RPA2
Replication protein A 32 kDa subunit
Also known as: RFA2_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P15927
- Gene
- RPA2
- Ensembl
- ENSG00000117748
- Chromosome
- 1
- Canonical length
- 270 aa
- Protein class
- Cancer-related genes, Plasma proteins, Predicted intracellular proteins
- Subcellular location
- Nucleoplasm,Nuclear bodies
OverviewNCBI Gene
This gene encodes a subunit of the heterotrimeric Replication Protein A (RPA) complex, which binds to single-stranded DNA (ssDNA), forming a nucleoprotein complex that plays an important role in DNA metabolism, being involved in DNA replication, repair, recombination, telomere maintenance, and co-ordinating the cellular response to DNA damage through activation of the ataxia telangiectasia and Rad3-related protein (ATR) kinase. The RPA complex protects single-stranded DNA from nucleases, prevents formation of secondary structures that would interfere with repair, and co-ordinates the recruitment and departure of different genome maintenance factors. The heterotrimeric complex has two different modes of ssDNA binding, a low-affinity and high-affinity mode, determined by which oligonucleotide/oligosaccharide-binding (OB) domains of the complex are utilized, and differing in the length of DNA bound. This subunit contains a single OB domain that participates in high-affinity DNA binding and also contains a winged helix domain at its carboxy terminus, which interacts with many genome maintenance protein. Post-translational modifications of the RPA complex also plays a role in co-ordinating different damage response pathways. [provided by RefSeq, Sep 2017]
Canonical amino-acid sequenceUniProt
270 residues, UniProt reviewed canonical sequence.
>P15927|RPA2
1 MWNSGFESYG SSSYGGAGGY TQSPGGFGSP APSQAEKKSR ARAQHIVPCT ISQLLSATLV
61 DEVFRIGNVE ISQVTIVGII RHAEKAPTNI VYKIDDMTAA PMDVRQWVDT DDTSSENTVV
121 PPETYVKVAG HLRSFQNKKS LVAFKIMPLE DMNEFTTHIL EVINAHMVLS KANSQPSAGR
181 APISNPGMSE AGNFGGNSFM PANGLTVAQN QVLNLIKACP RPEGLNFQDL KNQLKHMSVS
241 SIKQAVDFLS NEGHIYSTVD DDHFKSTDAELocalizationUniProt · AlphaFold · HPA
Whether an antibody against RPA2 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Intracellular
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.42
- Highest tissue expression
- 76 nTPM
Expression across tissuesHPA
Tissue
- skeletal muscle: 76 nTPM
- lymph node: 70 nTPM
- tonsil: 63 nTPM
- testis: 60 nTPM
- tongue: 59 nTPM
- ovary: 53 nTPM
Single-cell type
- oocytes: 267 nCPM
- early primary spermatocytes: 225 nCPM
- differentiating spermatogonia: 183 nCPM
- neutrophils: 118 nCPM
- cytotrophoblasts: 117 nCPM
- late primary spermatocytes: 106 nCPM
Immune cell
- total PBMC: 436 nTPM
- basophil: 324 nTPM
- MAIT T-cell: 305 nTPM
- NK-cell: 295 nTPM
- eosinophil: 291 nTPM
- naive CD4 T-cell: 288 nTPM
Brain region
- choroid plexus: 36 nTPM
- spinal cord: 34 nTPM
- white matter: 34 nTPM
- hypothalamus: 34 nTPM
- basal ganglia: 30 nTPM
- medulla oblongata: 29 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about RPA2.
Disease | ImmuneIEDB
Conditions an epitope on RPA2 was assayed in.
- hepatitis C B cell
- autoimmune hepatitis B cell
- sclerosing cholangitis B cell
- Alagille syndrome B cell
- Wilson disease B cell
- alpha 1-antitrypsin deficiency B cell
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.52
- gnomAD pLI
- 0.5
- gnomAD missense Z
- 0.77
- DepMap mean gene effect
- -1.82
- DepMap dependency class
- pan
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- base-excision repair
- DNA replication
- double-strand break repair via homologous recombination
- mismatch repair
- mitotic G1 DNA damage checkpoint signaling
- nucleotide-excision repair
- protein localization to chromosome
- regulation of DNA damage checkpoint
- regulation of double-strand break repair via homologous recombination
- telomere maintenance
Molecular functions
- damaged DNA binding
- enzyme binding
- G-rich strand telomeric DNA binding
- protein phosphatase binding
- single-stranded DNA binding
- telomeric DNA binding
- ubiquitin protein ligase binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of RPA2 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads RPA2 as an antibody target. Whether an autoantibody or antibody against RPA2 could matter depends on whether native RPA2 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
RPA2 is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label RPA2 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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