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UniProtKB - P27694 (RFA1_HUMAN)

Entry version 222 (02 Jun 2021)
Sequence version 2 (01 Feb 1996)
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Protein

Replication protein A 70 kDa DNA-binding subunit

Gene

RPA1

Organism
Homo sapiens (Human)
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 (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 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 bindingi197 – 281OBAdd BLAST85
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri481 – 503C4-typeSequence analysisAdd BLAST23

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P27694

Reactome - a knowledgebase of biological pathways and processes

More...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

SIGNOR Signaling Network Open Resource

More...SIGNORi		P27694

<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
Single-stranded DNA-binding protein
Cleaved into the following chain:
Replication protein A 70 kDa DNA-binding subunit, N-terminally processed
<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
Synonyms:REPA1, RPA70
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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
  • UP000005640 <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 17

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:10289, RPA1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		179835, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P27694

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000132383.11

<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

Keywords - Cellular componenti

Nucleus

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi41R → E: Loss of HELB-binding; when associated with E-43. 1 Publication1
Mutagenesisi43R → E: Loss of HELB-binding; when associated with E-41. 1 Publication1
Mutagenesisi449K → R: Significant reduction of sumoylation. Loss of sumoylation; when associated with R-577. 1 Publication1
Mutagenesisi500C → S: Loss of function in DNA replication and mismatch repair without effect on DNA-binding activity; when associated with S-503. 1 Publication1
Mutagenesisi503C → S: Loss of function in DNA replication and mismatch repair without effect on DNA-binding activity; when associated with S-500. 1 Publication1
Mutagenesisi577K → R: Slight sumoylation decrease. Loss of sumoylation; when associated with R-449. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		6117

Open Targets

More...OpenTargetsi		ENSG00000132383

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA34651

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P27694, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1764940

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		RPA1

Domain mapping of disease mutations (DMDM)

More...DMDMi		1350579

<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_00004232311 – 616Replication protein A 70 kDa DNA-binding subunitAdd BLAST616
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved; alternate1 Publication
ChainiPRO_00000972602 – 616Replication protein A 70 kDa DNA-binding subunit, N-terminally processedAdd BLAST615

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-acetylmethionineCombined sources1
<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)1 Publication
Cross-linki88Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei163N6-acetyllysine; alternateCombined sources1
Cross-linki163Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei167N6-acetyllysine; alternateCombined sources1
Cross-linki167Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei180PhosphothreonineCombined sources1
Cross-linki183Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei191PhosphothreonineCombined sources1
Cross-linki220Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki244Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei259N6-acetyllysine; alternateCombined sources1
Cross-linki259Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Cross-linki267Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki331Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei384PhosphoserineCombined sources1
Cross-linki410Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki431Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki449Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki458Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki553Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki577Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

<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 (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

Encyclopedia of Proteome Dynamics

More...EPDi		P27694

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P27694

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P27694

MaxQB - The MaxQuant DataBase

More...MaxQBi		P27694

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

More...PaxDbi		P27694

PeptideAtlas

More...PeptideAtlasi		P27694

PRoteomics IDEntifications database

More...PRIDEi		P27694

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		54405

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P27694

MetOSite database of methionine sulfoxide sites

More...MetOSitei		P27694

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

More...PhosphoSitePlusi		P27694

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P27694

<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		ENSG00000132383, Expressed in secondary oocyte and 248 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P27694, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P27694, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000132383, Low tissue specificity

<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 (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; leading to recruit PRIMPOL on chromatin and stimulate its DNA primase activity (PubMed:24126761, PubMed:25550423, PubMed:28534480).

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).

Interacts with RPA1; this interaction associates HROB with the RPA complex (By similarity).

By similarity17 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		112037, 558 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P27694

Database of interacting proteins

More...DIPi		DIP-24189N

Protein interaction database and analysis system

More...IntActi		P27694, 92 interactors

Molecular INTeraction database

More...MINTi		P27694

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000254719

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P27694

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P27694, 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

Secondary structure

1616
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		P27694

Small Angle Scattering Biological Data Bank

More...SASBDBi		P27694

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

More...SMRi		P27694

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P27694

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni121 – 154DisorderedSequence analysisAdd BLAST34

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi138 – 154Polar residuesSequence analysisAdd BLAST17

<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

Belongs to the replication factor A protein 1 family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri481 – 503C4-typeSequence analysisAdd BLAST23

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0851, Eukaryota

Ensembl GeneTree

More...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		P27694

Identification of Orthologs from Complete Genome Data

More...OMAi		YRLLINM

Database of Orthologous Groups

More...OrthoDBi		1189265at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P27694

TreeFam database of animal gene trees

More...TreeFami		TF105241

Family and domain databases

Conserved Domains Database

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

Database of protein disorder

More...DisProti		DP00061

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID00036

Integrated resource of protein families, domains and functional sites

More...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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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 allAlign All

P27694-1 [UniParc]FASTAAdd to basket
« Hide
        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
<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:iFE038F40F5886CD1
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 are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
I3L2M5I3L2M5_HUMAN
Replication protein A 70 kDa DNA-bi...
RPA1
153Annotation score:

