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. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair (BER) probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance.By similarity

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
DNA bindingⁱ	206 – 290	OBAdd BLAST		85

GO - Molecular functionⁱ

chromatin binding
Source: MGI
Inferred from direct assayⁱ
- 12091911
damaged DNA binding Source: UniProtKB
G-rich strand telomeric DNA binding Source: MGI
metal ion binding Source: UniProtKB-KW
single-stranded DNA binding Source: UniProtKB

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

base-excision repair Source: UniProtKB
chromosome organization
Source: MGI
Inferred from mutant phenotypeⁱ
- 15965476
DNA repair Source: MGI
DNA replication Source: UniProtKB
double-strand break repair via homologous recombination
Source: MGI
Inferred from mutant phenotypeⁱ
- 15470499
hemopoiesis
Source: MGI
Inferred from mutant phenotypeⁱ
- 15965476
homeostasis of number of cells within a tissue
Source: MGI
Inferred from mutant phenotypeⁱ
- 15965476
in utero embryonic development
Source: MGI
Inferred from mutant phenotypeⁱ
- 15470499
meiotic cell cycle
Source: MGI
Inferred from direct assayⁱ
- 12091911
mismatch repair Source: UniProtKB
nucleotide-excision repair Source: UniProtKB
positive regulation of cell proliferation
Source: MGI
Inferred from mutant phenotypeⁱ
- 15965476
protein localization to chromosome Source: UniProtKB
telomere maintenance Source: MGI

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-MMU-110312. Translesion synthesis by REV1. R-MMU-110314. Recognition of DNA damage by PCNA-containing replication complex. R-MMU-110320. Translesion Synthesis by POLH. R-MMU-174437. Removal of the Flap Intermediate from the C-strand. R-MMU-176187. Activation of ATR in response to replication stress. R-MMU-3108214. SUMOylation of DNA damage response and repair proteins. R-MMU-3371453. Regulation of HSF1-mediated heat shock response. R-MMU-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha). R-MMU-5358606. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta). R-MMU-5651801. PCNA-Dependent Long Patch Base Excision Repair. R-MMU-5655862. Translesion synthesis by POLK. R-MMU-5656121. Translesion synthesis by POLI. R-MMU-5656169. Termination of translesion DNA synthesis. R-MMU-5685938. HDR through Single Strand Annealing (SSA). R-MMU-5685942. HDR through Homologous Recombination (HRR). R-MMU-5693607. Processing of DNA double-strand break ends. R-MMU-5693616. Presynaptic phase of homologous DNA pairing and strand exchange. R-MMU-5696395. Formation of Incision Complex in GG-NER. R-MMU-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER. R-MMU-5696400. Dual Incision in GG-NER. R-MMU-6782135. Dual incision in TC-NER. R-MMU-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER. R-MMU-6783310. Fanconi Anemia Pathway. R-MMU-6804756. Regulation of TP53 Activity through Phosphorylation. R-MMU-68962. Activation of the pre-replicative complex. R-MMU-69166. Removal of the Flap Intermediate. R-MMU-69473. G2/M DNA damage checkpoint. R-MMU-912497. Meiotic Recombination.

Reactomeⁱ

R-MMU-110312. Translesion synthesis by REV1.
R-MMU-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-MMU-110320. Translesion Synthesis by POLH.
R-MMU-174437. Removal of the Flap Intermediate from the C-strand.
R-MMU-176187. Activation of ATR in response to replication stress.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.
R-MMU-3371453. Regulation of HSF1-mediated heat shock response.
R-MMU-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
R-MMU-5358606. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
R-MMU-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-MMU-5655862. Translesion synthesis by POLK.
R-MMU-5656121. Translesion synthesis by POLI.
R-MMU-5656169. Termination of translesion DNA synthesis.
R-MMU-5685938. HDR through Single Strand Annealing (SSA).
R-MMU-5685942. HDR through Homologous Recombination (HRR).
R-MMU-5693607. Processing of DNA double-strand break ends.
R-MMU-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-MMU-5696395. Formation of Incision Complex in GG-NER.
R-MMU-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-MMU-5696400. Dual Incision in GG-NER.
R-MMU-6782135. Dual incision in TC-NER.
R-MMU-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-MMU-6783310. Fanconi Anemia Pathway.
R-MMU-6804756. Regulation of TP53 Activity through Phosphorylation.
R-MMU-68962. Activation of the pre-replicative complex.
R-MMU-69166. Removal of the Flap Intermediate.
R-MMU-69473. G2/M DNA damage checkpoint.
R-MMU-912497. 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
Gene namesⁱ	Name:Rpa1
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [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 › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 11

