RPA4	RPA1	psi-mi:“MI:0914”(association)	0.740
XPA	HERC2	psi-mi:“MI:0914”(association)	0.680
BRCA1	RPA1	psi-mi:“MI:0915”(physical association)	0.650
BLM	RPA2	psi-mi:“MI:0914”(association)	0.640
RPA1	PRIMPOL	psi-mi:“MI:0915”(physical association)	0.620

BioGRID (3821): RPA1 (Affinity Capture-MS), RPA1 (Affinity Capture-Western), RPA1 (Affinity Capture-Western), RPA1 (Affinity Capture-MS), MTUS2 (Two-hybrid), RPA1 (Affinity Capture-Western), RPA1 (Affinity Capture-MS), RPA1 (Affinity Capture-MS), RPA2 (Two-hybrid), RPA4 (Two-hybrid), RPA1 (Affinity Capture-MS), RPA1 (Affinity Capture-MS), RPA1 (Affinity Capture-MS), RPA1 (Affinity Capture-MS), RPA1 (Affinity Capture-MS)

ESM2 similar proteins: A1L4Y1, A2QCJ2, B8A5I7, F1QR43, F4JP46, P09380, P09381, P27694, P28042, P32445, P35244, P41345, P59931, P59933, P78586, Q01217, Q04837, Q0JJS8, Q28EX9, Q2KJD7, Q32PB0, Q40089, Q4IBU4, Q4X0Z7, Q5AZT7, Q5FW17, Q5FWT7, Q5R4C4, Q5R7Q4, Q5R8R4, Q5RDQ0, Q5ZJJ8, Q641F1, Q69YN2, Q6DI37, Q6NLG7, Q6NWD4, Q6P4T2, Q6STH5, Q7S8C4

Diamond homologs: F4JSG3, P22336, P27694, Q01588, Q10Q08, Q23696, Q24492, Q5FW17, Q5R7Q4, Q5ZJJ2, Q65XV7, Q6NY74, Q6YZ49, Q8VEE4, Q92372, Q9FHJ6, Q9FME0, Q9SD82, Q9SKI4, O97472, Q19537

SIGNOR signaling

9 interactions.

A	Effect	B	Mechanism
RPA1	“up-regulates activity”	BRIP1	binding
PRPF19	“up-regulates activity”	RPA1	polyubiquitination
PAK1	“up-regulates activity”	RPA1	phosphorylation
RPA1	“up-regulates activity”	POLA1	binding
POT1	“down-regulates activity”	RPA1	binding
ACD	“down-regulates activity”	RPA1	binding
RAD23B	“up-regulates activity”	RPA1	binding
RPA1	up-regulates	Nucleotide-excision_repair

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 165 IntAct physical interaction partners (hypergeometric vs the genome-wide background, BH-FDR, gene-set size 15–500, ranked by fold). A functional readout of the neighbourhood — distinct from this gene’s own memberships above, and biased toward well-studied / hub proteins, so read it as themes rather than proof.

Reactome pathways:

Pathway	Partners	Fold	FDR
Impaired BRCA2 binding to PALB2	6	22.3×	3e-05
Defective homologous recombination repair (HRR) due to BRCA1 loss of function	6	20.6×	3e-05
Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function	6	20.6×	3e-05
Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function	6	20.6×	3e-05
Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA)	6	19.2×	4e-05
Homologous DNA Pairing and Strand Exchange	6	18.6×	5e-05
Presynaptic phase of homologous DNA pairing and strand exchange	8	17.7×	9e-06
Impaired BRCA2 binding to RAD51	7	17.6×	3e-05

GO biological processes:

GO term	Partners	Fold	FDR
double-strand break repair via nonhomologous end joining	7	20.2×	2e-05
nucleotide-excision repair	7	18.4×	3e-05
double-strand break repair via homologous recombination	12	12.8×	2e-07
DNA recombination	5	11.5×	9e-03
DNA repair	15	6.6×	7e-06
DNA damage response	12	4.4×	3e-03

Disease & clinical

Clinical variants and AI predictions

ClinVar

116 variants total. Per-class counts are floors (≥ shown; pagination cap):

Classification	Count (floor)
Pathogenic	2
Likely pathogenic	0
Uncertain significance	75
Likely benign	7
Benign	9

Top pathogenic / likely-pathogenic (2)

