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Protein

Replication protein A 14 kDa subunit

Gene

RPA3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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 (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. 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. RPA3 has its own single-stranded DNA-binding activity and may be responsible for polarity of the binding of the complex to DNA (PubMed:19010961). 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).1 Publication6 Publications

GO - Molecular functioni

  • damaged DNA binding Source: UniProtKB
  • single-stranded DNA binding Source: UniProtKB

GO - Biological processi

Keywordsi

Biological processDNA damage, DNA recombination, DNA repair, DNA replication

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-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

Names & Taxonomyi

Protein namesi
Recommended name:
Replication protein A 14 kDa subunit
Short name:
RP-A p14
Alternative name(s):
Replication factor A protein 3
Short name:
RF-A protein 3
Gene namesi
Name:RPA3
Synonyms:REPA3, RPA14
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

EuPathDBiHostDB:ENSG00000106399.11
HGNCiHGNC:10291 RPA3
MIMi179837 gene
neXtProtiNX_P35244

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

Pathology & Biotechi

Organism-specific databases

DisGeNETi6119
OpenTargetsiENSG00000106399
PharmGKBiPA34653

Polymorphism and mutation databases

BioMutaiRPA3
DMDMi464608

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000972762 – 121Replication protein A 14 kDa subunitAdd BLAST120

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylvalineCombined sources1
Cross-linki23Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki39Glycyl 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

Post-translational modificationi

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).1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiP35244
MaxQBiP35244
PaxDbiP35244
PeptideAtlasiP35244
PRIDEiP35244
ProteomicsDBi55011
TopDownProteomicsiP35244

PTM databases

iPTMnetiP35244
PhosphoSitePlusiP35244

Expressioni

Gene expression databases

BgeeiENSG00000106399 Expressed in 225 organ(s), highest expression level in bronchial epithelial cell
CleanExiHS_RPA3
ExpressionAtlasiP35244 baseline and differential
GenevisibleiP35244 HS

Organism-specific databases

HPAiHPA005708

Interactioni

Subunit structurei

Component of the canonical replication protein A complex (RPA), a heterotrimer composed of RPA1, RPA2 and RPA3. 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 RPA2.2 Publications

Binary interactionsi

Protein-protein interaction databases

BioGridi112039, 408 interactors
CORUMiP35244
DIPiDIP-24190N
IntActiP35244, 39 interactors
MINTiP35244
STRINGi9606.ENSP00000223129

Structurei

Secondary structure

1121
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP35244
SMRiP35244
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35244

Family & Domainsi

Phylogenomic databases

eggNOGiENOG410IZRM Eukaryota
ENOG4111REI LUCA
GeneTreeiENSGT00390000008029
HOGENOMiHOG000252930
HOVERGENiHBG003004
InParanoidiP35244
KOiK10740
OMAiKPRINCS
OrthoDBiEOG091G1178
PhylomeDBiP35244
TreeFamiTF105243

Family and domain databases

InterProiView protein in InterPro
IPR012340 NA-bd_OB-fold
IPR013970 Rfa2
PfamiView protein in Pfam
PF08661 Rep_fac-A_3, 1 hit
SUPFAMiSSF50249 SSF50249, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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

P35244-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVDMMDLPRS RINAGMLAQF IDKPVCFVGR LEKIHPTGKM FILSDGEGKN
60 70 80 90 100
GTIELMEPLD EEISGIVEVV GRVTAKATIL CTSYVQFKED SHPFDLGLYN
110 120
EAVKIIHDFP QFYPLGIVQH D
Length:121
Mass (Da):13,569
Last modified:February 1, 1994 - v1
Checksum:i3FD99851959FB498
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B5MC59B5MC59_HUMAN
Replication protein A 14 kDa subuni...
RPA3 hCG_17407
82Annotation score:

