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Protein

Replication protein A 32 kDa subunit

Gene

Rpa2

Organism
Mus musculus (Mouse)
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. 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. Through RFWD3 may activate CHEK1 and play a role in replication checkpoint control. 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
DNA bindingi74 – 148OBAdd BLAST75

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair, DNA replication

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-912446. Meiotic recombination.
R-MMU-912497. Meiotic Recombination.

Names & Taxonomyi

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
Replication protein A 34 kDa subunit
Short name:
RP-A p34
Gene namesi
Name:Rpa2
Synonyms:Rpa34
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1339939. Rpa2.

Subcellular locationi

  • Nucleus By similarity
  • NucleusPML body By similarity

  • Note: Redistributes to discrete nuclear foci upon DNA damage in an ATR-dependent manner.By similarity1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000972711 – 270Replication protein A 32 kDa subunitAdd BLAST270

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

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.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ62193.
MaxQBiQ62193.
PaxDbiQ62193.
PeptideAtlasiQ62193.
PRIDEiQ62193.

PTM databases

iPTMnetiQ62193.
PhosphoSitePlusiQ62193.

Expressioni

Gene expression databases

CleanExiMM_RPA2.

Interactioni

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) (By similarity). Interacts with SERTAD3. Interacts with TIPIN (PubMed:17141802). Interacts with TIMELESS (PubMed:17141802). Interacts with PPP4R2; the interaction is direct, DNA damage-dependent and mediates the recruitment of the PP4 catalytic subunit PPP4C (By similarity). Interacts (hyperphosphorylated) with RAD51 (By similarity). Interacts with SMARCAL1; the interaction is direct and mediates the recruitment to the RPA complex of SMARCAL1 (By similarity). Interacts with RAD52 and XPA; those interactions are direct and associate RAD52 and XPA to the RPA complex (By similarity). Interacts with FBXO18 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-48715N.
STRINGi10090.ENSMUSP00000099621.

Structurei

3D structure databases

ProteinModelPortaliQ62193.
SMRiQ62193.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni187 – 270Interaction with RAD52, TIPIN, UNG and XPABy similarityAdd BLAST84

Sequence similaritiesi

Contains 1 OB DNA-binding domain.Curated

Phylogenomic databases

eggNOGiKOG3108. Eukaryota.
COG5235. LUCA.
HOGENOMiHOG000216562.
HOVERGENiHBG000086.
InParanoidiQ62193.
PhylomeDBiQ62193.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR014646. Rfa2/RPA32.
IPR014892. RPA_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF08784. RPA_C. 1 hit.
[Graphical view]
PIRSFiPIRSF036949. RPA32. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF50249. SSF50249. 1 hit.

Sequencei

Sequence statusi: Complete.

Q62193-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWNSGFESFT SSTYGGRGGY TQSPGGFGSP TPSQAEKKSR VRAQHIVPCT
60 70 80 90 100
ISQLLSATLT DEVFRIGDVE ISQVTIVGII RHAEKAPTNI VYKIDDMTAP
110 120 130 140 150
PMDVRQWVDT DDASGENAVV PPETYVKVAG HLRSFQNKKS LVAFKIIPLE
160 170 180 190 200
DMNEFTAHIL EVVNSHMMLS KPNSQASAGR PSMSNPGMSE SFNFSGNNFM
210 220 230 240 250
PANRLTVVQN QVLNLIKACP RPEGLNFQDL RSQLQHMPVP SIKQAVDFLC
260 270
NEGHIYSTVD DDHFKSTDAE
Length:270
Mass (Da):29,718
Last modified:November 1, 1996 - v1
Checksum:iBF0EF86612A48011
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00812 mRNA. Translation: BAA00693.1.
CCDSiCCDS18734.1.
PIRiS28682.
UniGeneiMm.2870.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00812 mRNA. Translation: BAA00693.1.
CCDSiCCDS18734.1.
PIRiS28682.
UniGeneiMm.2870.

3D structure databases

ProteinModelPortaliQ62193.
SMRiQ62193.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48715N.
STRINGi10090.ENSMUSP00000099621.

PTM databases

iPTMnetiQ62193.
PhosphoSitePlusiQ62193.

Proteomic databases

EPDiQ62193.
MaxQBiQ62193.
PaxDbiQ62193.
PeptideAtlasiQ62193.
PRIDEiQ62193.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:1339939. Rpa2.

Phylogenomic databases

eggNOGiKOG3108. Eukaryota.
COG5235. LUCA.
HOGENOMiHOG000216562.
HOVERGENiHBG000086.
InParanoidiQ62193.
PhylomeDBiQ62193.

Enzyme and pathway databases

ReactomeiR-MMU-912446. Meiotic recombination.
R-MMU-912497. Meiotic Recombination.

Miscellaneous databases

ChiTaRSiRpa2. mouse.
PROiQ62193.
SOURCEiSearch...

Gene expression databases

CleanExiMM_RPA2.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR014646. Rfa2/RPA32.
IPR014892. RPA_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF08784. RPA_C. 1 hit.
[Graphical view]
PIRSFiPIRSF036949. RPA32. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF50249. SSF50249. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRFA2_MOUSE
AccessioniPrimary (citable) accession number: Q62193
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.