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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-Experimental evidence at transcript 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)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi74 – 14875OBAdd
BLAST

GO - Molecular functioni

  • damaged DNA binding Source: UniProtKB
  • protein N-terminus binding Source: RGD
  • single-stranded DNA binding Source: RGD

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-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-68962. Activation of the pre-replicative complex.
R-RNO-69166. Removal of the Flap Intermediate.

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
Gene namesi
Name:Rpa2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi619714. 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 similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 270270Replication protein A 32 kDa subunitPRO_0000097273Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei4 – 41Phosphoserine; by PRKDCBy similarity
Modified residuei8 – 81Phosphoserine; by PRKDCBy similarity
Modified residuei21 – 211Phosphothreonine; by PRKDCBy similarity
Modified residuei23 – 231Phosphoserine; by CDK2By similarity
Modified residuei29 – 291Phosphoserine; by CDK1By similarity
Modified residuei33 – 331Phosphoserine; by PRKDCBy similarity

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

PaxDbiQ63528.
PRIDEiQ63528.

Expressioni

Gene expression databases

GenevisibleiQ63528. RN.

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). 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 FBXO18.By similarity

GO - Molecular functioni

  • protein N-terminus binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000017549.

Structurei

3D structure databases

ProteinModelPortaliQ63528.
SMRiQ63528. Positions 44-170, 202-270.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni187 – 27084Interaction with RAD52, TIPIN, UNG and XPABy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 OB DNA-binding domain.Curated

Phylogenomic databases

eggNOGiKOG3108. Eukaryota.
COG5235. LUCA.
GeneTreeiENSGT00390000010045.
HOGENOMiHOG000216562.
HOVERGENiHBG000086.
InParanoidiQ63528.
KOiK10739.
OMAiSNPGMGE.
OrthoDBiEOG76X615.
PhylomeDBiQ63528.
TreeFamiTF105242.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.40.50.140. 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.

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
Checksum:i95C63555A1D4045E
GO

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.
UniGeneiRn.40389.

Genome annotation databases

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

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.
UniGeneiRn.40389.

3D structure databases

ProteinModelPortaliQ63528.
SMRiQ63528. Positions 44-170, 202-270.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000017549.

Proteomic databases

PaxDbiQ63528.
PRIDEiQ63528.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6118.
RGDi619714. Rpa2.

Phylogenomic databases

eggNOGiKOG3108. Eukaryota.
COG5235. LUCA.
GeneTreeiENSGT00390000010045.
HOGENOMiHOG000216562.
HOVERGENiHBG000086.
InParanoidiQ63528.
KOiK10739.
OMAiSNPGMGE.
OrthoDBiEOG76X615.
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-68962. Activation of the pre-replicative complex.
R-RNO-69166. Removal of the Flap Intermediate.

Miscellaneous databases

NextBioi611723.
PROiQ63528.

Gene expression databases

GenevisibleiQ63528. RN.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.40.50.140. 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...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  2. Nagelhus T., Haug T., Krokan H.E.
    Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-270.

Entry informationi

Entry nameiRFA2_RAT
AccessioniPrimary (citable) accession number: Q63528
Secondary accession number(s): Q6AY60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 26, 2005
Last modified: February 17, 2016
This is version 115 of the entry and version 2 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. 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.