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UniProtKB - Q63528 (RFA2_RAT)

Entry version 142 (02 Dec 2020)
Sequence version 2 (26 Apr 2005)
Previous versions | rss
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Protein

Replication protein A 32 kDa subunit

Gene

Rpa2

Organism
Rattus norvegicus (Rat)
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 transcript 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 bindingi74 – 148OBAdd BLAST75

<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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-110312, Translesion synthesis by REV1
R-RNO-110314, Recognition of DNA damage by PCNA-containing replication complex
R-RNO-110320, Translesion Synthesis by POLH
R-RNO-174437, Removal of the Flap Intermediate from the C-strand
R-RNO-176187, Activation of ATR in response to replication stress
R-RNO-3371453, Regulation of HSF1-mediated heat shock response
R-RNO-5358565, Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)
R-RNO-5358606, Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta)
R-RNO-5651801, PCNA-Dependent Long Patch Base Excision Repair
R-RNO-5655862, Translesion synthesis by POLK
R-RNO-5656121, Translesion synthesis by POLI
R-RNO-5656169, Termination of translesion DNA synthesis
R-RNO-5685938, HDR through Single Strand Annealing (SSA)
R-RNO-5685942, HDR through Homologous Recombination (HRR)
R-RNO-5693607, Processing of DNA double-strand break ends
R-RNO-5693616, Presynaptic phase of homologous DNA pairing and strand exchange
R-RNO-5696395, Formation of Incision Complex in GG-NER
R-RNO-5696397, Gap-filling DNA repair synthesis and ligation in GG-NER
R-RNO-5696400, Dual Incision in GG-NER
R-RNO-6782135, Dual incision in TC-NER
R-RNO-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER
R-RNO-6783310, Fanconi Anemia Pathway
R-RNO-6804756, Regulation of TP53 Activity through Phosphorylation
R-RNO-68962, Activation of the pre-replicative complex
R-RNO-69166, Removal of the Flap Intermediate
R-RNO-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 32 kDa subunit
Short name:
RP-A p32
Alternative name(s):
Replication factor A protein 2
Short name:
RF-A protein 2
<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:Rpa2
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<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
  • UP000002494 <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 5

Organism-specific databases

Rat genome database

More...RGDi		619714, Rpa2

<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_00000972731 – 270Replication protein A 32 kDa subunitAdd BLAST270

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
Modified residuei4Phosphoserine; by PRKDCBy similarity1
Modified residuei8Phosphoserine; by PRKDCBy similarity1
Modified residuei21Phosphothreonine; by PRKDCBy similarity1
Modified residuei23Phosphoserine; by CDK2By similarity1
Modified residuei29Phosphoserine; by CDK1By similarity1
Modified residuei33Phosphoserine; by PRKDCBy 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-linki37Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki38Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)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

Differentially phosphorylated throughout the cell cycle, becoming phosphorylated at the G1-S transition and dephosphorylated in late mitosis. Mainly phosphorylated at Ser-23 and Ser-29, by cyclin A-CDK2 and cyclin B-CDK1, respectively during DNA replication and mitosis. Dephosphorylation may require the serine/threonine-protein phosphatase 4. Phosphorylation at Ser-23 and Ser-29 is a prerequisite for further phosphorylation. Becomes hyperphosphorylated on additional residues including Ser-4, Ser-8, Thr-21 and Ser-33 in response to DNA damage. Hyperphosphorylation is mediated by ATM, ATR and PRKDC. Primarily recruited to DNA repair nuclear foci as a hypophosphorylated form it undergoes subsequent hyperphosphorylation, catalyzed by ATR. Hyperphosphorylation is required for RAD51 recruitment to chromatin and efficient DNA repair. Phosphorylation at Thr-21 depends upon RFWD3 presence.By similarity
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

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q63528

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

More...PaxDbi		Q63528

PRoteomics IDEntifications database

More...PRIDEi		Q63528

<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		ENSRNOG00000013005, Expressed in thymus and 22 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q63528, RN

<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 replication protein A complex (RPA/RP-A), a heterotrimeric complex composed of RPA1, RPA2 and RPA3.

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 SERTAD3.

Interacts with TIPIN.

Interacts with TIMELESS.

Interacts with PPP4R2; the interaction is direct, DNA damage-dependent and mediates the recruitment of the PP4 catalytic subunit PPP4C.

Interacts (hyperphosphorylated) with RAD51.

Interacts with SMARCAL1; the interaction is direct and mediates the recruitment to the RPA complex of SMARCAL1.

Interacts with RAD52 and XPA; those interactions are direct and associate RAD52 and XPA to the RPA complex.

Interacts with FBH1.

Interacts with ETAA1; the interaction is direct and promotes ETAA1 recruitment at stalled replication forks.

Interacts with DDI2 (By similarity).

By similarity

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		248725, 1 interactor

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000017549

<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		Q63528

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

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>Regioni187 – 270Interaction with RAD52, TIPIN, UNG and XPABy similarityAdd BLAST84

<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 2 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3108, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00390000010045

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_051033_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q63528

Identification of Orthologs from Complete Genome Data

More...OMAi		MQYAMAC

Database of Orthologous Groups

More...OrthoDBi		924826at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q63528

TreeFam database of animal gene trees

More...TreeFami		TF105242

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR012340, NA-bd_OB-fold
IPR040260, RFA2-like
IPR014646, Rfa2/RPA32
IPR014892, RPA_C
IPR036388, WH-like_DNA-bd_sf
IPR036390, WH_DNA-bd_sf

The PANTHER Classification System

More...PANTHERi		PTHR13989, PTHR13989, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF08784, RPA_C, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF036949, RPA32, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF46785, SSF46785, 1 hit
SSF50249, SSF50249, 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>Sequencei

<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.

