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Protein

Replication protein A 14 kDa subunit

Gene

RPA3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.

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.
TopDownProteomicsiP35244.

PTM databases

iPTMnetiP35244.
PhosphoSitePlusiP35244.

Expressioni

Gene expression databases

BgeeiENSG00000106399.
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

Show more details

Protein-protein interaction databases

BioGridi112039. 390 interactors.
CORUMiP35244.
DIPiDIP-24190N.
IntActiP35244. 28 interactors.
MINTiMINT-5002568.
STRINGi9606.ENSP00000223129.

Structurei

Secondary structure

1121
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 6Combined sources3
Beta strandi10 – 12Combined sources3
Helixi14 – 20Combined sources7
Beta strandi24 – 34Combined sources11
Beta strandi38 – 44Combined sources7
Beta strandi50 – 54Combined sources5
Beta strandi65 – 73Combined sources9
Beta strandi79 – 86Combined sources8
Beta strandi90 – 92Combined sources3
Helixi96 – 108Combined sources13
Helixi110 – 112Combined sources3

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...

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.

Sequencei

Sequence statusi: Complete.

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

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

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

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: October 25, 2017
This is version 166 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. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references