Organism-specific databases

MGIⁱ	MGI:1915525. Rpa1.

Keywords - Cellular componentⁱ

Nucleus

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000097261	1 – 623	Replication protein A 70 kDa DNA-binding subunitAdd BLAST		623

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	1	N-acetylmethionineBy similarity	1
Cross-linkⁱ	22	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linkⁱ	88	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residueⁱ	172	N6-acetyllysine; alternateCombined sources	1
Cross-linkⁱ	172	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residueⁱ	176	N6-acetyllysine; alternateCombined sources	1
Cross-linkⁱ	176	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residueⁱ	189	PhosphothreonineBy similarity	1
Cross-linkⁱ	192	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residueⁱ	200	PhosphothreonineBy similarity	1
Cross-linkⁱ	229	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linkⁱ	253	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residueⁱ	268	N6-acetyllysine; alternateBy similarity	1
Cross-linkⁱ	268	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linkⁱ	276	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linkⁱ	340	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residueⁱ	393	PhosphoserineBy similarity	1
Cross-linkⁱ	419	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linkⁱ	458	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linkⁱ	467	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linkⁱ	562	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linkⁱ	586	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

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. 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.By similarity

Sumoylated on lysine residues Lys-458 and Lys-586, with Lys-458 being the major site. Sumoylation promotes recruitment of RAD51 to the DNA damage foci to initiate DNA repair through homologous recombination. Desumoylated by SENP6 (By similarity).By similarity

Keywords - PTMⁱ

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	Q8VEE4.
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q8VEE4.
PaxDbⁱ	Q8VEE4.
PeptideAtlas More...PeptideAtlasⁱ	Q8VEE4.
PRIDEⁱ	Q8VEE4.

PTM databases

iPTMnetⁱ	Q8VEE4.
PhosphoSitePlusⁱ	Q8VEE4.

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSMUSG00000000751.
CleanExⁱ	MM_RPA1.
ExpressionAtlasⁱ	Q8VEE4. baseline and differential.
Genevisibleⁱ	Q8VEE4. MM.

Interactionⁱ

Subunit structureⁱ

Component of the canonical replication protein A complex (RPA), a heterotrimer composed of RPA1, RPA2 and RPA3. The DNA-binding activity may reside exclusively on the RPA1 subunit. Interacts with PRPF19; the PRP19-CDC5L complex is recruited to the sites of DNA repair where it ubiquitinates the replication protein A complex (RPA). Interacts with RIPK1. Interacts with the polymerase alpha subunit POLA1/p180; this interaction stabilizes the replicative complex and reduces the misincorporation rate of DNA polymerase alpha by acting as a fidelity clamp. Interacts with RAD51 and SENP6 to regulate DNA repair. Interacts with HELB; this interaction promotes HELB recruitment to chromatin following DNA damage. Interacts with PRIMPOL. Interacts with XPA; the interaction is direct and associates XPA with the RPA complex. Interacts with ETAA1; the interaction is direct and promotes ETAA1 recruitment at stalled replication forks.By similarity

Protein-protein interaction databases

BioGridⁱ	212778. 7 interactors.
CORUMⁱ	Q8VEE4.
IntActⁱ	Q8VEE4. 3 interactors.
STRINGⁱ	10090.ENSMUSP00000000767.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q8VEE4.
SMRⁱ	Q8VEE4.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the replication factor A protein 1 family.Curated

Keywords - Domainⁱ

Zinc-finger

Phylogenomic databases

eggNOGⁱ	KOG0851. Eukaryota. COG1599. LUCA.
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000012403.
HOGENOMⁱ	HOG000162322.
HOVERGENⁱ	HBG010502.
InParanoidⁱ	Q8VEE4.
KEGG Orthology (KO) More...KOⁱ	K07466.
PhylomeDBⁱ	Q8VEE4.