Q63528-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MWNSGFESFS SSSYGAAGGY TQSPGGFGSP TPSQAEKKSR ARAQHIVPCT 
        60         70         80         90        100
ISQLLSATLT DEVFKIGDVE ISQVTIVGII RHAEKAPTNI VYKIDDMTAA 
       110        120        130        140        150
PMDVRQWVDT DDTSGENTVV PPETYVKVAG HLRSFQNKKS LVAFKIIPLE 
       160        170        180        190        200
DMNEFTAHIL EVVNSHLMLS KANSQASVGR PSMSNPGMGE PGNFSGNNFM 
       210        220        230        240        250
PANGLTVVQN QVLNLIKACP RPEGLNFQDL RSQLQHMPVA SIKQAVDFLC 
       260        270
NEGHIYSTVD DDHFKSTDAE
Length:270
Mass (Da):29,346
Last modified:April 26, 2005 - 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:i95C63555A1D4045E
GO

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
BC079180 mRNA Translation: AAH79180.1
X98490 mRNA Translation: CAA67116.1

NCBI Reference Sequences

More...RefSeqi		NP_067593.1, NM_021582.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000017549; ENSRNOP00000017549; ENSRNOG00000013005

Database of genes from NCBI RefSeq genomes

More...GeneIDi		59102

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:59102

UCSC genome browser

More...UCSCi		RGD:619714, rat

<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
BC079180 mRNA Translation: AAH79180.1
X98490 mRNA Translation: CAA67116.1
RefSeqiNP_067593.1, NM_021582.1

3D structure databases

SMRiQ63528
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi248725, 1 interactor
STRINGi10116.ENSRNOP00000017549

Proteomic databases

jPOSTiQ63528
PaxDbiQ63528
PRIDEiQ63528

Genome annotation databases

EnsembliENSRNOT00000017549; ENSRNOP00000017549; ENSRNOG00000013005
GeneIDi59102
KEGGirno:59102
UCSCiRGD:619714, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		6118
RGDi619714, Rpa2

Phylogenomic databases

eggNOGiKOG3108, Eukaryota
GeneTreeiENSGT00390000010045
HOGENOMiCLU_051033_1_0_1
InParanoidiQ63528
OMAiMQYAMAC
OrthoDBi924826at2759
PhylomeDBiQ63528
TreeFamiTF105242

Enzyme and pathway databases

ReactomeiR-RNO-110312, Translesion synthesis by REV1
R-RNO-110314, Recognition of DNA damage by PCNA-containing replication complex
R-RNO-110320, Translesion Synthesis by POLH
R-RNO-174437, Removal of the Flap Intermediate from the C-strand
R-RNO-176187, Activation of ATR in response to replication stress
R-RNO-3371453, Regulation of HSF1-mediated heat shock response
R-RNO-5358565, Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)
R-RNO-5358606, Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta)
R-RNO-5651801, PCNA-Dependent Long Patch Base Excision Repair
R-RNO-5655862, Translesion synthesis by POLK
R-RNO-5656121, Translesion synthesis by POLI
R-RNO-5656169, Termination of translesion DNA synthesis
R-RNO-5685938, HDR through Single Strand Annealing (SSA)
R-RNO-5685942, HDR through Homologous Recombination (HRR)
R-RNO-5693607, Processing of DNA double-strand break ends
R-RNO-5693616, Presynaptic phase of homologous DNA pairing and strand exchange
R-RNO-5696395, Formation of Incision Complex in GG-NER
R-RNO-5696397, Gap-filling DNA repair synthesis and ligation in GG-NER
R-RNO-5696400, Dual Incision in GG-NER
R-RNO-6782135, Dual incision in TC-NER
R-RNO-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER
R-RNO-6783310, Fanconi Anemia Pathway
R-RNO-6804756, Regulation of TP53 Activity through Phosphorylation
R-RNO-68962, Activation of the pre-replicative complex
R-RNO-69166, Removal of the Flap Intermediate
R-RNO-69473, G2/M DNA damage checkpoint

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q63528

Gene expression databases

BgeeiENSRNOG00000013005, Expressed in thymus and 22 other tissues
GenevisibleiQ63528, RN

Family and domain databases

Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR012340, NA-bd_OB-fold
IPR040260, RFA2-like
IPR014646, Rfa2/RPA32
IPR014892, RPA_C
IPR036388, WH-like_DNA-bd_sf
IPR036390, WH_DNA-bd_sf
PANTHERiPTHR13989, PTHR13989, 1 hit
PfamiView protein in Pfam
PF08784, RPA_C, 1 hit
PIRSFiPIRSF036949, RPA32, 1 hit
SUPFAMiSSF46785, SSF46785, 1 hit
SSF50249, SSF50249, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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 nameiRFA2_RAT
<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: Q63528
Secondary accession number(s): Q6AY60
<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: November 1, 1997
Last sequence update: April 26, 2005
Last modified: December 2, 2020
This is version 142 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

<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. SIMILARITY comments
    Index of protein domains and families
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