Variant ID	HGVS	Classification
1342931	NM_002945.5(RPA1):c.718G>A (p.Glu240Lys)	Pathogenic
1342932	NM_002945.5(RPA1):c.680T>C (p.Val227Ala)	Pathogenic

SpliceAI

2949 predictions. Top by Δscore:

Variant	Effect	Δscore
17:1830074:G:GT	donor_gain	1.0000
17:1830074:G:T	donor_gain	1.0000
17:1830132:G:GT	donor_gain	1.0000
17:1842797:CCTCA:C	acceptor_loss	1.0000
17:1842798:CTCAG:C	acceptor_loss	1.0000
17:1842799:TCAG:T	acceptor_loss	1.0000
17:1842800:CAG:C	acceptor_loss	1.0000
17:1842801:A:AG	acceptor_gain	1.0000
17:1842801:AGGCC:A	acceptor_loss	1.0000
17:1842802:G:C	acceptor_loss	1.0000
17:1842802:G:GA	acceptor_gain	1.0000
17:1842802:GGCC:G	acceptor_gain	1.0000
17:1842854:G:GG	donor_gain	1.0000
17:1843918:A:AG	acceptor_gain	1.0000
17:1843919:G:GG	acceptor_gain	1.0000
17:1843919:GA:G	acceptor_gain	1.0000
17:1843919:GAAC:G	acceptor_gain	1.0000
17:1844576:A:AG	acceptor_gain	1.0000
17:1844577:G:GG	acceptor_gain	1.0000
17:1844577:GC:G	acceptor_gain	1.0000
17:1844577:GCT:G	acceptor_gain	1.0000
17:1844577:GCTTT:G	acceptor_gain	1.0000
17:1844682:GGAAG:G	donor_gain	1.0000
17:1844683:GAAGG:G	donor_gain	1.0000
17:1844685:AGG:A	donor_loss	1.0000
17:1844686:GGTA:G	donor_loss	1.0000
17:1844687:G:GC	donor_loss	1.0000
17:1844688:T:G	donor_loss	1.0000
17:1853090:T:A	acceptor_gain	1.0000
17:1853097:GCAGG:G	acceptor_loss	1.0000

AlphaMissense

4072 scored. Top likely-pathogenic:

Variant	Protein change	am_pathogenicity
17:1877213:T:A	W197R	1.000
17:1877213:T:C	W197R	1.000
17:1877232:T:A	V203D	1.000
17:1877258:T:A	W212R	1.000
17:1877258:T:C	W212R	1.000
17:1879014:T:C	F238L	1.000
17:1879016:C:A	F238L	1.000
17:1879016:C:G	F238L	1.000
17:1879688:T:A	W361R	1.000
17:1879688:T:C	W361R	1.000
17:1879690:G:C	W361C	1.000
17:1879690:G:T	W361C	1.000
17:1880606:T:C	F386L	1.000
17:1880608:C:A	F386L	1.000
17:1880608:C:G	F386L	1.000
17:1888732:T:C	Y478H	1.000
17:1888739:C:A	A480D	1.000
17:1888741:T:C	C481R	1.000
17:1888798:T:C	C500R	1.000
17:1888838:G:C	R513P	1.000
17:1891875:T:C	F532L	1.000
17:1891876:T:G	F532C	1.000
17:1891877:C:A	F532L	1.000
17:1891877:C:G	F532L	1.000
17:1842843:T:C	L25P	0.999
17:1843963:G:C	R43P	0.999
17:1843974:A:C	S47R	0.999
17:1843976:T:A	S47R	0.999
17:1843976:T:G	S47R	0.999
17:1843977:G:C	D48H	0.999

dbSNP variants (sampled 300 via entrez): RS1000044210 (17:1829893 G>GA), RS1000048285 (17:1866466 C>T), RS1000058811 (17:1890194 A>G), RS1000144585 (17:1854516 C>T), RS1000149838 (17:1894153 G>A), RS1000215305 (17:1860719 G>A), RS1000266833 (17:1861505 G>A), RS1000275905 (17:1898280 G>T), RS1000281539 (17:1898479 G>A,C,T), RS1000303083 (17:1855315 C>A), RS1000312728 (17:1873235 T>C), RS1000393729 (17:1873558 C>G), RS1000422075 (17:1828737 C>T), RS1000426178 (17:1866807 A>G), RS1000516755 (17:1854242 A>G)

Disease associations

OMIM: gene MIM:179835 | disease phenotypes: MIM:619767

GenCC curated gene-disease

Disease	Classification	Inheritance
pulmonary fibrosis and/or bone marrow failure, telomere-related, 6	Strong	Autosomal dominant

ClinGen Gene-Disease Validity (1)

Expert-panel classifications — Definitive > Strong > Moderate > Limited > Disputed > Refuted.

