RPA1

Functionⁱ

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 (PubMed:27723720, PubMed:27723717). Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage (PubMed:9430682). 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 (PubMed:24332808). It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage (PubMed:17765923). 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 (PubMed:7697716). Plays also a role in base excision repair (BER) probably through interaction with UNG (PubMed:9765279). Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance (PubMed:17959650). 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 (PubMed:19996105).12 Publications

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
DNA bindingⁱ	197 – 281	OBAdd BLAST		85
Zinc fingerⁱ	481 – 503	C4-typeSequence analysisAdd BLAST		23

GO - Molecular functionⁱ

damaged DNA binding
Source: UniProtKB
Inferred from direct assayⁱ
G-rich strand telomeric DNA binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 16973897
- 24747047
metal ion binding Source: UniProtKB-KW
sequence-specific DNA binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
single-stranded DNA binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19010961
- 8990123
single-stranded telomeric DNA binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

base-excision repair
Source: UniProtKB
Inferred from direct assayⁱ
- 9765279
cellular response to DNA damage stimulus
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 27248496
DNA damage response, detection of DNA damage Source: Reactome
DNA-dependent DNA replication
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
DNA recombination
Source: ProtInc
Traceable author statementⁱ
- 8756712
DNA repair
Source: CACAO
Inferred from mutant phenotypeⁱ
- 18469000
DNA replication
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 9430682
DNA unwinding involved in DNA replication
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
double-strand break repair via homologous recombination
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 17765923
error-free translesion synthesis Source: Reactome
error-prone translesion synthesis Source: Reactome
G1/S transition of mitotic cell cycle Source: Reactome
interstrand cross-link repair Source: Reactome
meiotic cell cycle
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
mismatch repair
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 9430682
nucleotide-excision repair
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 9430682
nucleotide-excision repair, DNA gap filling Source: Reactome
nucleotide-excision repair, DNA incision Source: Reactome
nucleotide-excision repair, DNA incision, 5'-to lesion Source: Reactome
nucleotide-excision repair, preincision complex assembly Source: Reactome
nucleotide-excision repair, preincision complex stabilization Source: Reactome
protein localization to chromosome
Source: UniProtKB
Inferred from direct assayⁱ
- 27723717
- 27723720
regulation of cellular response to heat Source: Reactome
telomere maintenance
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 17959650
telomere maintenance via semi-conservative replication Source: Reactome
telomere maintenance via telomerase
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
transcription-coupled nucleotide-excision repair Source: Reactome
translesion synthesis Source: Reactome

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-binding
Biological process	DNA damage, DNA recombination, DNA repair, DNA replication
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

Reactomeⁱ	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

Reactomeⁱ

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

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Replication protein A 70 kDa DNA-binding subunit Short name: RP-A p70 Alternative name(s): Replication factor A protein 1 Short name: RF-A protein 1 Single-stranded DNA-binding protein Cleaved into the following chain: Replication protein A 70 kDa DNA-binding subunit, N-terminally processed
Gene namesⁱ	Name:RPA1 Synonyms:REPA1, RPA70
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 17

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000132383.11
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:10289 RPA1
MIMⁱ	179835 gene
neXtProtⁱ	NX_P27694

Keywords - Cellular componentⁱ

Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	41	R → E: Loss of HELB-binding; when associated with E-43. 1 Publication	1
Mutagenesisⁱ	43	R → E: Loss of HELB-binding; when associated with E-41. 1 Publication	1
Mutagenesisⁱ	449	K → R: Significant reduction of sumoylation. Loss of sumoylation; when associated with R-577. 1 Publication	1
Mutagenesisⁱ	500	C → S: Loss of function in DNA replication and mismatch repair without effect on DNA-binding activity; when associated with S-503. 1 Publication	1
Mutagenesisⁱ	503	C → S: Loss of function in DNA replication and mismatch repair without effect on DNA-binding activity; when associated with S-500. 1 Publication	1
Mutagenesisⁱ	577	K → R: Slight sumoylation decrease. Loss of sumoylation; when associated with R-449. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	6117
Open Targets More...OpenTargetsⁱ	ENSG00000132383
PharmGKBⁱ	PA34651

