HUMAN:RFA2

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	RPA2 (synonyms: REPA2, RPA32, RPA34)
Protein Name(s)	Replication protein A 32 kDa subunit RP-A p32 Replication factor A protein 2 RF-A protein 2 Replication protein A 34 kDa subunit RP-A p34
External Links
UniProt	P15927
EMBL	J05249 CR450348 DQ001128 AL109927 AL109927 AL109927 BC001630 BC012157 BC021257
CCDS	CCDS314.1 CCDS72740.1
PIR	A43711
RefSeq	NP_001273005.1 NP_001284487.1 NP_002937.1
UniGene	Hs.79411
PDB	1DPU 1L1O 1QUQ 1Z1D 2PI2 2PQA 2Z6K 3KDF 4MQV 4OU0
PDBsum	1DPU 1L1O 1QUQ 1Z1D 2PI2 2PQA 2Z6K 3KDF 4MQV 4OU0
ProteinModelPortal	P15927
SMR	P15927
BioGrid	112038
DIP	DIP-24187N
IntAct	P15927
MINT	MINT-5002459
STRING	9606.ENSP00000363021
PhosphoSite	P15927
DMDM	132474
MaxQB	P15927
PaxDb	P15927
PRIDE	P15927
DNASU	6118
Ensembl	ENST00000313433 ENST00000373909 ENST00000373912
GeneID	6118
KEGG	hsa:6118
UCSC	uc001bpe.1
CTD	6118
GeneCards	GC01M028218
HGNC	HGNC:10290
HPA	CAB016538 HPA026306 HPA026309
MIM	179836
neXtProt	NX_P15927
PharmGKB	PA34652
eggNOG	COG5235
GeneTree	ENSGT00390000010045
HOGENOM	HOG000216562
HOVERGEN	HBG000086
InParanoid	P15927
KO	K10739
OMA	SNPGMGE
OrthoDB	EOG76X615
PhylomeDB	P15927
TreeFam	TF105242
Reactome	REACT_1095 REACT_1993 REACT_200744 REACT_200780 REACT_2055 REACT_2141 REACT_228019 REACT_228145 REACT_257 REACT_27271 REACT_311 REACT_378 REACT_408 REACT_6769 REACT_70 REACT_7999
ChiTaRS	RPA2
EvolutionaryTrace	P15927
GeneWiki	RPA2
GenomeRNAi	6118
NextBio	23759
PRO	PR:P15927
Proteomes	UP000005640
Bgee	P15927
CleanEx	HS_RPA2
ExpressionAtlas	P15927
Genevestigator	P15927
GO	GO:0005662 GO:0005654 GO:0005634 GO:0016605 GO:0003684 GO:0019899 GO:0019903 GO:0003697 GO:0031625 GO:0006284 GO:0000730 GO:0006281 GO:0006260 GO:0006271 GO:0006302 GO:0000724 GO:0000082 GO:0006298 GO:0000278 GO:0031571 GO:0006289 GO:0000718 GO:0006297 GO:2000001 GO:0010569 GO:0000723 GO:0000722 GO:0032201 GO:0006283
Gene3D	1.10.10.10 2.40.50.140
InterPro	IPR012340 IPR004365 IPR014646 IPR014892 IPR011991
Pfam	PF08784 PF01336
PIRSF	PIRSF036949
SUPFAM	SSF50249