Disease	Classification	Inheritance
dyskeratosis congenita and related telomere biology disorder	Limited	AD

Mondo (1): pulmonary fibrosis and/or bone marrow failure, telomere-related, 6 (MONDO:0030690)

Orphanet (0):

HPO phenotypes

17 total (17 of 17 shown, HPO-id order):

HPO	Term
HP:0000006	Autosomal dominant inheritance
HP:0001876	Pancytopenia
HP:0001888	Decreased total lymphocyte count
HP:0002091	Restrictive ventilatory defect
HP:0002206	Pulmonary fibrosis
HP:0002216	Premature graying of hair
HP:0002745	Oral leukoplakia
HP:0002863	Myelodysplasia
HP:0003577	Congenital onset
HP:0003596	Middle age onset
HP:0003621	Juvenile onset
HP:0004313	Decreased circulating immunoglobulin concentration
HP:0005528	Bone marrow hypocellularity
HP:0007588	Reticular hyperpigmentation
HP:0008404	Nail dystrophy
HP:0031413	Short telomere length
HP:0031545	Abnormally low T cell receptor excision circle level

GWAS associations

0 associations (top):

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (2): CHEMBL1764940 (SINGLE PROTEIN), CHEMBL3885545 (PROTEIN-PROTEIN INTERACTION)

PharmGKB: 1 entry (VIP=true, CPIC=false)

Binding affinities (BindingDB)

5 measured of 7 human assays (7 total across all organisms); most potent 5 below. Values come from heterogeneous assays and are not directly comparable.

Ligand	Measure	Value	Patent
4-[5-(4-bromophenyl)-3-(2-chloro-7-ethoxyquinolin-3-yl)-3,4-dihydropyrazol-2-yl]-4-oxobutanoic acid	IC50	12900 nM	US-9533969: Materials and method for inhibiting replication protein A and uses thereof
CHEMBL2407442	KD	18300 nM
4-[5-(4-methylphenyl)-3-[3-(4-methylphenyl)-1-phenyl-4-pyrazolyl]-3,4-dihydropyrazol-2-yl]-4-oxobutanoic acid	IC50	20300 nM	US-9533969: Materials and method for inhibiting replication protein A and uses thereof
4-[5-(4-bromophenyl)-3-[3-(4-methylphenyl)-1-phenylpyrazol-4-yl]-3,4-dihydropyrazol-2-yl]-4-oxobutanoic acid	IC50	56100 nM	US-9533969: Materials and method for inhibiting replication protein A and uses thereof
4-[5-(4-methoxyphenyl)-3-[3-(4-methylphenyl)-1-phenylpyrazol-4-yl]-3,4-dihydropyrazol-2-yl]-4-oxobutanoic acid	IC50	71700 nM	US-9533969: Materials and method for inhibiting replication protein A and uses thereof

ChEMBL bioactivities

73 potent at pChembl≥5 of 128 total, top 50 by pChembl (potency: 10 = 0.1 nM, 6 = 1 µM).

