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Protein

Replication protein A 32 kDa subunit

Gene

RPA2

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. 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. 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

GO - Biological processi

Keywordsi

Molecular functionDNA-binding
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
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

EuPathDBiHostDB:ENSG00000117748.9
HGNCiHGNC:10290 RPA2
MIMi179836 gene
neXtProtiNX_P15927

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

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
Mutagenesisi37 – 38KK → RR: Impaired ubiquitination without affecting homologous recombination. 1 Publication2
Mutagenesisi248F → A: Abolishes interaction with RFWD3, leading to impair DNA interstrand cross-links (ICL) repair. 1 Publication1
Mutagenesisi252E → A: Abolishes interaction with RFWD3, leading to impair DNA interstrand cross-links (ICL) repair. 1 Publication1
Mutagenesisi253G → A: Does not affect interaction with RFWD3. 1 Publication1
Mutagenesisi254H → A: Abolishes interaction with RFWD3, leading to impair DNA interstrand cross-links (ICL) repair. 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 PRKDC2 Publications1
Modified residuei8Phosphoserine; by PRKDC2 Publications1
Modified residuei21Phosphothreonine; by PRKDC4 Publications1
Modified residuei23Phosphoserine; by CDK2Combined sources3 Publications1
Modified residuei29Phosphoserine; by CDK1Combined sources4 Publications1
Modified residuei33Phosphoserine; by PRKDC3 Publications1
Cross-linki37Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki38Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

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.9 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 (PubMed:24332808). 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).2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP15927
MaxQBiP15927
PaxDbiP15927
PeptideAtlasiP15927
PRIDEiP15927
ProteomicsDBi53246
53247 [P15927-2]
53248 [P15927-3]

PTM databases

iPTMnetiP15927
PhosphoSitePlusiP15927
SwissPalmiP15927

Expressioni

Inductioni

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

Gene expression databases

BgeeiENSG00000117748 Expressed in 227 organ(s), highest expression level in leukocyte
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 FBH1 (PubMed:23319600). Interacts with ETAA1; the interaction is direct and promotes ETAA1 recruitment at stalled replication forks (PubMed:27601467, PubMed:27723720, PubMed:27723717). Interacts with RFWD3 (PubMed:21504906, PubMed:21558276, PubMed:26474068, PubMed:28575657).22 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi112038, 462 interactors
CORUMiP15927
DIPiDIP-24187N
IntActiP15927, 89 interactors
MINTiP15927
STRINGi9606.ENSP00000363021

Structurei

Secondary structure

1270
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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
InterProiView protein in InterPro
IPR012340 NA-bd_OB-fold
IPR014646 Rfa2/RPA32
IPR014892 RPA_C
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF08784 RPA_C, 1 hit
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

This entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5TEJ0Q5TEJ0_HUMAN
Replication protein A 32 kDa subuni...
RPA2
122Annotation score:
Q5TEJ7Q5TEJ7_HUMAN
Replication protein A 32 kDa subuni...
RPA2
179Annotation score:

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02330014Y → S1 PublicationCorresponds to variant dbSNP:rs28988896Ensembl.1
Natural variantiVAR_02330115G → R1 PublicationCorresponds to variant dbSNP:rs28988897Ensembl.1
Natural variantiVAR_023302203N → S1 PublicationCorresponds to variant dbSNP:rs28904899Ensembl.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 No translation available.
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

Similar proteinsi

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 No translation available.
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, 462 interactors
CORUMiP15927
DIPiDIP-24187N
IntActiP15927, 89 interactors
MINTiP15927
STRINGi9606.ENSP00000363021

PTM databases

iPTMnetiP15927
PhosphoSitePlusiP15927
SwissPalmiP15927

Polymorphism and mutation databases

BioMutaiRPA2
DMDMi132474

Proteomic databases

EPDiP15927
MaxQBiP15927
PaxDbiP15927
PeptideAtlasiP15927
PRIDEiP15927
ProteomicsDBi53246
53247 [P15927-2]
53248 [P15927-3]

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
EuPathDBiHostDB:ENSG00000117748.9
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

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
PROiPR:P15927
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000117748 Expressed in 227 organ(s), highest expression level in leukocyte
CleanExiHS_RPA2
ExpressionAtlasiP15927 baseline and differential
GenevisibleiP15927 HS

Family and domain databases

Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR012340 NA-bd_OB-fold
IPR014646 Rfa2/RPA32
IPR014892 RPA_C
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF08784 RPA_C, 1 hit
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 historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: October 10, 2018
This is version 200 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, Direct protein sequencing, Reference proteome

Documents

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