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Protein

Replication protein A 32 kDa subunit

Gene

RPA2

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. 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.13 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi74 – 148OBAdd BLAST75

GO - Molecular functioni

  • damaged DNA binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • protein phosphatase binding Source: UniProtKB
  • single-stranded DNA binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  • base-excision repair Source: UniProtKB
  • DNA damage response, detection of DNA damage Source: Reactome
  • DNA replication Source: UniProtKB
  • double-strand break repair via homologous recombination Source: UniProtKB
  • error-free translesion synthesis Source: Reactome
  • error-prone translesion synthesis Source: Reactome
  • G1/S transition of mitotic cell cycle Source: Reactome
  • interstrand cross-link repair Source: Reactome
  • mismatch repair Source: UniProtKB
  • mitotic G1 DNA damage checkpoint Source: UniProtKB
  • nucleotide-excision repair Source: UniProtKB
  • nucleotide-excision repair, DNA gap filling Source: Reactome
  • nucleotide-excision repair, DNA incision Source: Reactome
  • nucleotide-excision repair, DNA incision, 3'-to lesion Source: Reactome
  • nucleotide-excision repair, DNA incision, 5'-to lesion Source: Reactome
  • nucleotide-excision repair, preincision complex assembly Source: Reactome
  • nucleotide-excision repair, preincision complex stabilization Source: Reactome
  • regulation of cellular response to heat Source: Reactome
  • regulation of DNA damage checkpoint Source: UniProtKB
  • regulation of double-strand break repair via homologous recombination Source: UniProtKB
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • telomere maintenance Source: UniProtKB
  • telomere maintenance via recombination Source: Reactome
  • transcription-coupled nucleotide-excision repair Source: Reactome
  • translesion synthesis Source: Reactome
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair, DNA replication

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000117748-MONOMER.
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.
SIGNORiP15927.

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:REPA2, RPA32, RPA34
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:10290. RPA2.

Subcellular locationi

GO - Cellular componenti

  • chromatin Source: CACAO
  • DNA replication factor A complex Source: UniProtKB
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • PML body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi4S → A: Increased RAD51 foci formation and homologous recombination efficiency at DNA double-strand breaks; when associated with A-8. 1 Publication1
Mutagenesisi8S → A: Increased RAD51 foci formation and homologous recombination efficiency at DNA double-strand breaks; when associated with A-4. 2 Publications1
Mutagenesisi8S → D: Lower homologous recombination efficiency following DNA double strand break. Impaired DNA synthesis following DNA damage; when associated with D-33. No effect on cell-cycle progression, nor DNA synthesis in undamaged cells; when associated with D-23; D-29 and D-33. Impaired DNA double strand breaks repair; when associated with D-23; D-29 and D-33. Extended DNA damage-induced G2-M checkpoint; when associated with D-23; D-29 and D-33. Preferentially interacts with RAD51; when associated with D-23; D-29 and D-33. 2 Publications1
Mutagenesisi23S → D: No effect on DNA synthesis following DNA damage; when associated with D-29. No effect on cell-cycle progression, nor DNA synthesis in undamaged cells; when associated with D-8; D-29 and D-33. Impaired DNA double strand breaks repair; when associated with D-8; D-29 and D-33. Extended DNA damage-induced G2-M checkpoint; when associated with D-8; D-29 and D-33. Preferentially interacts with RAD51; when associated with D-8; D-29 and D-33. 1 Publication1
Mutagenesisi29S → A: Reduces phosphorylation by CDK1. 2 Publications1
Mutagenesisi29S → D: No effect on DNA synthesis following DNA damage; when associated with D-23. No effect on cell-cycle progression, nor DNA synthesis in undamaged cells; when associated with D-8; D-23 and D-33. Impaired DNA double strand breaks repair; when associated with D-8; D-23 and D-33. Extended DNA damage-induced G2-M checkpoint; when associated with D-8; D-23 and D-33. Preferentially interacts with RAD51; when associated with D-8; D-23 and D-33. 2 Publications1
Mutagenesisi33S → D: Lower homologous recombination efficiency following DNA double strand break. Impaired DNA synthesis following DNA damage; when associated with D-8. No effect on cell-cycle progression, nor DNA synthesis in undamaged cells; when associated with D-8; D-23 and D-29. Impaired DNA double strand breaks repair; when associated with D-8; D-23 and D-29. Extended DNA damage-induced G2-M checkpoint; when associated with D-8; D-23 and D-29. Preferentially interacts with RAD51; when associated with D-8; D-23 and D-29. 1 Publication1

Organism-specific databases

DisGeNETi6118.
OpenTargetsiENSG00000117748.
PharmGKBiPA34652.