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07493 mRNA Translation: AAA58350.1
BT007320 mRNA Translation: AAP35984.1
DQ003136 Genomic DNA Translation: AAX84517.1
AC004948 Genomic DNA Translation: AAQ96878.1
BC005264 mRNA Translation: AAH05264.1
BC009868 mRNA Translation: AAH09868.1
CCDSiCCDS5356.1
PIRiA46008
RefSeqiNP_002938.1, NM_002947.4
UniGeneiHs.487540

Genome annotation databases

EnsembliENST00000223129; ENSP00000223129; ENSG00000106399
ENST00000396682; ENSP00000379914; ENSG00000106399
GeneIDi6119
KEGGihsa:6119
UCSCiuc003sri.4 human

Similar proteinsi

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07493 mRNA Translation: AAA58350.1
BT007320 mRNA Translation: AAP35984.1
DQ003136 Genomic DNA Translation: AAX84517.1
AC004948 Genomic DNA Translation: AAQ96878.1
BC005264 mRNA Translation: AAH05264.1
BC009868 mRNA Translation: AAH09868.1
CCDSiCCDS5356.1
PIRiA46008
RefSeqiNP_002938.1, NM_002947.4
UniGeneiHs.487540

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1L1OX-ray2.80A/D1-121[»]
1QUQX-ray2.50B/D1-121[»]
2PI2X-ray2.00E/F/G/H1-121[»]
2PQAX-ray2.50B/D1-121[»]
2Z6KX-ray3.00C/D1-121[»]
3KDFX-ray1.98A/C1-121[»]
ProteinModelPortaliP35244
SMRiP35244
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112039, 408 interactors
CORUMiP35244
DIPiDIP-24190N
IntActiP35244, 39 interactors
MINTiP35244
STRINGi9606.ENSP00000223129

PTM databases

iPTMnetiP35244
PhosphoSitePlusiP35244

Polymorphism and mutation databases

BioMutaiRPA3
DMDMi464608

Proteomic databases

EPDiP35244
MaxQBiP35244
PaxDbiP35244
PeptideAtlasiP35244
PRIDEiP35244
ProteomicsDBi55011
TopDownProteomicsiP35244

Protocols and materials databases

DNASUi6119
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000223129; ENSP00000223129; ENSG00000106399
ENST00000396682; ENSP00000379914; ENSG00000106399
GeneIDi6119
KEGGihsa:6119
UCSCiuc003sri.4 human

Organism-specific databases

CTDi6119
DisGeNETi6119
EuPathDBiHostDB:ENSG00000106399.11
GeneCardsiRPA3
HGNCiHGNC:10291 RPA3
HPAiHPA005708
MIMi179837 gene
neXtProtiNX_P35244
OpenTargetsiENSG00000106399
PharmGKBiPA34653
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IZRM Eukaryota
ENOG4111REI LUCA
GeneTreeiENSGT00390000008029
HOGENOMiHOG000252930
HOVERGENiHBG003004
InParanoidiP35244
KOiK10740
OMAiKPRINCS
OrthoDBiEOG091G1178
PhylomeDBiP35244
TreeFamiTF105243

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-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

ChiTaRSiRPA3 human
EvolutionaryTraceiP35244
GeneWikiiRPA3
GenomeRNAii6119
PROiPR:P35244
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000106399 Expressed in 225 organ(s), highest expression level in bronchial epithelial cell
CleanExiHS_RPA3
ExpressionAtlasiP35244 baseline and differential
GenevisibleiP35244 HS

Family and domain databases

InterProiView protein in InterPro
IPR012340 NA-bd_OB-fold
IPR013970 Rfa2
PfamiView protein in Pfam
PF08661 Rep_fac-A_3, 1 hit
SUPFAMiSSF50249 SSF50249, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiRFA3_HUMAN
AccessioniPrimary (citable) accession number: P35244
Secondary accession number(s): Q549U6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: November 7, 2018
This is version 175 of the entry and version 1 of the sequence. See complete history.
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
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Main funding by: National Institutes of Health

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