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0000785	chromatin	PMID:10336450^[1]	ECO:0000314			C	Figure 2-Mobilization of chromatin-bound RPA	complete CACAO 6129
enables	GO:0098505	G-rich strand telomeric DNA binding	PMID:24747047^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0000723	telomere maintenance	PMID:24747047^[2]	ECO:0000305	curator inference used in manual assertion	GO:0098505	P	Seeded From UniProt	complete
involved_in	GO:0034502	protein localization to chromosome	PMID:27723717^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	PMID:27723717^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005662	DNA replication factor A complex	PMID:27723717^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0034502	protein localization to chromosome	PMID:27723720^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	PMID:27723720^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005662	DNA replication factor A complex	PMID:27723720^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0000784	nuclear chromosome, telomeric region	PMID:19135898^[5]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0000785	chromatin	PMID:10336450^[1]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:2000001	regulation of DNA damage checkpoint	PMID:21504906^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
colocalizes_with	GO:0035861	site of double-strand break	PMID:21504906^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:21504906^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q6PCD5	F	Seeded From UniProt	complete
involved_in	GO:0031571	mitotic G1 DNA damage checkpoint	PMID:21731742^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0019903	protein phosphatase binding	PMID:20154705^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9NY27	F	Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:19793862^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9NZC9	F	Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:19793863^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9NZC9	F	Seeded From UniProt	complete
colocalizes_with	GO:0016605	PML body	PMID:17959650^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0016605	PML body	PMID:12814551^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0010569	regulation of double-strand break repair via homologous recombination	PMID:20154705^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006298	mismatch repair	PMID:9430682^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006289	nucleotide-excision repair	PMID:9430682^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006284	base-excision repair	PMID:9765279^[14]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	PMID:9430682^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	PMID:2406247^[15]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005662	DNA replication factor A complex	PMID:11927569^[16]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005662	DNA replication factor A complex	PMID:2406247^[15]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:10982866^[17]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003697	single-stranded DNA binding	PMID:19010961^[18]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003697	single-stranded DNA binding	PMID:2406247^[15]	ECO:0000305	curator inference used in manual assertion	GO:0005662	F	Seeded From UniProt	complete
enables	GO:0003697	single-stranded DNA binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q63528	F	Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	PMID:7700386^[19]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
colocalizes_with	GO:0000781	chromosome, telomeric region	PMID:17959650^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0000724	double-strand break repair via homologous recombination	PMID:17765923^[20]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0000723	telomere maintenance	PMID:17959650^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0035861	site of double-strand break	PMID:21873635^[21]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000360435 PomBase:SPCC1753.01c	C	Seeded From UniProt	complete
involved_in	GO:0006289	nucleotide-excision repair	PMID:21873635^[21]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000360435 SGD:S000005256 UniProtKB:P15927 UniProtKB:Q13156	P	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	PMID:21873635^[21]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000360435 SGD:S000005256 TAIR:locus:2061072 UniProtKB:P15927 UniProtKB:Q13156 UniProtKB:Q8LFJ8	P	Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	PMID:21873635^[21]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000360435 SGD:S000005256 TAIR:locus:2061072 UniProtKB:P15927	P	Seeded From UniProt	complete
part_of	GO:0005662	DNA replication factor A complex	PMID:21873635^[21]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000360435 PomBase:SPCC1753.01c RGD:619714 SGD:S000005256 UniProtKB:P15927 UniProtKB:Q13156	C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21873635^[21]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1915581 PANTHER:PTN001421418 PomBase:SPCC1753.01c RGD:619714 SGD:S000005256 TAIR:locus:2007352 TAIR:locus:2061072 UniProtKB:P15927 UniProtKB:Q13156 UniProtKB:Q57ZN9 UniProtKB:Q6K9U2 UniProtKB:Q8LFJ8 UniProtKB:Q9H668	C	Seeded From UniProt	complete