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.

Sequenceⁱ

Sequence statusⁱ: Complete.

Q8VEE4-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MVGHLSEGAI EVMIQQENTS IKPILQVINI RPISTGNRSP RYRLLMSDGL 
        60         70         80         90        100
NTLSSFMLAT QLNTLVEGGQ LASNCVCQVH KFIVNTLKDG RKVVVLMDLE 
       110        120        130        140        150
VMKSAEDVGL KIGNPVPYNE GYGQQQQQQQ QQQQQAVPSP ASAATPPASK 
       160        170        180        190        200
PQPQNGSLGM GSTAAKAYGA SKPFGKPAGT GLLQPSGGTQ SKVVPIASLT 
       210        220        230        240        250
PYQSKWTICA RVTNKSQIRT WSNSRGEGKL FSLELVDESG EIRATAFNEQ 
       260        270        280        290        300
VDKFFPLIEV NKVYYFSKGA LKIANKQFSA VKNDYEMTFN NETSVLPCED 
       310        320        330        340        350
GHHLPTVQFD FTGIGDLESK AKDALVDIIG ICKSYEDSIK ITVKSNNREV 
       360        370        380        390        400
AKRNIYLMDM SGKVVTTTLW GEDADKFDGS RQPVMAIKGA RVSDFGGRSL 
       410        420        430        440        450
SVLSSSTVIV NPDIPEAYKL RGWFDSEGQA LDGVSISDHR SGGAGGGNTN 
       460        470        480        490        500
WKTLHEAKSE NLGQGDKADY FSTVAAVVFL RKENCMYQAC PTQDCNKKVI 
       510        520        530        540        550
DQQNGLYRCE KCDREFPNFK YRMILSANIA DFQENQWVTC FQESAEAILG 
       560        570        580        590        600
QNTMYLGELK EKNEQAFEEV FQNANFRSFT FRIRVKLETY NDESRIKATV 
       610        620 
MDVKPVDFRD YGRRLIANIR KNM

Length:623

Mass (Da):69,037

Last modified:March 1, 2002 - v1

Checksum:ⁱ2317F69F1E51B657

GO

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱ	134 – 135	Missing 1 Publication		2

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AK148035 mRNA. Translation: BAE28302.1. AK150785 mRNA. Translation: BAE29849.1. AK151590 mRNA. Translation: BAE30530.1. AK153144 mRNA. Translation: BAE31755.1. AK165316 mRNA. Translation: BAE38134.1. AK165944 mRNA. Translation: BAE38476.1. AK167598 mRNA. Translation: BAE39655.1. AK169599 mRNA. Translation: BAE41250.1. AL603834 Genomic DNA. No translation available. BC019119 mRNA. Translation: AAH19119.1.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS25044.1.
NCBI Reference Sequences More...RefSeqⁱ	NP_001157695.1. NM_001164223.1. NP_080929.1. NM_026653.2.
UniGeneⁱ	Mm.102574. Mm.180734. Mm.254027. Mm.472099.

Genome annotation databases

Ensemblⁱ	ENSMUST00000092907; ENSMUSP00000090585; ENSMUSG00000000751.
GeneIDⁱ	68275.
KEGGⁱ	mmu:68275.
UCSC genome browser More...UCSCⁱ	uc007kdi.2. mouse.