Chemistry databases

ChEMBLⁱ	CHEMBL1764940

ChEMBLⁱ

CHEMBL1764940

Polymorphism and mutation databases

BioMutaⁱ	RPA1
DMDMⁱ	1350579

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Length
ChainⁱPRO_0000423231	1 – 616	Replication protein A 70 kDa DNA-binding subunitAdd BLAST	616
Initiator methionineⁱ		Removed; alternate1 Publication
ChainⁱPRO_0000097260	2 – 616	Replication protein A 70 kDa DNA-binding subunit, N-terminally processedAdd BLAST	615

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	1	N-acetylmethionineCombined sources	1
Cross-linkⁱ	22	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linkⁱ	88	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residueⁱ	163	N6-acetyllysine; alternateCombined sources	1
Cross-linkⁱ	163	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residueⁱ	167	N6-acetyllysine; alternateCombined sources	1
Cross-linkⁱ	167	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residueⁱ	180	PhosphothreonineCombined sources	1
Cross-linkⁱ	183	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residueⁱ	191	PhosphothreonineCombined sources	1
Cross-linkⁱ	220	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linkⁱ	244	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residueⁱ	259	N6-acetyllysine; alternateCombined sources	1
Cross-linkⁱ	259	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Cross-linkⁱ	267	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linkⁱ	331	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residueⁱ	384	PhosphoserineCombined sources	1
Cross-linkⁱ	410	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linkⁱ	431	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linkⁱ	449	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linkⁱ	458	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linkⁱ	553	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linkⁱ	577	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

Post-translational modificationⁱ

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 (PubMed:24332808). 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 (PubMed:26474068).2 Publications

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 SENP6.1 Publication

Keywords - PTMⁱ

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	P27694
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P27694
PaxDbⁱ	P27694
PeptideAtlas More...PeptideAtlasⁱ	P27694
PRIDEⁱ	P27694
ProteomicsDBⁱ	54405

PTM databases

iPTMnetⁱ	P27694
PhosphoSitePlusⁱ	P27694
SwissPalmⁱ	P27694

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000132383 Expressed in 235 organ(s), highest expression level in secondary oocyte
CleanExⁱ	HS_RPA1
ExpressionAtlasⁱ	P27694 baseline and differential
Genevisibleⁱ	P27694 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB004563 HPA006914 HPA046497

HPAⁱ

CAB004563
HPA006914
HPA046497

Interactionⁱ

Subunit structureⁱ

Component of the canonical replication protein A complex (RPA), an heterotrimer composed of RPA1, RPA2 and RPA3 (PubMed:27723720, PubMed:27723717). Also 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 (PubMed:7760808, PubMed:19116208). 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) (PubMed:24332808). Interacts with RIPK1 (PubMed:16135809). 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 (PubMed:9214288). Interacts with RAD51 and SENP6 to regulate DNA repair (PubMed:20705237). Interacts with HELB; this interaction promotes HELB recruitment to chromatin following DNA damage (PubMed:22194613, PubMed:26774285). Interacts with PRIMPOL (PubMed:24126761). Interacts with XPA; the interaction is direct and associates XPA with the RPA complex (PubMed:7700386, PubMed:9699634, PubMed:10563794). Interacts with ETAA1; the interaction is direct and promotes ETAA1 recruitment at stalled replication forks (PubMed:27601467, PubMed:27723720, PubMed:27723717).15 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
	P03070	3	EBI-621389,EBI-617698	From Simian virus 40.
BLM	P54132	4	EBI-621389,EBI-621372
MTUS2	Q5JR59	3	EBI-621389,EBI-742948
POLA1	P09884	2	EBI-621389,EBI-850026
PRIMPOL	Q96LW4	7	EBI-621389,EBI-10044038
RPA2	P15927	11	EBI-621389,EBI-621404
RPA3	P35244	8	EBI-621389,EBI-621428
WRN	Q14191	9	EBI-621389,EBI-368417