Polymorphism and mutation databases

BioMutaiRPA2.
DMDMi132474.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000972701 – 270Replication protein A 32 kDa subunitAdd BLAST270

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1 Publication1
Modified residuei4Phosphoserine; by PRKDC1 Publication1
Modified residuei8Phosphoserine; by PRKDC1 Publication1
Modified residuei21Phosphothreonine; by PRKDC3 Publications1
Modified residuei23Phosphoserine; by CDK2Combined sources3 Publications1
Modified residuei29Phosphoserine; by CDK1Combined sources4 Publications1
Modified residuei33Phosphoserine; by PRKDC2 Publications1

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.8 Publications
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.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP15927.
MaxQBiP15927.
PaxDbiP15927.
PeptideAtlasiP15927.
PRIDEiP15927.

PTM databases

iPTMnetiP15927.
PhosphoSitePlusiP15927.
SwissPalmiP15927.

Expressioni

Inductioni

Translationally up-regulated in response to DNA damage (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000117748.
CleanExiHS_RPA2.
ExpressionAtlasiP15927. baseline and differential.
GenevisibleiP15927. HS.

Organism-specific databases

HPAiCAB016538.
HPA026306.
HPA026309.

Interactioni

Subunit structurei

Component of the replication protein A complex (RPA/RP-A), a heterotrimeric complex composed of RPA1, RPA2 and RPA3 (PubMed:2406247, PubMed:19116208, PubMed:10449415). Interacts with PRPF19; the PRP19-CDC5L complex is recruited to the sites of DNA repair where it ubiquitinates the replication protein A complex (RPA) (PubMed:24332808). Interacts with SERTAD3 (PubMed:10982866). Interacts with TIPIN (PubMed:17141802, PubMed:17296725). 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 (PubMed:20154705). Interacts (hyperphosphorylated) with RAD51 (PubMed:20154705). Interacts with SMARCAL1; the interaction is direct and mediates the recruitment to the RPA complex of SMARCAL1 (PubMed:19793861, PubMed:19793862, PubMed:19793863). Interacts with RAD52 and XPA; those interactions are direct and associate RAD52 and XPA to the RPA complex (PubMed:7700386, PubMed:8702565, PubMed:17765923, PubMed:11081631). Interacts with FBXO18 (PubMed:23319600).17 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC45O754194EBI-621404,EBI-374969
EIF4EBP3O605163EBI-621404,EBI-746950
GAPDHP044062EBI-621404,EBI-354056
RPA1P276948EBI-621404,EBI-621389
RPA3P352448EBI-621404,EBI-621428
SERTAD3Q9UJW95EBI-621404,EBI-748621
SMARCAL1Q9NZC913EBI-621404,EBI-5457961
TIPINQ9BVW54EBI-621404,EBI-2515360
UNGP130516EBI-621404,EBI-1025947
XPAP230254EBI-621404,EBI-295222

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • protein phosphatase binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112038. 452 interactors.
DIPiDIP-24187N.
IntActiP15927. 74 interactors.
MINTiMINT-5002459.
STRINGi9606.ENSP00000363021.

Structurei

Secondary structure

1270
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi46 – 48Combined sources3
Helixi51 – 55Combined sources5
Beta strandi58 – 62Combined sources5
Beta strandi64 – 66Combined sources3
Beta strandi69 – 71Combined sources3
Beta strandi73 – 85Combined sources13
Beta strandi87 – 95Combined sources9
Beta strandi97 – 100Combined sources4
Beta strandi102 – 107Combined sources6
Beta strandi125 – 135Combined sources11
Beta strandi138 – 148Combined sources11
Helixi153 – 171Combined sources19
Helixi207 – 218Combined sources12
Turni222 – 224Combined sources3
Helixi227 – 233Combined sources7
Helixi239 – 252Combined sources14
Beta strandi254 – 257Combined sources4
Beta strandi263 – 266Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DPUNMR-A172-270[»]
1L1OX-ray2.80B/E44-171[»]
1QUQX-ray2.50A/C43-171[»]
1Z1DNMR-A172-270[»]
2PI2X-ray2.00A/B/C/D1-270[»]
2PQAX-ray2.50A/C42-172[»]
2Z6KX-ray3.00A/B1-270[»]
3KDFX-ray1.98B/D41-172[»]
4MQVX-ray1.95A/C202-270[»]
4OU0X-ray1.40A202-270[»]
ProteinModelPortaliP15927.
SMRiP15927.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15927.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni187 – 270Interaction with RAD52, TIPIN, UNG and XPA1 PublicationAdd BLAST84

