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Entry version 159 (07 Oct 2020)
Sequence version 1 (01 Mar 2002)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi206 – 290OBAdd BLAST85

<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

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
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

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Rpa1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1915525, Rpa1

<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

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

Keywords - Cellular componenti

Nucleus

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000972611 – 623Replication protein A 70 kDa DNA-binding subunitAdd BLAST623

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

More...
EPDi
Q8VEE4

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q8VEE4

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q8VEE4

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q8VEE4

PeptideAtlas

More...
PeptideAtlasi
Q8VEE4

PRoteomics IDEntifications database

More...
PRIDEi
Q8VEE4

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q8VEE4

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q8VEE4

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q8VEE4

<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

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000000751, Expressed in primary oocyte and 313 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q8VEE4, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q8VEE4, MM

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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; leading to recruit PRIMPOL on chromatin and stimulate its DNA primase activity.

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.

Interacts with RPA1; this interaction associates HROB with the RPA complex (PubMed:31467087).

By similarity1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
212778, 40 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q8VEE4

Protein interaction database and analysis system

More...
IntActi
Q8VEE4, 4 interactors

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000000767

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q8VEE4, protein

<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

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q8VEE4

Database of comparative protein structure models

More...
ModBasei
Search...

<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

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0851, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00390000012403

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_012393_2_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q8VEE4

KEGG Orthology (KO)

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KOi
K07466

Identification of Orthologs from Complete Genome Data

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OMAi
YRLLINM

Database of Orthologous Groups

More...
OrthoDBi
1189265at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q8VEE4

Family and domain databases

Conserved Domains Database

More...
CDDi
cd04476, RPA1_DBD_C, 1 hit
cd04477, RPA1N, 1 hit

Integrated resource of protein families, domains and functional sites

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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

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50249, SSF50249, 4 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00617, rpa1, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2317F69F1E51B657
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5SWN2Q5SWN2_MOUSE
Replication protein A subunit
Rpa1
644Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti134 – 135Missing 1 Publication2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000092907; ENSMUSP00000090585; ENSMUSG00000000751

Database of genes from NCBI RefSeq genomes

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GeneIDi
68275

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:68275

UCSC genome browser

More...
UCSCi
uc007kdi.2, mouse

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

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

3D structure databases

SMRiQ8VEE4
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi212778, 40 interactors
CORUMiQ8VEE4
IntActiQ8VEE4, 4 interactors
STRINGi10090.ENSMUSP00000000767

PTM databases

iPTMnetiQ8VEE4
PhosphoSitePlusiQ8VEE4
SwissPalmiQ8VEE4

Proteomic databases

EPDiQ8VEE4
jPOSTiQ8VEE4
MaxQBiQ8VEE4
PaxDbiQ8VEE4
PeptideAtlasiQ8VEE4
PRIDEiQ8VEE4

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
1868, 465 antibodies

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
6117
MGIiMGI:1915525, Rpa1

Phylogenomic databases

eggNOGiKOG0851, Eukaryota
GeneTreeiENSGT00390000012403
HOGENOMiCLU_012393_2_1_1
InParanoidiQ8VEE4
KOiK07466
OMAiYRLLINM
OrthoDBi1189265at2759
PhylomeDBiQ8VEE4

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

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
68275, 7 hits in 20 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Rpa1, mouse

Protein Ontology

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PROi
PR:Q8VEE4
RNActiQ8VEE4, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSMUSG00000000751, Expressed in primary oocyte and 313 other tissues
ExpressionAtlasiQ8VEE4, baseline and differential
GenevisibleiQ8VEE4, MM

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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRFA1_MOUSE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q8VEE4
Secondary accession number(s): Q3TEJ8
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: March 1, 2002
Last modified: October 7, 2020
This is version 159 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<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

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
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