Protein-protein interaction databases

BioGridⁱ	112037, 485 interactors
CORUMⁱ	P27694
Database of interacting proteins More...DIPⁱ	DIP-24189N
IntActⁱ	P27694, 77 interactors
Molecular INTeraction database More...MINTⁱ	P27694
STRINGⁱ	9606.ENSP00000254719

Chemistry databases

BindingDBⁱ

P27694

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	2 – 4	Combined sources	3
Helixⁱ	9 – 14	Combined sources	6
Turnⁱ	15 – 17	Combined sources	3
Beta strandⁱ	18 – 20	Combined sources	3
Beta strandⁱ	24 – 32	Combined sources	9
Beta strandⁱ	36 – 38	Combined sources	3
Beta strandⁱ	42 – 47	Combined sources	6
Beta strandⁱ	49 – 58	Combined sources	10
Helixⁱ	60 – 62	Combined sources	3
Helixⁱ	63 – 67	Combined sources	5
Beta strandⁱ	70 – 74	Combined sources	5
Beta strandⁱ	76 – 86	Combined sources	11
Beta strandⁱ	88 – 90	Combined sources	3
Beta strandⁱ	92 – 103	Combined sources	12
Helixⁱ	105 – 108	Combined sources	4
Helixⁱ	187 – 189	Combined sources	3
Beta strandⁱ	198 – 206	Combined sources	9
Beta strandⁱ	210 – 213	Combined sources	4
Beta strandⁱ	218 – 227	Combined sources	10
Beta strandⁱ	232 – 238	Combined sources	7
Helixⁱ	239 – 245	Combined sources	7
Helixⁱ	246 – 248	Combined sources	3
Beta strandⁱ	254 – 258	Combined sources	5
Beta strandⁱ	261 – 264	Combined sources	4
Helixⁱ	267 – 269	Combined sources	3
Beta strandⁱ	275 – 279	Combined sources	5
Beta strandⁱ	285 – 288	Combined sources	4
Helixⁱ	305 – 310	Combined sources	6
Beta strandⁱ	316 – 326	Combined sources	11
Beta strandⁱ	330 – 334	Combined sources	5
Turnⁱ	335 – 338	Combined sources	4
Beta strandⁱ	339 – 349	Combined sources	11
Beta strandⁱ	355 – 361	Combined sources	7
Helixⁱ	362 – 367	Combined sources	6
Beta strandⁱ	375 – 384	Combined sources	10
Beta strandⁱ	388 – 392	Combined sources	5
Beta strandⁱ	398 – 402	Combined sources	5
Helixⁱ	406 – 416	Combined sources	11
Turnⁱ	417 – 419	Combined sources	3
Helixⁱ	445 – 451	Combined sources	7
Turnⁱ	452 – 454	Combined sources	3
Beta strandⁱ	455 – 458	Combined sources	4
Beta strandⁱ	460 – 471	Combined sources	12
Beta strandⁱ	477 – 480	Combined sources	4
Beta strandⁱ	491 – 493	Combined sources	3
Turnⁱ	494 – 496	Combined sources	3
Beta strandⁱ	497 – 500	Combined sources	4
Turnⁱ	501 – 504	Combined sources	4
Beta strandⁱ	505 – 509	Combined sources	5
Beta strandⁱ	512 – 521	Combined sources	10
Beta strandⁱ	526 – 532	Combined sources	7
Helixⁱ	533 – 540	Combined sources	8
Helixⁱ	544 – 550	Combined sources	7
Helixⁱ	555 – 564	Combined sources	10
Turnⁱ	565 – 567	Combined sources	3
Beta strandⁱ	569 – 577	Combined sources	9
Beta strandⁱ	588 – 596	Combined sources	9
Helixⁱ	599 – 615	Combined sources	17

Show more details

3D structure databases

Database of protein disorder More...DisProtⁱ	DP00061
ProteinModelPortalⁱ	P27694
SMRⁱ	P27694
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P27694

EvolutionaryTraceⁱ

P27694

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the replication factor A protein 1 family.Curated

Zinc finger

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	481 – 503	C4-typeSequence analysisAdd BLAST		23