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1 – 29Gly/Ser-richAdd BLAST29
Compositional biasi37 – 45Arg/Lys-rich (basic)9
Compositional biasi95 – 123Asp/Glu-rich (acidic)Add BLAST29
Compositional biasi127 – 145Arg/Lys-rich (basic)Add BLAST19
Compositional biasi247 – 270Asp/Glu-rich (acidic)Add BLAST24

Sequence similaritiesi

Contains 1 OB DNA-binding domain.Curated

Phylogenomic databases

eggNOGiKOG3108. Eukaryota.
COG5235. LUCA.
GeneTreeiENSGT00390000010045.
HOGENOMiHOG000216562.
HOVERGENiHBG000086.
InParanoidiP15927.
KOiK10739.
OMAiSNPGMGE.
OrthoDBiEOG091G0L35.
PhylomeDBiP15927.
TreeFamiTF105242.

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.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P15927-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MWNSGFESYG SSSYGGAGGY TQSPGGFGSP APSQAEKKSR ARAQHIVPCT
60 70 80 90 100
ISQLLSATLV DEVFRIGNVE ISQVTIVGII RHAEKAPTNI VYKIDDMTAA
110 120 130 140 150
PMDVRQWVDT DDTSSENTVV PPETYVKVAG HLRSFQNKKS LVAFKIMPLE
160 170 180 190 200
DMNEFTTHIL EVINAHMVLS KANSQPSAGR APISNPGMSE AGNFGGNSFM
210 220 230 240 250
PANGLTVAQN QVLNLIKACP RPEGLNFQDL KNQLKHMSVS SIKQAVDFLS
260 270
NEGHIYSTVD DDHFKSTDAE
Length:270
Mass (Da):29,247
Last modified:April 1, 1990 - v1
Checksum:i61A563EA7B34A9B1
GO
Isoform 2 (identifier: P15927-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MWNS → MGRGDRNKRSIR

Note: No experimental confirmation available.
Show »
Length:278
Mass (Da):30,156
Checksum:i680A88DB44410EBC
GO
Isoform 3 (identifier: P15927-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MWNS → MWNSNDGGAG...QALILLFKTG

Note: No experimental confirmation available.
Show »
Length:358
Mass (Da):38,810
Checksum:iB21291661BDEEAFA
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02330014Y → S.1 PublicationCorresponds to variant rs28988896dbSNPEnsembl.1
Natural variantiVAR_02330115G → R.1 PublicationCorresponds to variant rs28988897dbSNPEnsembl.1
Natural variantiVAR_023302203N → S.1 PublicationCorresponds to variant rs28904899dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0172011 – 4MWNS → MGRGDRNKRSIR in isoform 2. Curated4
Alternative sequenceiVSP_0172021 – 4MWNS → MWNSNDGGAGWRRKRIAGGF SKRASLGSERRVVAGEEGRE RSWGVWGSPAGRRRGRLGRL GQCLKGRSLREPAGFSEAWD VAQALILLFKTG in isoform 3. Curated4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05249 mRNA. Translation: AAA36560.1.
CR450348 mRNA. Translation: CAG29344.1.
DQ001128 Genomic DNA. Translation: AAX84514.1.
AL109927 Genomic DNA. Translation: CAI21777.1.
AL109927 Genomic DNA. Translation: CAI21778.1.
AL109927 Genomic DNA. Translation: CAI21775.1.
BC001630 mRNA. Translation: AAH01630.1.
BC012157 mRNA. Translation: AAH12157.1.
BC021257 mRNA. Translation: AAH21257.1.
CCDSiCCDS314.1. [P15927-1]
CCDS72740.1. [P15927-2]
PIRiA43711.
RefSeqiNP_001273005.1. NM_001286076.1.
NP_001284487.1. NM_001297558.1. [P15927-2]
NP_002937.1. NM_002946.4. [P15927-1]
UniGeneiHs.79411.

