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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 ‘Function’ 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 ‘Function’ 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

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

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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

<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_and_taxonomy_section">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:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_manual">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

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000132383.11

Human Gene Nomenclature Database

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HGNCi
HGNC:10289 RPA1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
179835 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P27694

<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; Source: COMPARTMENTS

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_and_biotech_section">'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

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DisGeNETi
6117

Open Targets

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OpenTargetsi
ENSG00000132383

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA34651

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1764940

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
RPA1

Domain mapping of disease mutations (DMDM)

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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.<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_processing_section">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_processing_section">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_processing_section">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

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EPDi
P27694

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P27694

MaxQB - The MaxQuant DataBase

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MaxQBi
P27694

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

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PaxDbi
P27694

PeptideAtlas

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PeptideAtlasi
P27694

PRoteomics IDEntifications database

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PRIDEi
P27694

ProteomicsDB human proteome resource

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ProteomicsDBi
54405

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P27694

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

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PhosphoSitePlusi
P27694

SwissPalm database of S-palmitoylation events

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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

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Bgeei
ENSG00000132383 Expressed in 235 organ(s), highest expression level in secondary oocyte

CleanEx database of gene expression profiles

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CleanExi
HS_RPA1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P27694 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P27694 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB004563
HPA006914
HPA046497

<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_section">'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_section">'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), an 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 (PubMed:24126761). 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).15 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
112037, 491 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P27694

Database of interacting proteins

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DIPi
DIP-24189N

Protein interaction database and analysis system

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IntActi
P27694, 77 interactors

Molecular INTeraction database

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MINTi
P27694

STRING: functional protein association networks

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STRINGi
9606.ENSP00000254719

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P27694

<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

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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[»]

Database of protein disorder

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DisProti
DP00061

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P27694

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

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SMRi
P27694

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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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

<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

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

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eggNOGi
KOG0851 Eukaryota
COG1599 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000012403

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000162322

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG010502

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P27694

KEGG Orthology (KO)

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KOi
K07466

Identification of Orthologs from Complete Genome Data

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OMAi
NIYLMDT

Database of Orthologous Groups

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OrthoDBi
1189265at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P27694

TreeFam database of animal gene trees

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TreeFami
TF105241

Family and domain databases

Conserved Domains Database

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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

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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

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SUPFAMi
SSF50249 SSF50249, 4 hits

TIGRFAMs; a protein family database

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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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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. Translation N-terminally shortened.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

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.461925
Hs.595562

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

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">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
UniGeneiHs.461925
Hs.595562

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
DisProtiDP00061
ProteinModelPortaliP27694
SMRiP27694
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112037, 491 interactors
CORUMiP27694
DIPiDIP-24189N
IntActiP27694, 77 interactors
MINTiP27694
STRINGi9606.ENSP00000254719

Chemistry databases

BindingDBiP27694
ChEMBLiCHEMBL1764940

PTM databases

iPTMnetiP27694
PhosphoSitePlusiP27694
SwissPalmiP27694

Polymorphism and mutation databases

BioMutaiRPA1
DMDMi1350579

Proteomic databases

EPDiP27694
jPOSTiP27694
MaxQBiP27694
PaxDbiP27694
PeptideAtlasiP27694
PRIDEiP27694
ProteomicsDBi54405

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
6117
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
6117
DisGeNETi6117
EuPathDBiHostDB:ENSG00000132383.11

GeneCards: human genes, protein and diseases

More...
GeneCardsi
RPA1
HGNCiHGNC:10289 RPA1
HPAiCAB004563
HPA006914
HPA046497
MIMi179835 gene
neXtProtiNX_P27694
OpenTargetsiENSG00000132383
PharmGKBiPA34651

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0851 Eukaryota
COG1599 LUCA
GeneTreeiENSGT00390000012403
HOGENOMiHOG000162322
HOVERGENiHBG010502
InParanoidiP27694
KOiK07466
OMAiNIYLMDT
OrthoDBi1189265at2759
PhylomeDBiP27694
TreeFamiTF105241

Enzyme and pathway databases

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

Miscellaneous databases

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

Protein Ontology

More...
PROi
PR:P27694

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000132383 Expressed in 235 organ(s), highest expression level in secondary oocyte
CleanExiHS_RPA1
ExpressionAtlasiP27694 baseline and differential
GenevisibleiP27694 HS

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

More...
ProtoNeti
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_and_isoforms">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: January 16, 2019
This is version 204 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  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. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
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