Keywords - Domainⁱ

Zinc-finger

Phylogenomic databases

eggNOGⁱ	KOG0851 Eukaryota COG1599 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000012403
HOGENOMⁱ	HOG000162322
HOVERGENⁱ	HBG010502
InParanoidⁱ	P27694
KEGG Orthology (KO) More...KOⁱ	K07466
OMAⁱ	NIYLMDT
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G02VJ
PhylomeDBⁱ	P27694
TreeFamⁱ	TF105241

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd04476 RPA1_DBD_C, 1 hit cd04477 RPA1N, 1 hit
InterProⁱ	View protein in InterPro IPR012340 NA-bd_OB-fold IPR004365 NA-bd_OB_tRNA IPR013955 Rep_factor-A_C IPR007199 Rep_factor-A_N IPR031657 REPA_OB_2 IPR004591 Rfa1
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF04057 Rep-A_N, 1 hit PF08646 Rep_fac-A_C, 1 hit PF16900 REPA_OB_2, 1 hit PF01336 tRNA_anti-codon, 1 hit
SUPFAMⁱ	SSF50249 SSF50249, 4 hits
TIGRFAMsⁱ	TIGR00617 rpa1, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show all Align All

P27694-1 [UniParc]FASTA Add to basket

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        10         20         30         40         50
MVGQLSEGAI AAIMQKGDTN IKPILQVINI RPITTGNSPP RYRLLMSDGL 
        60         70         80         90        100
NTLSSFMLAT QLNPLVEEEQ LSSNCVCQIH RFIVNTLKDG RRVVILMELE 
       110        120        130        140        150
VLKSAEAVGV KIGNPVPYNE GLGQPQVAPP APAASPAASS RPQPQNGSSG 
       160        170        180        190        200
MGSTVSKAYG ASKTFGKAAG PSLSHTSGGT QSKVVPIASL TPYQSKWTIC 
       210        220        230        240        250
ARVTNKSQIR TWSNSRGEGK LFSLELVDES GEIRATAFNE QVDKFFPLIE 
       260        270        280        290        300
VNKVYYFSKG TLKIANKQFT AVKNDYEMTF NNETSVMPCE DDHHLPTVQF 
       310        320        330        340        350
DFTGIDDLEN KSKDSLVDII GICKSYEDAT KITVRSNNRE VAKRNIYLMD 
       360        370        380        390        400
TSGKVVTATL WGEDADKFDG SRQPVLAIKG ARVSDFGGRS LSVLSSSTII 
       410        420        430        440        450
ANPDIPEAYK LRGWFDAEGQ ALDGVSISDL KSGGVGGSNT NWKTLYEVKS 
       460        470        480        490        500
ENLGQGDKPD YFSSVATVVY LRKENCMYQA CPTQDCNKKV IDQQNGLYRC 
       510        520        530        540        550
EKCDTEFPNF KYRMILSVNI ADFQENQWVT CFQESAEAIL GQNAAYLGEL 
       560        570        580        590        600
KDKNEQAFEE VFQNANFRSF IFRVRVKVET YNDESRIKAT VMDVKPVDYR 
       610 
EYGRRLVMSI RRSALM

Length:616

Mass (Da):68,138

Last modified:February 1, 1996 - v2

Checksum:ⁱFE038F40F5886CD1

GO

Computationally mapped potential isoform sequencesⁱ

There are 3 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

I3L2M5	I3L2M5_HUMAN	Replication protein A 70 kDa DNA-bi... Replication protein A 70 kDa DNA-binding subunit	RPA1	153	Annotation score:
I3L524	I3L524_HUMAN	Replication protein A 70 kDa DNA-bi... Replication protein A 70 kDa DNA-binding subunit	RPA1	124	Annotation score:
I3L4R8	I3L4R8_HUMAN	Replication protein A 70 kDa DNA-bi... Replication protein A 70 kDa DNA-binding subunit	RPA1	313	Annotation score:

