HUMAN:RFA1

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	RPA1 (synonyms: REPA1, RPA70)
Protein Name(s)	Replication protein A 70 kDa DNA-binding subunit RP-A p70 Replication factor A protein 1 RF-A protein 1 Single-stranded DNA-binding protein Replication protein A 70 kDa DNA-binding subunit, N-terminally processed
External Links
UniProt	P27694
EMBL	M63488 AK289704 AB209732 AY599563 CH471108 BC018126
CCDS	CCDS11014.1
PIR	A40457
RefSeq	NP_002936.1
UniGene	Hs.461925
PDB	1EWI 1FGU 1JMC 1L1O 2B29 2B3G 4IJH 4IJL 4IPC 4IPD 4IPG 4IPH 4LUO 4LUV 4LUZ 4LW1 4LWC 4NB3 4O0A
PDBsum	1EWI 1FGU 1JMC 1L1O 2B29 2B3G 4IJH 4IJL 4IPC 4IPD 4IPG 4IPH 4LUO 4LUV 4LUZ 4LW1 4LWC 4NB3 4O0A
DisProt	DP00061
ProteinModelPortal	P27694
SMR	P27694
BioGrid	112037
DIP	DIP-24189N
IntAct	P27694
MINT	MINT-91488
STRING	9606.ENSP00000254719
BindingDB	P27694
ChEMBL	CHEMBL1764940
PhosphoSite	P27694
DMDM	1350579
MaxQB	P27694
PaxDb	P27694
PeptideAtlas	P27694
PRIDE	P27694
DNASU	6117
Ensembl	ENST00000254719
GeneID	6117
KEGG	hsa:6117
UCSC	uc002fto.2
CTD	6117
GeneCards	GC17P001680
HGNC	HGNC:10289
HPA	CAB004563 HPA006914 HPA046497
MIM	179835
neXtProt	NX_P27694
PharmGKB	PA34651
eggNOG	COG1599
GeneTree	ENSGT00390000012403
HOGENOM	HOG000162322
HOVERGEN	HBG010502
InParanoid	P27694
KO	K07466
OMA	VIAFKGC
OrthoDB	EOG7GXPBM
PhylomeDB	P27694
TreeFam	TF105241
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	RPA1
EvolutionaryTrace	P27694
GeneWiki	Replication_protein_A1
GenomeRNAi	6117
NextBio	23755
PRO	PR:P27694
Proteomes	UP000005640
Bgee	P27694
CleanEx	HS_RPA1
ExpressionAtlas	P27694
Genevestigator	P27694
GO	GO:0015629 GO:0005737 GO:0005662 GO:0000800 GO:0001673 GO:0005654 GO:0005634 GO:0016605 GO:0003682 GO:0003684 GO:0046872 GO:0003697 GO:0006284 GO:0000730 GO:0006310 GO:0006281 GO:0006260 GO:0006271 GO:0006261 GO:0006302 GO:0000724 GO:0000082 GO:0030097 GO:0048873 GO:0001701 GO:0007126 GO:0006298 GO:0000278 GO:0006289 GO:0000718 GO:0006297 GO:0008284 GO:0000723 GO:0000722 GO:0032201 GO:0006283
Gene3D	2.40.50.140
InterPro	IPR012340 IPR004365 IPR013955 IPR007199 IPR004591
Pfam	PF04057 PF08646 PF01336
SUPFAM	SSF50249
TIGRFAMs	TIGR00617