pChembl	Type	Value	Unit	Molecule
9.32	Kd	0.48	nM	CHEMBL3422471
9.27	Kd	0.54	nM	CHEMBL3422472
9.26	Kd	0.55	nM	CHEMBL3422469
8.82	Kd	1.5	nM	CHEMBL3422468
8.77	Kd	1.7	nM	CHEMBL3422476
8.66	Kd	2.2	nM	CHEMBL3422474
8.60	Kd	2.5	nM	CHEMBL3422467
8.09	Kd	8.2	nM	CHEMBL3422465
8.03	Kd	9.3	nM	CHEMBL3422475
8.03	Kd	9.4	nM	CHEMBL3422470
7.99	Kd	10.36	nM	CHEMBL5653589
7.99	ED50	10.36	nM	CHEMBL5653589
7.82	Kd	15	nM	CHEMBL3422461
7.75	Kd	18	nM	CHEMBL3422459
7.66	Kd	22	nM	CHEMBL3236301
7.66	Kd	22	nM	CHEMBL3422466
7.64	Kd	23	nM	CHEMBL3422460
7.47	Kd	34	nM	CHEMBL3422473
7.46	Kd	35	nM	CHEMBL3422458
7.38	Kd	42	nM	CHEMBL3236545
7.35	Kd	45	nM	CHEMBL3422456
7.32	Kd	48	nM	CHEMBL3236544
7.27	Kd	54	nM	CHEMBL3422435
7.25	Kd	56	nM	CHEMBL3422463
7.24	Kd	57	nM	CHEMBL3422464
7.23	Kd	59	nM	CHEMBL3422448
7.17	Kd	67	nM	CHEMBL3422435
7.16	Kd	70	nM	CHEMBL3422462
7.14	Kd	72	nM	CHEMBL3422457
7.14	Kd	72	nM	CHEMBL3422446
7.10	Kd	79	nM	CHEMBL3422442
7.08	Kd	83	nM	CHEMBL3422455
7.05	Kd	90	nM	CHEMBL3421641
7.05	Kd	90	nM	CHEMBL3422445
6.98	Kd	104	nM	CHEMBL3422452
6.91	Kd	123	nM	CHEMBL3422444
6.89	Kd	129	nM	CHEMBL3422447
6.85	Kd	140	nM	CHEMBL3422438
6.72	Kd	190	nM	CHEMBL3088230
6.64	Kd	227	nM	CHEMBL3422451
6.58	Kd	260	nM	CHEMBL1576514
6.54	Kd	290	nM	CHEMBL3088230
6.51	Kd	310	nM	CHEMBL3422449
6.49	Kd	323	nM	CHEMBL3088230
6.48	Kd	330	nM	CHEMBL3236299
6.39	Kd	410	nM	CHEMBL3422434
6.32	Kd	480	nM	CHEMBL3236288
6.24	Kd	580	nM	CHEMBL3236298
6.24	Kd	570	nM	CHEMBL3236302
6.24	Kd	580	nM	CHEMBL3088227

PubChem BioAssay actives

72 with measured affinity, of 188 total; 50 most potent distinct compounds. Largely complementary to BindingDB; screening values are coarse (µM, 4 dp), so sub-nM hits tie at the floor.