Sequence cautionⁱ

The sequence BAD92969 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_019236	351	T → A2 PublicationsCorresponds to variant dbSNP:rs5030755Ensembl.		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M63488 mRNA Translation: AAA36584.1 AK289704 mRNA Translation: BAF82393.1 AB209732 mRNA Translation: BAD92969.1 Different initiation. AY599563 Genomic DNA Translation: AAS94324.1 CH471108 Genomic DNA Translation: EAW90574.1 BC018126 mRNA Translation: AAH18126.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS11014.1
PIRⁱ	A40457
NCBI Reference Sequences More...RefSeqⁱ	NP_002936.1, NM_002945.3
UniGeneⁱ	Hs.461925 Hs.595562

Genome annotation databases

Ensemblⁱ	ENST00000254719; ENSP00000254719; ENSG00000132383
GeneIDⁱ	6117
KEGGⁱ	hsa:6117
UCSC genome browser More...UCSCⁱ	uc002fto.3 human

Keywords - Coding sequence diversityⁱ

Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P27694	Replication protein A 70 kDa DNA-binding subunit (Fragment)		HUMAN		153	UniRef100_P27694
Replication protein A 70 kDa DNA-binding subunit (Fragment)		HUMAN		124
UPI00002005C1		HUMAN		603

Protein	Similar proteins		Species	Score	Length	Source
P27694	Replication protein A 70 kDa DNA-binding subunit		PONAB		616	UniRef90_P27694
Replication protein A 70 kDa DNA-binding subunit (Fragment)		HUMAN		153
Replication protein A subunit		CALJA		628
Replication protein A subunit		PAPAN		625
Replication protein A subunit		TARSY		617
+49

Protein	Similar proteins		Species	Score	Length	Source
P27694	Replication protein A 70 kDa DNA-binding subunit		PONAB		616	UniRef50_P27694
Replication protein A 70 kDa DNA-binding subunit		CHICK		614
Replication protein A 70 kDa DNA-binding subunit (Fragment)		HUMAN		153
Replication protein A subunit		CALJA		628
Replication protein A subunit		PAPAN		625
+198

Cross-referencesⁱ

Web resourcesⁱ

NIEHS-SNPs

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M63488 mRNA Translation: AAA36584.1 AK289704 mRNA Translation: BAF82393.1 AB209732 mRNA Translation: BAD92969.1 Different initiation. AY599563 Genomic DNA Translation: AAS94324.1 CH471108 Genomic DNA Translation: EAW90574.1 BC018126 mRNA Translation: AAH18126.1
CCDSⁱ	CCDS11014.1
PIRⁱ	A40457
RefSeqⁱ	NP_002936.1, NM_002945.3
UniGeneⁱ	Hs.461925 Hs.595562

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1EWI	NMR	-	A	1-114	[»]
	1FGU	X-ray	2.50	A/B	182-432	[»]
	1JMC	X-ray	2.40	A	181-422	[»]
	1L1O	X-ray	2.80	C/F	436-616	[»]
	2B29	X-ray	1.60	A	1-120	[»]
	2B3G	X-ray	1.60	A	1-120	[»]
	4IJH	X-ray	1.50	A	1-120	[»]
	4IJL	X-ray	1.70	A	1-120	[»]
	4IPC	X-ray	1.22	A	1-120	[»]
	4IPD	X-ray	1.51	A	1-120	[»]
	4IPG	X-ray	1.58	A	1-120	[»]
	4IPH	X-ray	1.94	A	1-120	[»]
	4LUO	X-ray	1.54	A	1-120	[»]
	4LUV	X-ray	1.40	A	1-120	[»]
	4LUZ	X-ray	1.90	A	1-120	[»]
	4LW1	X-ray	1.63	A	1-120	[»]
	4LWC	X-ray	1.61	A	1-120	[»]
	4NB3	X-ray	1.35	A/B	1-120	[»]
	4O0A	X-ray	1.20	A	1-120	[»]
	4R4C	X-ray	1.40	A	1-120	[»]
	4R4I	X-ray	1.40	A	1-120	[»]
	4R4O	X-ray	1.33	A	1-120	[»]
	4R4Q	X-ray	1.35	A	1-120	[»]
	4R4T	X-ray	1.28	A	1-120	[»]
	5E7N	X-ray	1.21	A	1-120	[»]
	5EAY	X-ray	1.55	A/B/C/D	3-120	[»]
	5N85	X-ray	2.00	A	1-120	[»]
	5N8A	X-ray	1.28	A	1-120	[»]
DisProtⁱ	DP00061
ProteinModelPortalⁱ	P27694
SMRⁱ	P27694
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	112037, 485 interactors
CORUMⁱ	P27694
DIPⁱ	DIP-24189N
IntActⁱ	P27694, 77 interactors
MINTⁱ	P27694
STRINGⁱ	9606.ENSP00000254719