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0031576	G2/M transition checkpoint	PMID:18469000^[1]	ECO:0000315			P		P.19099, Table 1, Figures 1,2	complete CACAO 2019
	GO:0006281	DNA repair	PMID:18469000^[1]	ECO:0000315			P		Figure 6	complete CACAO 2022
	GO:0006260	DNA replication	PMID:8756712^[2]	ECO:0000315			P		Figure 4.	complete CACAO 2026
part_of	GO:0090734	site of DNA damage	PMID:27248496^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		C	part_of:(GO:0005634)	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	PMID:27248496^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_at:(GO:0005634)	Seeded From UniProt	complete
involved_in	GO:0000723	telomere maintenance	PMID:24747047^[4]	ECO:0000305	curator inference used in manual assertion	GO:0098505	P		Seeded From UniProt	complete
involved_in	GO:0000723	telomere maintenance	PMID:16973897^[5]	ECO:0000305	curator inference used in manual assertion	GO:0098505	P		Seeded From UniProt	complete
involved_in	GO:0000723	telomere maintenance	PMID:26041456^[6]	ECO:0000305	curator inference used in manual assertion	GO:0098505	P		Seeded From UniProt	complete
enables	GO:0098505	G-rich strand telomeric DNA binding	PMID:26041456^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0098505	G-rich strand telomeric DNA binding	PMID:16973897^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0098505	G-rich strand telomeric DNA binding	PMID:24747047^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0034502	protein localization to chromosome	PMID:27723717^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034502	protein localization to chromosome	PMID:27723720^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	PMID:27723717^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	PMID:27723720^[8]	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^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005662	DNA replication factor A complex	PMID:27723720^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0000784	nuclear chromosome, telomeric region	PMID:19135898^[9]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	PMID:18469000^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
colocalizes_with	GO:0016605	PML body	PMID:17959650^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006298	mismatch repair	PMID:9430682^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006289	nucleotide-excision repair	PMID:9430682^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006284	base-excision repair	PMID:9765279^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	PMID:9430682^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005662	DNA replication factor A complex	PMID:11927569^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:17959650^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003697	single-stranded DNA binding	PMID:19010961^[14]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003697	single-stranded DNA binding	PMID:8990123^[15]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	PMID:7700386^[16]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0000724	double-strand break repair via homologous recombination	PMID:17765923^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000723	telomere maintenance	PMID:17959650^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051321	meiotic cell cycle	PMID:21873635^[18]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1915525 PANTHER:PTN000588618	P		Seeded From UniProt	complete
enables	GO:0043565	sequence-specific DNA binding	PMID:21873635^[18]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000588618 SGD:S000000065	F		Seeded From UniProt	complete
enables	GO:0043047	single-stranded telomeric DNA binding	PMID:21873635^[18]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000588618 PomBase:SPBC660.13c	F		Seeded From UniProt	complete
involved_in	GO:0007004	telomere maintenance via telomerase	PMID:21873635^[18]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000588618 PomBase:SPBC660.13c SGD:S000000065	P		Seeded From UniProt	complete
involved_in	GO:0006289	nucleotide-excision repair	PMID:21873635^[18]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000588618 SGD:S000000065 UniProtKB:P27694	P		Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	PMID:21873635^[18]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000588618 PomBase:SPBC660.13c SGD:S000000065 UniProtKB:P27694 UniProtKB:Q6YZ49	P		Seeded From UniProt	complete
involved_in	GO:0006268	DNA unwinding involved in DNA replication	PMID:21873635^[18]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000588618 PomBase:SPBC660.13c SGD:S000000065	P		Seeded From UniProt	complete
involved_in	GO:0006261	DNA-dependent DNA replication	PMID:21873635^[18]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0010173 PANTHER:PTN000588618 UniProtKB:Q9U0J0	P		Seeded From UniProt	complete
part_of	GO:0005662	DNA replication factor A complex	PMID:21873635^[18]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0010173 PANTHER:PTN000588618 PomBase:SPBC660.13c RGD:1307376 SGD:S000000065 UniProtKB:P27694 UniProtKB:Q10Q08	C		Seeded From UniProt	complete
enables	GO:0003697	single-stranded DNA binding	PMID:21873635^[18]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0010173 PANTHER:PTN000588618 PomBase:SPBC660.13c RGD:1307376 SGD:S000000065 UniProtKB:P27694	F		Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	PMID:21873635^[18]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000588618 UniProtKB:P27694	F		Seeded From UniProt	complete
part_of	GO:0000784	nuclear chromosome, telomeric region	PMID:21873635^[18]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000588618 PomBase:SPBC660.13c	C		Seeded From UniProt	complete
involved_in	GO:0000724	double-strand break repair via homologous recombination	PMID:21873635^[18]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1915525 PANTHER:PTN000588618 SGD:S000000065 UniProtKB:P27694	P		Seeded From UniProt	complete
involved_in	GO:0000723	telomere maintenance	PMID:21873635^[18]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000588618 PomBase:SPBC660.13c UniProtKB:P27694	P		Seeded From UniProt	complete
part_of	GO:0016605	PML body	PMID:16135809^[19]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005662	DNA replication factor A complex	PMID:16135809^[19]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P15927	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
part_of	GO:0005662	DNA replication factor A complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q7TP21 ensembl:ENSRNOP00000004229	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:Q7TP21 ensembl:ENSRNOP00000004229	F		Seeded From UniProt	complete
enables	GO:0003676	nucleic acid binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004365	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:IPR004591 InterPro:IPR007199	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:IPR004591 InterPro:IPR007199	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:IPR004591 InterPro:IPR007199	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:IPR004591	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:IPR004591	P		Seeded From UniProt	complete
involved_in	GO:0006310	DNA recombination	PMID:8756712^[2]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006261	DNA-dependent DNA replication	PMID:8756712^[2]	ECO:0000304	author statement supported by traceable reference used in manual assertion		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-4551616 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
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
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: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: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
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
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	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
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
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Notes