Compound	Assay	Type	Value	Unit
5-[4-[[4-(5-carboxyfuran-2-yl)-2-chlorophenyl]methylcarbamothioyl]phenyl]-1-(3,4-dichlorophenyl)pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0005	uM
5-[4-[[6-(5-carboxyfuran-2-yl)-1-sulfanylidene-3,4-dihydroisoquinolin-2-yl]methyl]phenyl]-1-(3,4-dichlorophenyl)pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0005	uM
5-[4-[[[4-(5-carboxyfuran-2-yl)benzenecarbothioyl]amino]methyl]phenyl]-1-(3,4-dichlorophenyl)pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0006	uM
5-[4-[[4-(5-carboxyfuran-2-yl)phenyl]methylcarbamothioyl]phenyl]-1-(3,4-dichlorophenyl)pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0015	uM
5-[3-chloro-4-[[4-[2-(3,4-dichlorophenyl)pyrazol-3-yl]phenyl]methylcarbamothioyl]phenyl]furan-2-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0017	uM
1-(3,4-dichlorophenyl)-5-[4-[[[4-(2H-tetrazol-5-yl)benzenecarbothioyl]amino]methyl]phenyl]pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0022	uM
5-[4-[[3-(5-carboxyfuran-2-yl)phenyl]methylcarbamothioyl]phenyl]-1-(3,4-dichlorophenyl)pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0025	uM
5-[3-[[acetyl-[[4-(5-carboxyfuran-2-yl)phenyl]methyl]amino]methyl]phenyl]-1-(3,4-dichlorophenyl)pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0082	uM
1-(3,4-dichlorophenyl)-5-[4-[[[4-(5-oxo-4H-1,2,4-oxadiazol-3-yl)benzenecarbothioyl]amino]methyl]phenyl]pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0093	uM
5-[4-[[4-(5-carboxyfuran-2-yl)-2-chlorophenyl]methylcarbamoyl]phenyl]-1-(3,4-dichlorophenyl)pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0094	uM
4-methyl-3-[(2-methyl-6-pyridin-3-ylpyrazolo[3,4-d]pyrimidin-4-yl)amino]-N-[3-(trifluoromethyl)phenyl]benzamide	2149236: Binding affinity to human RPA1 incubated for 45 mins by Kinobead based pull down assay	kd	0.0104	uM
5-[4-[[(4-bromobenzenecarbothioyl)amino]methyl]phenyl]-1-(3,4-dichlorophenyl)pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0150	uM
5-[4-(benzylcarbamothioyl)phenyl]-1-(3,4-dichlorophenyl)pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0180	uM
5-[3-[[4-(5-carboxyfuran-2-yl)phenyl]methylcarbamoyl]phenyl]-1-(3,4-dichlorophenyl)pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0220	uM
5-[[(2S)-1-[[(2S)-1-[[(2S,3R)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-amino-4-methyl-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]amino]-3-(3,4-dichlorophenyl)-1-oxopropan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]carbamothioylamino]-2-(3-hydroxy-6-oxoxanthen-9-yl)benzoic acid	1127879: Binding affinity to recombinant human RPA70 N-terminal domain (1 to 120 amino acids) expressed in Escherichia coli BL21-DE3 by fluorescence polarization anisotropy assay	kd	0.0220	uM
1-(3,4-dichlorophenyl)-5-[4-[(4-methoxyphenyl)methylcarbamothioyl]phenyl]pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0230	uM
1-(3,4-dichlorophenyl)-5-[4-[[(4-sulfamoylbenzenecarbothioyl)amino]methyl]phenyl]pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0340	uM
5-[4-[[(4-bromobenzoyl)amino]methyl]phenyl]-1-(3,4-dichlorophenyl)pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0350	uM
5-[[(2S)-4-amino-1-[[(2S)-1-[[(2S,3R)-1-[[(2S)-1-[[(3S,6S,9S,12R,16Z,21R)-9-(2-amino-2-oxoethyl)-3-(2-carboxyethyl)-21-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(1S)-1-carboxy-3-methylbutyl]amino]-1-oxopropan-2-yl]amino]-3-(3,4-dichlorophenyl)-1-oxopropan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]carbamoyl]-12,21-dimethyl-6-(2-methylpropyl)-2,5,8,11-tetraoxo-1,4,7,10-tetrazacyclohenicos-16-en-12-yl]amino]-1-oxopropan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-1,4-dioxobutan-2-yl]carbamothioylamino]-2-(3-hydroxy-6-oxoxanthen-9-yl)benzoic acid	1127879: Binding affinity to recombinant human RPA70 N-terminal domain (1 to 120 amino acids) expressed in Escherichia coli BL21-DE3 by fluorescence polarization anisotropy assay	kd	0.0420	uM
1-(3,4-dichlorophenyl)-5-[4-[(4-methoxyphenyl)methylcarbamoyl]phenyl]pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0450	uM
5-[[(2S)-4-amino-1-[[(2S)-1-[[(2S,3R)-1-[[(2S)-1-[[(3S,6S,9S,12R,16Z,21R)-3-(2-carboxyethyl)-9-(carboxymethyl)-21-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(1S)-1-carboxy-3-methylbutyl]amino]-1-oxopropan-2-yl]amino]-3-(3,4-dichlorophenyl)-1-oxopropan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]carbamoyl]-12,21-dimethyl-6-(2-methylpropyl)-2,5,8,11-tetraoxo-1,4,7,10-tetrazacyclohenicos-16-en-12-yl]amino]-1-oxopropan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-1,4-dioxobutan-2-yl]carbamothioylamino]-2-(3-hydroxy-6-oxoxanthen-9-yl)benzoic acid	1127879: Binding affinity to recombinant human RPA70 N-terminal domain (1 to 120 amino acids) expressed in Escherichia coli BL21-DE3 by fluorescence polarization anisotropy assay	kd	0.0480	uM
5-(4-chlorophenyl)-1-(3,4-dichlorophenyl)pyrazole-3-carboxylic acid	1202917: Binding affinity to RPA70N protein (unknown origin) by HSQC NMR-based titration method	kd	0.0540	uM
1-(3,4-dichlorophenyl)-5-[4-[[[4-(trifluoromethoxy)phenyl]sulfonylamino]methyl]phenyl]pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0560	uM
5-[3-[[[4-(5-carboxyfuran-2-yl)phenyl]methylamino]methyl]phenyl]-1-(3,4-dichlorophenyl)pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0570	uM