Chemistry databases

BindingDBⁱ	P27694
ChEMBLⁱ	CHEMBL1764940

PTM databases

iPTMnetⁱ	P27694
PhosphoSitePlusⁱ	P27694
SwissPalmⁱ	P27694

Polymorphism and mutation databases

BioMutaⁱ	RPA1
DMDMⁱ	1350579

Proteomic databases

EPDⁱ	P27694
MaxQBⁱ	P27694
PaxDbⁱ	P27694
PeptideAtlasⁱ	P27694
PRIDEⁱ	P27694
ProteomicsDBⁱ	54405

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	6117
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000254719; ENSP00000254719; ENSG00000132383
GeneIDⁱ	6117
KEGGⁱ	hsa:6117
UCSCⁱ	uc002fto.3 human

Organism-specific databases

CTDⁱ	6117
DisGeNETⁱ	6117
EuPathDBⁱ	HostDB:ENSG00000132383.11
GeneCardsⁱ	RPA1
HGNCⁱ	HGNC:10289 RPA1
HPAⁱ	CAB004563 HPA006914 HPA046497
MIMⁱ	179835 gene
neXtProtⁱ	NX_P27694
OpenTargetsⁱ	ENSG00000132383
PharmGKBⁱ	PA34651
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0851 Eukaryota COG1599 LUCA
GeneTreeⁱ	ENSGT00390000012403
HOGENOMⁱ	HOG000162322
HOVERGENⁱ	HBG010502
InParanoidⁱ	P27694
KOⁱ	K07466
OMAⁱ	NIYLMDT
OrthoDBⁱ	EOG091G02VJ
PhylomeDBⁱ	P27694
TreeFamⁱ	TF105241

Enzyme and pathway databases

Reactomeⁱ	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

Reactomeⁱ

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

Miscellaneous databases

ChiTaRSⁱ	RPA1 human
EvolutionaryTraceⁱ	P27694
GeneWikiⁱ	Replication_protein_A1
GenomeRNAiⁱ	6117
Protein Ontology More...PROⁱ	PR:P27694
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000132383 Expressed in 235 organ(s), highest expression level in secondary oocyte
CleanExⁱ	HS_RPA1
ExpressionAtlasⁱ	P27694 baseline and differential
Genevisibleⁱ	P27694 HS

Family and domain databases

CDDⁱ	cd04476 RPA1_DBD_C, 1 hit cd04477 RPA1N, 1 hit
InterProⁱ	View protein in InterPro IPR012340 NA-bd_OB-fold IPR004365 NA-bd_OB_tRNA IPR013955 Rep_factor-A_C IPR007199 Rep_factor-A_N IPR031657 REPA_OB_2 IPR004591 Rfa1
Pfamⁱ	View protein in Pfam PF04057 Rep-A_N, 1 hit PF08646 Rep_fac-A_C, 1 hit PF16900 REPA_OB_2, 1 hit PF01336 tRNA_anti-codon, 1 hit
SUPFAMⁱ	SSF50249 SSF50249, 4 hits
TIGRFAMsⁱ	TIGR00617 rpa1, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	RFA1_HUMAN
Accessionⁱ	P27694Primary (citable) accession number: P27694 Secondary accession number(s): A8K0Y9, Q59ES9
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
	Last sequence update:	February 1, 1996
	Last modified:	November 7, 2018
	This is version 202 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
Human chromosome 17
Human chromosome 17: entries, gene names and cross-references to MIM
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

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UniProtKB - P27694 (RFA1_HUMAN)

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Replication protein A 70 kDa DNA-binding subunit

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Keywords - Domaini

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