Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q8VEE4 (RFA1_MOUSE)

(max 400 entries)x

Your basket is currently empty. i

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Replication protein A 70 kDa DNA-binding subunit

Gene

Rpa1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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 keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi206 – 290OBAdd BLAST85

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

  • base-excision repair Source: UniProtKB
  • chromosome organization Source: MGI
  • DNA repair Source: MGI
  • DNA replication Source: UniProtKB
  • double-strand break repair via homologous recombination Source: MGI
  • hemopoiesis Source: MGI
  • homeostasis of number of cells within a tissue Source: MGI
  • in utero embryonic development Source: MGI
  • meiotic cell cycle Source: MGI
  • mismatch repair Source: UniProtKB
  • nucleotide-excision repair Source: UniProtKB
  • positive regulation of cell proliferation Source: MGI
  • protein localization to chromosome Source: UniProtKB
  • telomere maintenance Source: MGI
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionDNA-binding
Biological processDNA damage, DNA recombination, DNA repair, DNA replication
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-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

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1915525 Rpa1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000972611 – 623Replication protein A 70 kDa DNA-binding subunitAdd BLAST623

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Cross-linki22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki88Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei172N6-acetyllysine; alternateCombined sources1
Cross-linki172Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei176N6-acetyllysine; alternateCombined sources1
Cross-linki176Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei189PhosphothreonineBy similarity1
Cross-linki192Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei200PhosphothreonineBy similarity1
Cross-linki229Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki253Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei268N6-acetyllysine; alternateBy similarity1
Cross-linki268Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki276Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki340Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei393PhosphoserineBy similarity1
Cross-linki419Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki458Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki467Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki562Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki586Glycyl 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

EPDiQ8VEE4
MaxQBiQ8VEE4
PaxDbiQ8VEE4
PeptideAtlasiQ8VEE4
PRIDEiQ8VEE4

PTM databases

iPTMnetiQ8VEE4
PhosphoSitePlusiQ8VEE4
SwissPalmiQ8VEE4

Expressioni

Gene expression databases

BgeeiENSMUSG00000000751
CleanExiMM_RPA1
ExpressionAtlasiQ8VEE4 baseline and differential
GenevisibleiQ8VEE4 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

BioGridi212778, 7 interactors
CORUMiQ8VEE4
IntActiQ8VEE4, 3 interactors
STRINGi10090.ENSMUSP00000000767

Structurei

3D structure databases

ProteinModelPortaliQ8VEE4
SMRiQ8VEE4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the replication factor A protein 1 family.Curated

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0851 Eukaryota
COG1599 LUCA
GeneTreeiENSGT00390000012403
HOGENOMiHOG000162322
HOVERGENiHBG010502
InParanoidiQ8VEE4
KOiK07466
PhylomeDBiQ8VEE4

Family and domain databases

CDDicd04476 RPA1_DBD_C, 1 hit
cd04477 RPA1N, 1 hit
InterProiView 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
PfamiView 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
SUPFAMiSSF50249 SSF50249, 4 hits
TIGRFAMsiTIGR00617 rpa1, 1 hit

Sequencei

Sequence statusi: Complete.

Q8VEE4-1 [UniParc]FASTAAdd 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 keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti134 – 135Missing 1 Publication2

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
CCDSiCCDS25044.1
RefSeqiNP_001157695.1, NM_001164223.1
NP_080929.1, NM_026653.2
UniGeneiMm.102574
Mm.180734
Mm.254027
Mm.472099

Genome annotation databases

EnsembliENSMUST00000092907; ENSMUSP00000090585; ENSMUSG00000000751
GeneIDi68275
KEGGimmu:68275
UCSCiuc007kdi.2 mouse

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiRFA1_MOUSE
AccessioniPrimary (citable) accession number: Q8VEE4
Secondary accession number(s): Q3TEJ8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: March 1, 2002
Last modified: May 23, 2018
This is version 142 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health