5-(4-carboxyphenyl)-1-(3,4-dichlorophenyl)pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0590	uM
5-[4-(benzenesulfonamidomethyl)phenyl]-1-(3,4-dichlorophenyl)pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0700	uM
1-(3,4-dichlorophenyl)-5-[4-[[(4-methoxybenzoyl)amino]methyl]phenyl]pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0720	uM
1-(3,4-dichlorophenyl)-5-(4-methylphenyl)pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0720	uM
1-(3,4-dichlorophenyl)-5-(4-methoxyphenyl)pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0790	uM
5-[4-(benzylcarbamoyl)phenyl]-1-(3,4-dichlorophenyl)pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0830	uM
1-(3,4-dichlorophenyl)-5-(3-methylphenyl)pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0900	uM
5-[4-(benzamidomethyl)phenyl]-1-(3,4-dichlorophenyl)pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.0900	uM
1-(3,4-dichlorophenyl)-5-(4-hydroxyphenyl)pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.1040	uM
1-(3,4-dichlorophenyl)-5-phenylpyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.1230	uM
5-(3-carboxyphenyl)-1-(3,4-dichlorophenyl)pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.1290	uM
1-(3-bromophenyl)-5-(4-methoxyphenyl)pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.1400	uM
5-[4-[[[4-(5-carboxyfuran-2-yl)-2-chlorobenzenecarbothioyl]amino]methyl]phenyl]-1-(3,4-dichlorophenyl)pyrazole-3-carboxylic acid	1054755: Displacement of FITC-ATRIP2 from RPA70N (1 to 120) (unknown origin) by FPA assay	kd	0.1900	uM
5-(4-aminophenyl)-1-(3,4-dichlorophenyl)pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.2270	uM
1,5-bis(4-chlorophenyl)pyrazole-3-carboxylic acid	1202917: Binding affinity to RPA70N protein (unknown origin) by HSQC NMR-based titration method	kd	0.2600	uM
5-(4-cyanophenyl)-1-(3,4-dichlorophenyl)pyrazole-3-carboxylic acid	1202918: Binding affinity to RPA70N protein (unknown origin) incubated for 1 hr using FITC-ATRIP/FITC-ATRIP2 peptide probe by fluorescence polarization anisotropy assay	kd	0.3100	uM
5-[[(2S)-1-[[(2S)-1-[[(2S,3R)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-amino-4-methyl-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]carbamothioylamino]-2-(3-hydroxy-6-oxoxanthen-9-yl)benzoic acid	1127879: Binding affinity to recombinant human RPA70 N-terminal domain (1 to 120 amino acids) expressed in Escherichia coli BL21-DE3 by fluorescence polarization anisotropy assay	kd	0.3300	uM
5-(4-chlorophenyl)-1-(2,4-dichlorophenyl)pyrazole-3-carboxylic acid	1202917: Binding affinity to RPA70N protein (unknown origin) by HSQC NMR-based titration method	kd	0.4100	uM
5-[[(2S)-1-[[(2S)-1-[[(2S,3R)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-amino-3-hydroxy-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]carbamothioylamino]-2-(3-hydroxy-6-oxoxanthen-9-yl)benzoic acid	1127879: Binding affinity to recombinant human RPA70 N-terminal domain (1 to 120 amino acids) expressed in Escherichia coli BL21-DE3 by fluorescence polarization anisotropy assay	kd	0.4800	uM
5-[[(2S)-3-carboxy-1-[[(2S)-1-[[(2S,3R)-1-[[(2S)-1-[[(3S,6S,9S,12R,16Z,21R)-3-(2-carboxyethyl)-9-(carboxymethyl)-21-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(1S)-1-carboxy-3-methylbutyl]amino]-1-oxopropan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]carbamoyl]-12,21-dimethyl-6-(2-methylpropyl)-2,5,8,11-tetraoxo-1,4,7,10-tetrazacyclohenicos-16-en-12-yl]amino]-1-oxopropan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-1-oxopropan-2-yl]carbamothioylamino]-2-(3-hydroxy-6-oxoxanthen-9-yl)benzoic acid	1127879: Binding affinity to recombinant human RPA70 N-terminal domain (1 to 120 amino acids) expressed in Escherichia coli BL21-DE3 by fluorescence polarization anisotropy assay	kd	0.5700	uM
1-(3-methylphenyl)-5-phenylpyrazole-3-carboxylic acid	1202917: Binding affinity to RPA70N protein (unknown origin) by HSQC NMR-based titration method	kd	0.5800	uM
5-[[(2S)-1-[[(2S)-1-[[(2S,3R)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-amino-1-oxopropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]carbamothioylamino]-2-(3-hydroxy-6-oxoxanthen-9-yl)benzoic acid	1127879: Binding affinity to recombinant human RPA70 N-terminal domain (1 to 120 amino acids) expressed in Escherichia coli BL21-DE3 by fluorescence polarization anisotropy assay	kd	0.5800	uM
4-bromo-2-[[3-[(3,4-dichlorophenyl)sulfamoyl]-4-methylbenzoyl]amino]benzoic acid	1506441: Binding affinity to RPA70 (unknown origin) by FITC-labeled probe based fluorescence polarization anisotropy	kd	0.8100	uM
1-(4-methoxyphenyl)-5-phenylpyrazole-3-carboxylic acid	1202917: Binding affinity to RPA70N protein (unknown origin) by HSQC NMR-based titration method	kd	0.8950	uM
5-[[(2S)-1-[[(2S)-1-[[(2S,3R)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-amino-1-oxopropan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]carbamothioylamino]-2-(3-hydroxy-6-oxoxanthen-9-yl)benzoic acid	1127879: Binding affinity to recombinant human RPA70 N-terminal domain (1 to 120 amino acids) expressed in Escherichia coli BL21-DE3 by fluorescence polarization anisotropy assay	kd	0.9100	uM
1,5-diphenylpyrazole-3-carboxylic acid	1202917: Binding affinity to RPA70N protein (unknown origin) by HSQC NMR-based titration method	kd	1.1500	uM