enables	GO:0003697	single-stranded DNA binding	PMID:21873635^[21]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1915581 PANTHER:PTN001421418 RGD:619714 SGD:S000005256 UniProtKB:P15927 UniProtKB:Q59Z33 UniProtKB:Q9H668	F	Seeded From UniProt	complete
part_of	GO:0000781	chromosome, telomeric region	PMID:21873635^[21]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000360435 SGD:S000005256	C	Seeded From UniProt	complete
involved_in	GO:0000724	double-strand break repair via homologous recombination	PMID:21873635^[21]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000360435 SGD:S000005256 UniProtKB:P15927 UniProtKB:Q8LFJ8	P	Seeded From UniProt	complete
part_of	GO:0005662	DNA replication factor A complex	PMID:16135809^[22]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P27694	C	Seeded From UniProt	complete
part_of	GO:0016604	nuclear body	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0047485	protein N-terminus binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q63528 ensembl:ENSRNOP00000017549	F	Seeded From UniProt	complete
part_of	GO:0005662	DNA replication factor A complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q63528 ensembl:ENSRNOP00000017549	C	Seeded From UniProt	complete
enables	GO:0003697	single-stranded DNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q63528 ensembl:ENSRNOP00000017549	F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR014646	F	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR014646	C	Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR014646	P	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR014646	P	Seeded From UniProt	complete
involved_in	GO:0006310	DNA recombination	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR014646	P	Seeded From UniProt	complete
involved_in	GO:1901796	regulation of signal transduction by p53 class mediator	Reactome:R-HSA-5633007	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:1900034	regulation of cellular response to heat	Reactome:R-HSA-3371453	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0070987	error-free translesion synthesis	Reactome:R-HSA-110320	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0042769	DNA damage response, detection of DNA damage	Reactome:R-HSA-110314	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0042276	error-prone translesion synthesis	Reactome:R-HSA-5656121 Reactome:R-HSA-5655862 Reactome:R-HSA-110312	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0036297	interstrand cross-link repair	Reactome:R-HSA-6783310	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0033683	nucleotide-excision repair, DNA incision	Reactome:R-HSA-5696400	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0032201	telomere maintenance via semi-conservative replication	Reactome:R-HSA-174451 Reactome:R-HSA-174445 Reactome:R-HSA-174441	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0019985	translesion synthesis	Reactome:R-HSA-110313	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006297	nucleotide-excision repair, DNA gap filling	Reactome:R-HSA-5696397	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006296	nucleotide-excision repair, DNA incision, 5'-to lesion	Reactome:R-HSA-5690988	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006295	nucleotide-excision repair, DNA incision, 3'-to lesion	Reactome:R-HSA-5690990	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006294	nucleotide-excision repair, preincision complex assembly	Reactome:R-HSA-5689317	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006293	nucleotide-excision repair, preincision complex stabilization	Reactome:R-HSA-5690991	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006283	transcription-coupled nucleotide-excision repair	Reactome:R-HSA-6781827	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	Reactome:R-HSA-5684887 Reactome:R-HSA-5684875 Reactome:R-HSA-176264 Reactome:R-HSA-176250 Reactome:R-HSA-176175 Reactome:R-HSA-176101	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-69144 Reactome:R-HSA-69142 Reactome:R-HSA-69140 Reactome:R-HSA-68916 Reactome:R-HSA-6799332 Reactome:R-HSA-6788392 Reactome:R-HSA-6788385 Reactome:R-HSA-6782227 Reactome:R-HSA-6782224 Reactome:R-HSA-6782211 Reactome:R-HSA-6782208 Reactome:R-HSA-6782204 Reactome:R-HSA-6782141 Reactome:R-HSA-6782138 Reactome:R-HSA-5693580 Reactome:R-HSA-5693564 Reactome:R-HSA-5693561 Reactome:R-HSA-5693542 Reactome:R-HSA-5691001 Reactome:R-HSA-5690997 Reactome:R-HSA-5690991 Reactome:R-HSA-5690990 Reactome:R-HSA-5690988 Reactome:R-HSA-5690213 Reactome:R-HSA-5689317 Reactome:R-HSA-5687758 Reactome:R-HSA-5686657 Reactome:R-HSA-5686642 Reactome:R-HSA-5685156 Reactome:R-HSA-5685011 Reactome:R-HSA-5684887 Reactome:R-HSA-5684882 Reactome:R-HSA-5684875 Reactome:R-HSA-5656158 Reactome:R-HSA-5656148 Reactome:R-HSA-5656105 Reactome:R-HSA-5655965 Reactome:R-HSA-5655892 Reactome:R-HSA-5655835 Reactome:R-HSA-5655481 Reactome:R-HSA-5655466 Reactome:R-HSA-5654989 