Genome annotation databases

EnsembliENST00000313433; ENSP00000363015; ENSG00000117748. [P15927-3]
ENST00000373909; ENSP00000363017; ENSG00000117748. [P15927-2]
ENST00000373912; ENSP00000363021; ENSG00000117748. [P15927-1]
GeneIDi6118.
KEGGihsa:6118.
UCSCiuc001bpe.3. human. [P15927-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05249 mRNA. Translation: AAA36560.1.
CR450348 mRNA. Translation: CAG29344.1.
DQ001128 Genomic DNA. Translation: AAX84514.1.
AL109927 Genomic DNA. Translation: CAI21777.1.
AL109927 Genomic DNA. Translation: CAI21778.1.
AL109927 Genomic DNA. Translation: CAI21775.1.
BC001630 mRNA. Translation: AAH01630.1.
BC012157 mRNA. Translation: AAH12157.1.
BC021257 mRNA. Translation: AAH21257.1.
CCDSiCCDS314.1. [P15927-1]
CCDS72740.1. [P15927-2]
PIRiA43711.
RefSeqiNP_001273005.1. NM_001286076.1.
NP_001284487.1. NM_001297558.1. [P15927-2]
NP_002937.1. NM_002946.4. [P15927-1]
UniGeneiHs.79411.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DPUNMR-A172-270[»]
1L1OX-ray2.80B/E44-171[»]
1QUQX-ray2.50A/C43-171[»]
1Z1DNMR-A172-270[»]
2PI2X-ray2.00A/B/C/D1-270[»]
2PQAX-ray2.50A/C42-172[»]
2Z6KX-ray3.00A/B1-270[»]
3KDFX-ray1.98B/D41-172[»]
4MQVX-ray1.95A/C202-270[»]
4OU0X-ray1.40A202-270[»]
ProteinModelPortaliP15927.
SMRiP15927.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112038. 452 interactors.
DIPiDIP-24187N.
IntActiP15927. 74 interactors.
MINTiMINT-5002459.
STRINGi9606.ENSP00000363021.

PTM databases

iPTMnetiP15927.
PhosphoSitePlusiP15927.
SwissPalmiP15927.

Polymorphism and mutation databases

BioMutaiRPA2.
DMDMi132474.

Proteomic databases

EPDiP15927.
MaxQBiP15927.
PaxDbiP15927.
PeptideAtlasiP15927.
PRIDEiP15927.

Protocols and materials databases

DNASUi6118.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000313433; ENSP00000363015; ENSG00000117748. [P15927-3]
ENST00000373909; ENSP00000363017; ENSG00000117748. [P15927-2]
ENST00000373912; ENSP00000363021; ENSG00000117748. [P15927-1]
GeneIDi6118.
KEGGihsa:6118.
UCSCiuc001bpe.3. human. [P15927-1]

Organism-specific databases

CTDi6118.
DisGeNETi6118.
GeneCardsiRPA2.
HGNCiHGNC:10290. RPA2.
HPAiCAB016538.
HPA026306.
HPA026309.
MIMi179836. gene.
neXtProtiNX_P15927.
OpenTargetsiENSG00000117748.
PharmGKBiPA34652.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3108. Eukaryota.
COG5235. LUCA.
GeneTreeiENSGT00390000010045.
HOGENOMiHOG000216562.
HOVERGENiHBG000086.
InParanoidiP15927.
KOiK10739.
OMAiSNPGMGE.
OrthoDBiEOG091G0L35.
PhylomeDBiP15927.
TreeFamiTF105242.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000117748-MONOMER.
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.
SIGNORiP15927.

Miscellaneous databases

ChiTaRSiRPA2. human.
EvolutionaryTraceiP15927.
GeneWikiiRPA2.
GenomeRNAii6118.
PROiP15927.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000117748.
CleanExiHS_RPA2.
ExpressionAtlasiP15927. baseline and differential.
GenevisibleiP15927. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: P15927
Secondary accession number(s): Q52II0, Q5TEI9, Q5TEJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: November 30, 2016
This is version 184 of the entry and version 1 of the sequence. [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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.