Keywords - Coding sequence diversityⁱ

Polymorphism

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
Q8VEE4	UPI000A30EFB4 UPI0004549BE8 UPI000A316BCC A0A0S3NTW6 A0A1U7Q438 A0A0G2KAT3 UPI00038C23F9 UPI00042AE0BA UPI000B4F1FD1 A0A1A6HZH2 +1	Mus pahari (Gairdner's shrew-mouse) (Coelomys pahari) Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) Mus caroli (Ryukyu mouse) (Ricefield mouse) Tokudaia muenninki (Okinawa island spiny rat) Mesocricetus auratus (Golden hamster) Rattus norvegicus (Rat) Microtus ochrogaster (Prairie vole) Peromyscus maniculatus bairdii (Prairie deer mouse) Meriones unguiculatus (Mongolian jird) (Mongolian gerbil) Neotoma lepida (Desert woodrat)	623	UniRef90_Q8VEE4	Cluster: Replication protein A 70 kDa DNA-binding subunit	12

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
Q8VEE4	UPI000A30EFB4 UPI0004549BE8 UPI000A316BCC A0A0S3NTW6 A0A0G2KAT3 UPI00038C23F9 UPI00042AE0BA UPI000B4F1FD1 A0A1U7Q438 A0A1A6HZH2 +11	Mus pahari (Gairdner's shrew-mouse) (Coelomys pahari) Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) Mus caroli (Ryukyu mouse) (Ricefield mouse) Tokudaia muenninki (Okinawa island spiny rat) Rattus norvegicus (Rat) Microtus ochrogaster (Prairie vole) Peromyscus maniculatus bairdii (Prairie deer mouse) Meriones unguiculatus (Mongolian jird) (Mongolian gerbil) Mesocricetus auratus (Golden hamster) Neotoma lepida (Desert woodrat) And more	623	UniRef50_Q8VEE4	Cluster: Replication protein A 70 kDa DNA-binding subunit	22

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AK148035 mRNA. Translation: BAE28302.1. AK150785 mRNA. Translation: BAE29849.1. AK151590 mRNA. Translation: BAE30530.1. AK153144 mRNA. Translation: BAE31755.1. AK165316 mRNA. Translation: BAE38134.1. AK165944 mRNA. Translation: BAE38476.1. AK167598 mRNA. Translation: BAE39655.1. AK169599 mRNA. Translation: BAE41250.1. AL603834 Genomic DNA. No translation available. BC019119 mRNA. Translation: AAH19119.1.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS25044.1.
NCBI Reference Sequences More...RefSeqⁱ	NP_001157695.1. NM_001164223.1. NP_080929.1. NM_026653.2.
UniGeneⁱ	Mm.102574. Mm.180734. Mm.254027. Mm.472099.

3D structure databases

ProteinModelPortalⁱ	Q8VEE4.
SMRⁱ	Q8VEE4.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	212778. 7 interactors.
CORUMⁱ	Q8VEE4.
IntActⁱ	Q8VEE4. 3 interactors.
STRINGⁱ	10090.ENSMUSP00000000767.

PTM databases

iPTMnetⁱ	Q8VEE4.
PhosphoSitePlusⁱ	Q8VEE4.

Proteomic databases

EPDⁱ	Q8VEE4.
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q8VEE4.
PaxDbⁱ	Q8VEE4.
PeptideAtlas More...PeptideAtlasⁱ	Q8VEE4.
PRIDEⁱ	Q8VEE4.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSMUST00000092907; ENSMUSP00000090585; ENSMUSG00000000751.
GeneIDⁱ	68275.
KEGGⁱ	mmu:68275.
UCSC genome browser More...UCSCⁱ	uc007kdi.2. mouse.

Organism-specific databases

CTDⁱ	6117.
MGIⁱ	MGI:1915525. Rpa1.

Phylogenomic databases

eggNOGⁱ	KOG0851. Eukaryota. COG1599. LUCA.
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000012403.
HOGENOMⁱ	HOG000162322.
HOVERGENⁱ	HBG010502.
InParanoidⁱ	Q8VEE4.
KEGG Orthology (KO) More...KOⁱ	K07466.
PhylomeDBⁱ	Q8VEE4.