Annotation score:1 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>
I3L524I3L524_HUMAN
Replication protein A 70 kDa DNA-bi...
RPA1
124Annotation score:

Annotation score:1 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>
I3L4R8I3L4R8_HUMAN
Replication protein A 70 kDa DNA-bi...
RPA1
313Annotation score:

Annotation score:1 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>

<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

The sequence BAD92969 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

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 variantiVAR_019236351T → A2 PublicationsCorresponds to variant dbSNP:rs5030755Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

Protein sequence database of the Protein Information Resource

More...PIRi		A40457

NCBI Reference Sequences

More...RefSeqi		NP_002936.1, NM_002945.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000254719; ENSP00000254719; ENSG00000132383

Database of genes from NCBI RefSeq genomes

More...GeneIDi		6117

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:6117

UCSC genome browser

More...UCSCi		uc002fto.3, human

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">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

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
CCDSiCCDS11014.1
PIRiA40457
RefSeqiNP_002936.1, NM_002945.3

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 entryMethodResolution (Å)ChainPositionsPDBsum
1EWINMR-A1-114[»]
1FGUX-ray2.50A/B182-432[»]
1JMCX-ray2.40A181-422[»]
1L1OX-ray2.80C/F436-616[»]
2B29X-ray1.60A1-120[»]
2B3GX-ray1.60A1-120[»]
4IJHX-ray1.50A1-120[»]
4IJLX-ray1.70A1-120[»]
4IPCX-ray1.22A1-120[»]
4IPDX-ray1.51A1-120[»]
4IPGX-ray1.58A1-120[»]
4IPHX-ray1.94A1-120[»]
4LUOX-ray1.54A1-120[»]
4LUVX-ray1.40A1-120[»]
4LUZX-ray1.90A1-120[»]
4LW1X-ray1.63A1-120[»]
4LWCX-ray1.61A1-120[»]
4NB3X-ray1.35A/B1-120[»]
4O0AX-ray1.20A1-120[»]
4R4CX-ray1.40A1-120[»]
4R4IX-ray1.40A1-120[»]
4R4OX-ray1.33A1-120[»]
4R4QX-ray1.35A1-120[»]
4R4TX-ray1.28A1-120[»]
5E7NX-ray1.21A1-120[»]
5EAYX-ray1.55A/B/C/D3-120[»]
5N85X-ray2.00A1-120[»]
5N8AX-ray1.28A1-120[»]
BMRBiP27694
SASBDBiP27694
SMRiP27694
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi112037, 558 interactors
CORUMiP27694
DIPiDIP-24189N
IntActiP27694, 92 interactors
MINTiP27694
STRINGi9606.ENSP00000254719

Chemistry databases

BindingDBiP27694
ChEMBLiCHEMBL1764940

PTM databases

iPTMnetiP27694
MetOSiteiP27694
PhosphoSitePlusiP27694
SwissPalmiP27694

Genetic variation databases

BioMutaiRPA1
DMDMi1350579

Proteomic databases

EPDiP27694
jPOSTiP27694
MassIVEiP27694
MaxQBiP27694
PaxDbiP27694
PeptideAtlasiP27694
PRIDEiP27694
ProteomicsDBi54405

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		1868, 478 antibodies

The DNASU plasmid repository

More...DNASUi		6117

Genome annotation databases

EnsembliENST00000254719; ENSP00000254719; ENSG00000132383
GeneIDi6117
KEGGihsa:6117
UCSCiuc002fto.3, human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		6117
DisGeNETi6117

GeneCards: human genes, protein and diseases

More...GeneCardsi		RPA1
HGNCiHGNC:10289, RPA1
HPAiENSG00000132383, Low tissue specificity
MIMi179835, gene
neXtProtiNX_P27694
OpenTargetsiENSG00000132383
PharmGKBiPA34651
VEuPathDBiHostDB:ENSG00000132383.11

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0851, Eukaryota
GeneTreeiENSGT00390000012403
HOGENOMiCLU_012393_2_1_1
InParanoidiP27694
OMAiYRLLINM
OrthoDBi1189265at2759
PhylomeDBiP27694
TreeFamiTF105241

Enzyme and pathway databases

PathwayCommonsiP27694
ReactomeiR-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
SIGNORiP27694

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		6117, 797 hits in 1000 CRISPR screens

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

More...ChiTaRSi		RPA1, human
EvolutionaryTraceiP27694

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Replication_protein_A1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		6117
PharosiP27694, Tchem

Protein Ontology

More...PROi		PR:P27694
RNActiP27694, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000132383, Expressed in secondary oocyte and 248 other tissues
ExpressionAtlasiP27694, baseline and differential
GenevisibleiP27694, HS

Family and domain databases

CDDicd04476, RPA1_DBD_C, 1 hit
cd04477, RPA1N, 1 hit
DisProtiDP00061
IDEALiIID00036
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

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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_HUMAN
<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: P27694
Secondary accession number(s): A8K0Y9, Q59ES9
<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: August 1, 1992
Last sequence update: February 1, 1996
Last modified: June 2, 2021
This is version 222 of the entry and version 2 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
DisclaimerAny 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.

<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

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families
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