Reactome:R-HSA-5654986 Reactome:R-HSA-5654985 Reactome:R-HSA-5653840 Reactome:R-HSA-5653838 Reactome:R-HSA-5653786 Reactome:R-HSA-5653780 Reactome:R-HSA-5653770 Reactome:R-HSA-5653766 Reactome:R-HSA-5653756 Reactome:R-HSA-5653754 Reactome:R-HSA-5652151 Reactome:R-HSA-5652009 Reactome:R-HSA-5652005 Reactome:R-HSA-5651992 Reactome:R-HSA-5651809 Reactome:R-HSA-5651805 Reactome:R-HSA-5358599 Reactome:R-HSA-5358579 Reactome:R-HSA-5333051 Reactome:R-HSA-176264 Reactome:R-HSA-176250 Reactome:R-HSA-176175 Reactome:R-HSA-176101 Reactome:R-HSA-174451 Reactome:R-HSA-174445 Reactome:R-HSA-174441 Reactome:R-HSA-110371 Reactome:R-HSA-110368 Reactome:R-HSA-110364 Reactome:R-HSA-110363 Reactome:R-HSA-110319 Reactome:R-HSA-110317 Reactome:R-HSA-110316 Reactome:R-HSA-110311 Reactome:R-HSA-110308 Reactome:R-HSA-110307	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0000082	G1/S transition of mitotic cell cycle	Reactome:R-HSA-69206	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0227	P	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0234	P	Seeded From UniProt	complete
involved_in	GO:0006310	DNA recombination	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0233	P	Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0235	P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C	Seeded From UniProt	complete
part_of	GO:0016605	PML body	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0465	C	Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Treuner, K et al. (1999) Phosphorylation of replication protein A middle subunit (RPA32) leads to a disassembly of the RPA heterotrimer. J. Biol. Chem. 274 15556-61 PubMed GONUTS page
↑ ^2.0 ^2.1 Safa, L et al. (2014) Binding polarity of RPA to telomeric sequences and influence of G-quadruplex stability. Biochimie 103 80-8 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Haahr, P et al. (2016) Activation of the ATR kinase by the RPA-binding protein ETAA1. Nat. Cell Biol. 18 1196-1207 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Bass, TE et al. (2016) ETAA1 acts at stalled replication forks to maintain genome integrity. Nat. Cell Biol. 18 1185-1195 PubMed GONUTS page
↑ Déjardin, J & Kingston, RE (2009) Purification of proteins associated with specific genomic Loci. Cell 136 175-86 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Gong, Z & Chen, J (2011) E3 ligase RFWD3 participates in replication checkpoint control. J. Biol. Chem. 286 22308-13 PubMed GONUTS page
↑ Liaw, H et al. (2011) DNA-PK-dependent RPA2 hyperphosphorylation facilitates DNA repair and suppresses sister chromatid exchange. PLoS ONE 6 e21424 PubMed GONUTS page
↑ ^8.0 ^8.1 Lee, DH et al. (2010) A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombination. Nat. Struct. Mol. Biol. 17 365-72 PubMed GONUTS page
↑ Ciccia, A et al. (2009) The SIOD disorder protein SMARCAL1 is an RPA-interacting protein involved in replication fork restart. Genes Dev. 23 2415-25 PubMed GONUTS page
↑ Yusufzai, T et al. (2009) The annealing helicase HARP is recruited to DNA repair sites via an interaction with RPA. Genes Dev. 23 2400-4 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 Grudic, A et al. (2007) Replication protein A prevents accumulation of single-stranded telomeric DNA in cells that use alternative lengthening of telomeres. Nucleic Acids Res. 35 7267-78 PubMed GONUTS page
↑ Barr, SM et al. (2003) ATR kinase activity regulates the intranuclear translocation of ATR and RPA following ionizing radiation. Curr. Biol. 13 1047-51 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 Lin, YL et al. (1998) 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. J. Biol. Chem. 273 1453-61 PubMed GONUTS page
↑ DeMott, MS et al. (1998) Replication protein A stimulates long patch DNA base excision repair. J. Biol. Chem. 273 27492-8 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 Erdile, LF et al. (1990) The primary structure of the 32-kDa subunit of human replication protein A. J. Biol. Chem. 265 3177-82 PubMed GONUTS page
↑ Bochkareva, E et al. (2002) Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA. EMBO J. 21 1855-63 PubMed GONUTS page
↑ Cho, JM et al. (2000) RBT1, a novel transcriptional co-activator, binds the second subunit of replication protein A. Nucleic Acids Res. 28 3478-85 PubMed GONUTS page
↑ Salas, TR et al. (2009) Evidence for direct contact between the RPA3 subunit of the human replication protein A and single-stranded DNA. Nucleic Acids Res. 37 38-46 PubMed GONUTS page
↑ He, Z et al. (1995) RPA involvement in the damage-recognition and incision steps of nucleotide excision repair. Nature 374 566-9 PubMed GONUTS page
↑ Sleeth, KM et al. (2007) RPA mediates recombination repair during replication stress and is displaced from DNA by checkpoint signalling in human cells. J. Mol. Biol. 373 38-47 PubMed GONUTS page
↑ ^21.0 ^21.1 ^21.2 ^21.3 ^21.4 ^21.5 ^21.6 ^21.7 ^21.8 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Park, J et al. (2005) Sumoylation of the novel protein hRIP{beta} is involved in replication protein A deposition in PML nuclear bodies. Mol. Cell. Biol. 25 8202-14 PubMed GONUTS page