Enzyme and pathway databases

Reactomeⁱ	R-MMU-110312. Translesion synthesis by REV1. R-MMU-110314. Recognition of DNA damage by PCNA-containing replication complex. R-MMU-110320. Translesion Synthesis by POLH. R-MMU-174437. Removal of the Flap Intermediate from the C-strand. R-MMU-176187. Activation of ATR in response to replication stress. R-MMU-3108214. SUMOylation of DNA damage response and repair proteins. R-MMU-3371453. Regulation of HSF1-mediated heat shock response. R-MMU-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha). R-MMU-5358606. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta). R-MMU-5651801. PCNA-Dependent Long Patch Base Excision Repair. R-MMU-5655862. Translesion synthesis by POLK. R-MMU-5656121. Translesion synthesis by POLI. R-MMU-5656169. Termination of translesion DNA synthesis. R-MMU-5685938. HDR through Single Strand Annealing (SSA). R-MMU-5685942. HDR through Homologous Recombination (HRR). R-MMU-5693607. Processing of DNA double-strand break ends. R-MMU-5693616. Presynaptic phase of homologous DNA pairing and strand exchange. R-MMU-5696395. Formation of Incision Complex in GG-NER. R-MMU-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER. R-MMU-5696400. Dual Incision in GG-NER. R-MMU-6782135. Dual incision in TC-NER. R-MMU-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER. R-MMU-6783310. Fanconi Anemia Pathway. R-MMU-6804756. Regulation of TP53 Activity through Phosphorylation. R-MMU-68962. Activation of the pre-replicative complex. R-MMU-69166. Removal of the Flap Intermediate. R-MMU-69473. G2/M DNA damage checkpoint. R-MMU-912497. Meiotic Recombination.

Reactomeⁱ

R-MMU-110312. Translesion synthesis by REV1.
R-MMU-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-MMU-110320. Translesion Synthesis by POLH.
R-MMU-174437. Removal of the Flap Intermediate from the C-strand.
R-MMU-176187. Activation of ATR in response to replication stress.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.
R-MMU-3371453. Regulation of HSF1-mediated heat shock response.
R-MMU-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
R-MMU-5358606. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
R-MMU-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-MMU-5655862. Translesion synthesis by POLK.
R-MMU-5656121. Translesion synthesis by POLI.
R-MMU-5656169. Termination of translesion DNA synthesis.
R-MMU-5685938. HDR through Single Strand Annealing (SSA).
R-MMU-5685942. HDR through Homologous Recombination (HRR).
R-MMU-5693607. Processing of DNA double-strand break ends.
R-MMU-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-MMU-5696395. Formation of Incision Complex in GG-NER.
R-MMU-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-MMU-5696400. Dual Incision in GG-NER.
R-MMU-6782135. Dual incision in TC-NER.
R-MMU-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-MMU-6783310. Fanconi Anemia Pathway.
R-MMU-6804756. Regulation of TP53 Activity through Phosphorylation.
R-MMU-68962. Activation of the pre-replicative complex.
R-MMU-69166. Removal of the Flap Intermediate.
R-MMU-69473. G2/M DNA damage checkpoint.
R-MMU-912497. Meiotic Recombination.

Miscellaneous databases

ChiTaRSⁱ	Rpa1. mouse.
Protein Ontology More...PROⁱ	PR:Q8VEE4.
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000000751.
CleanExⁱ	MM_RPA1.
ExpressionAtlasⁱ	Q8VEE4. baseline and differential.
Genevisibleⁱ	Q8VEE4. MM.

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.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	RFA1_MOUSE
Accessionⁱ	Q8VEE4Primary (citable) accession number: Q8VEE4 Secondary accession number(s): Q3TEJ8
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
	Last sequence update:	March 1, 2002
	Last modified:	March 28, 2018
	This is version 141 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q8VEE4 (RFA1_MOUSE)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Replication protein A 70 kDa DNA-binding subunit

Select a section on the left to see content.

<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

<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 - 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

<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

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

<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

<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

3D structure 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

Phylogenomic databases

Family and domain databases

Natural variant

Sequence databases

Genome annotation databases

<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

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM 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

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