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Protein

Replication protein A 70 kDa DNA-binding subunit

Gene

Rpa1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

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

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.
R-MMU-912446. Meiotic recombination.
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
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-acetyllysineCombined sources1
Cross-linki172Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei176N6-acetyllysineCombined sources1
Cross-linki176Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By 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-acetyllysineBy similarity1
Cross-linki268Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By 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.

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. 6 interactors.
CORUMiQ8VEE4.
IntActiQ8VEE4. 2 interactors.
STRINGi10090.ENSMUSP00000000767.

Structurei

3D structure databases

ProteinModelPortaliQ8VEE4.
SMRiQ8VEE4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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. Translation: CAI23976.1.
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: September 27, 2017
This is version 136 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