[PMID:10336450-1] 1.0 ^1.1 Treuner, K et al. (1999) Phosphorylation of replication protein A middle subunit (RPA32) leads to a disassembly of the RPA heterotrimer. J. Biol. Chem. 274 15556-61 PubMed GONUTS page

[PMID:24747047-2] 2.0 ^2.1 Safa, L et al. (2014) Binding polarity of RPA to telomeric sequences and influence of G-quadruplex stability. Biochimie 103 80-8 PubMed GONUTS page

[PMID:27723717-3] 3.0 ^3.1 ^3.2 Haahr, P et al. (2016) Activation of the ATR kinase by the RPA-binding protein ETAA1. Nat. Cell Biol. 18 1196-1207 PubMed GONUTS page

[PMID:27723720-4] 4.0 ^4.1 ^4.2 Bass, TE et al. (2016) ETAA1 acts at stalled replication forks to maintain genome integrity. Nat. Cell Biol. 18 1185-1195 PubMed GONUTS page

[PMID:19135898-5] Déjardin, J & Kingston, RE (2009) Purification of proteins associated with specific genomic Loci. Cell 136 175-86 PubMed GONUTS page

[PMID:21504906-6] 6.0 ^6.1 ^6.2 Gong, Z & Chen, J (2011) E3 ligase RFWD3 participates in replication checkpoint control. J. Biol. Chem. 286 22308-13 PubMed GONUTS page

[PMID:21731742-7] Liaw, H et al. (2011) DNA-PK-dependent RPA2 hyperphosphorylation facilitates DNA repair and suppresses sister chromatid exchange. PLoS ONE 6 e21424 PubMed GONUTS page

[PMID:20154705-8] 8.0 ^8.1 Lee, DH et al. (2010) A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombination. Nat. Struct. Mol. Biol. 17 365-72 PubMed GONUTS page

[PMID:19793862-9] Ciccia, A et al. (2009) The SIOD disorder protein SMARCAL1 is an RPA-interacting protein involved in replication fork restart. Genes Dev. 23 2415-25 PubMed GONUTS page

[PMID:19793863-10] Yusufzai, T et al. (2009) The annealing helicase HARP is recruited to DNA repair sites via an interaction with RPA. Genes Dev. 23 2400-4 PubMed GONUTS page

[PMID:17959650-11] 11.0 ^11.1 ^11.2 Grudic, A et al. (2007) Replication protein A prevents accumulation of single-stranded telomeric DNA in cells that use alternative lengthening of telomeres. Nucleic Acids Res. 35 7267-78 PubMed GONUTS page

[PMID:12814551-12] Barr, SM et al. (2003) ATR kinase activity regulates the intranuclear translocation of ATR and RPA following ionizing radiation. Curr. Biol. 13 1047-51 PubMed GONUTS page

[PMID:9430682-13] 13.0 ^13.1 ^13.2 Lin, YL et al. (1998) 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. J. Biol. Chem. 273 1453-61 PubMed GONUTS page

[PMID:9765279-14] DeMott, MS et al. (1998) Replication protein A stimulates long patch DNA base excision repair. J. Biol. Chem. 273 27492-8 PubMed GONUTS page

[PMID:2406247-15] 15.0 ^15.1 ^15.2 Erdile, LF et al. (1990) The primary structure of the 32-kDa subunit of human replication protein A. J. Biol. Chem. 265 3177-82 PubMed GONUTS page

[PMID:11927569-16] Bochkareva, E et al. (2002) Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA. EMBO J. 21 1855-63 PubMed GONUTS page

[PMID:10982866-17] Cho, JM et al. (2000) RBT1, a novel transcriptional co-activator, binds the second subunit of replication protein A. Nucleic Acids Res. 28 3478-85 PubMed GONUTS page

[PMID:19010961-18] Salas, TR et al. (2009) Evidence for direct contact between the RPA3 subunit of the human replication protein A and single-stranded DNA. Nucleic Acids Res. 37 38-46 PubMed GONUTS page

[PMID:7700386-19] He, Z et al. (1995) RPA involvement in the damage-recognition and incision steps of nucleotide excision repair. Nature 374 566-9 PubMed GONUTS page

[PMID:17765923-20] Sleeth, KM et al. (2007) RPA mediates recombination repair during replication stress and is displaced from DNA by checkpoint signalling in human cells. J. Mol. Biol. 373 38-47 PubMed GONUTS page

[PMID:21873635-21] 21.0 ^21.1 ^21.2 ^21.3 ^21.4 ^21.5 ^21.6 ^21.7 ^21.8 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:16135809-22] Park, J et al. (2005) Sumoylation of the novel protein hRIP{beta} is involved in replication protein A deposition in PML nuclear bodies. Mol. Cell. Biol. 25 8202-14 PubMed GONUTS page

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HUMAN:RFA2

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