CTD chemical–gene interactions

75 total (human), top 30 by PubMed support.

Chemical	Actions (top 5)	PubMed papers
bisphenol A	affects expression, decreases expression, increases expression	4
sodium arsenite	affects localization, decreases expression, increases abundance	3
Resveratrol	affects cotreatment, increases expression, decreases expression	2
Arsenic	decreases expression, increases abundance, affects methylation	2
tert-Butylhydroperoxide	decreases expression	2
FR900359	affects phosphorylation	1
bisphenol F	increases expression	1
TAK-243	increases sumoylation	1
methylmercuric chloride	decreases expression	1
lasiocarpine	increases metabolic processing, decreases expression	1
triphenyl phosphate	affects expression	1
uranyl acetate	affects expression	1
4-biphenylamine	decreases expression	1
2,2’-methylenebis(4-methyl-6-tert-butylphenol)	affects expression, affects response to substance	1
trichostatin A	decreases expression	1
riddelliine	decreases expression, increases metabolic processing	1
mono-(2-ethylhexyl)phthalate	increases abundance, increases methylation	1
butyraldehyde	decreases expression	1
1,2-dielaidoylphosphatidylethanolamine	increases expression	1
perfluorooctanoic acid	decreases expression	1
doxifluridine	decreases response to substance	1
ochratoxin A	increases expression	1
2,3-bis(3’-hydroxybenzyl)butyrolactone	increases expression, affects cotreatment	1
di-n-butylphosphoric acid	affects expression	1
perfluorooctane sulfonic acid	decreases expression	1
AM 251	decreases expression	1
CPG-oligonucleotide	decreases expression	1
K 7174	decreases expression	1
4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamide	increases expression, affects cotreatment	1
erucylphospho-N,N,N-trimethylpropylammonium	decreases expression	1

ChEMBL screening assays

28 unique, capped per target: 28 binding

Representative assays (with source publication via chembl_document):

Assay ID	Type	Description	Source paper
CHEMBL1769911	Binding	Inhibition of recombinant human N-terminal domain of RPA70 DNA binding domain-F binding to 30-mer double strand DNA at <100 uM preincubated for 5mins before dsDNA addition measured after 30 mins by electrophoretic mobility shift assay	Small molecule inhibitor of the RPA70 N-terminal protein interaction domain discovered using in silico and in vitro methods. — Bioorg Med Chem

Clinical trials (associated diseases)

0 trials via MONDO — disease-level, not drug-specific.