References

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

↑ ^1.0 ^1.1 ^1.2 Haring, SJ et al. (2008) Cellular functions of human RPA1. Multiple roles of domains in replication, repair, and checkpoints. J. Biol. Chem. 283 19095-111 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Gomes, XV & Wold, MS (1996) Functional domains of the 70-kilodalton subunit of human replication protein A. Biochemistry 35 10558-68 PubMed GONUTS page
↑ ^3.0 ^3.1 Gilmore, JM et al. (2016) WDR76 Co-Localizes with Heterochromatin Related Proteins and Rapidly Responds to DNA Damage. PLoS ONE 11 e0155492 PubMed GONUTS page
↑ ^4.0 ^4.1 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
↑ ^5.0 ^5.1 Salas, TR et al. (2006) Human replication protein A unfolds telomeric G-quadruplexes. Nucleic Acids Res. 34 4857-65 PubMed GONUTS page
↑ ^6.0 ^6.1 Audry, J et al. (2015) RPA prevents G-rich structure formation at lagging-strand telomeres to allow maintenance of chromosome ends. EMBO J. 34 1942-58 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 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
↑ ^8.0 ^8.1 ^8.2 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
↑ ^10.0 ^10.1 ^10.2 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
↑ ^11.0 ^11.1 ^11.2 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
↑ 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
↑ 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
↑ Bochkarev, A et al. (1997) Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA. Nature 385 176-81 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
↑ ^18.00 ^18.01 ^18.02 ^18.03 ^18.04 ^18.05 ^18.06 ^18.07 ^18.08 ^18.09 ^18.10 ^18.11 ^18.12 ^18.13 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^19.0 ^19.1 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:18469000-1] 1.0 ^1.1 ^1.2 Haring, SJ et al. (2008) Cellular functions of human RPA1. Multiple roles of domains in replication, repair, and checkpoints. J. Biol. Chem. 283 19095-111 PubMed GONUTS page

[PMID:8756712-2] 2.0 ^2.1 ^2.2 Gomes, XV & Wold, MS (1996) Functional domains of the 70-kilodalton subunit of human replication protein A. Biochemistry 35 10558-68 PubMed GONUTS page

[PMID:27248496-3] 3.0 ^3.1 Gilmore, JM et al. (2016) WDR76 Co-Localizes with Heterochromatin Related Proteins and Rapidly Responds to DNA Damage. PLoS ONE 11 e0155492 PubMed GONUTS page

[PMID:24747047-4] 4.0 ^4.1 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:16973897-5] 5.0 ^5.1 Salas, TR et al. (2006) Human replication protein A unfolds telomeric G-quadruplexes. Nucleic Acids Res. 34 4857-65 PubMed GONUTS page

[PMID:26041456-6] 6.0 ^6.1 Audry, J et al. (2015) RPA prevents G-rich structure formation at lagging-strand telomeres to allow maintenance of chromosome ends. EMBO J. 34 1942-58 PubMed GONUTS page

[PMID:27723717-7] 7.0 ^7.1 ^7.2 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:27723720-8] 8.0 ^8.1 ^8.2 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:19135898-9] Déjardin, J & Kingston, RE (2009) Purification of proteins associated with specific genomic Loci. Cell 136 175-86 PubMed GONUTS page

[PMID:17959650-10] 10.0 ^10.1 ^10.2 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:9430682-11] 11.0 ^11.1 ^11.2 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:9765279-12] 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:11927569-13] 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:19010961-14] 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:8990123-15] Bochkarev, A et al. (1997) Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA. Nature 385 176-81 PubMed GONUTS page

[PMID:7700386-16] 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:17765923-17] 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:21873635-18] 18.00 ^18.01 ^18.02 ^18.03 ^18.04 ^18.05 ^18.06 ^18.07 ^18.08 ^18.09 ^18.10 ^18.11 ^18.12 ^18.13 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:16135809-19] 19.0 ^19.1 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:RFA1

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