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P15927

- RFA2_HUMAN

UniProt

P15927 - RFA2_HUMAN

Protein

Replication protein A 32 kDa subunit

Gene

RPA2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    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. 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.12 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi74 – 14875OBAdd
    BLAST

    GO - Molecular functioni

    1. damaged DNA binding Source: UniProtKB
    2. enzyme binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein phosphatase binding Source: UniProtKB
    5. single-stranded DNA binding Source: UniProtKB
    6. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. base-excision repair Source: UniProtKB
    2. DNA recombinase assembly Source: Reactome
    3. DNA repair Source: Reactome
    4. DNA replication Source: UniProtKB
    5. DNA strand elongation involved in DNA replication Source: Reactome
    6. double-strand break repair Source: Reactome
    7. double-strand break repair via homologous recombination Source: UniProtKB
    8. G1/S transition of mitotic cell cycle Source: Reactome
    9. mismatch repair Source: UniProtKB
    10. mitotic cell cycle Source: Reactome
    11. mitotic G1 DNA damage checkpoint Source: UniProtKB
    12. nucleotide-excision repair Source: UniProtKB
    13. nucleotide-excision repair, DNA damage removal Source: Reactome
    14. nucleotide-excision repair, DNA gap filling Source: Reactome
    15. regulation of DNA damage checkpoint Source: UniProtKB
    16. regulation of double-strand break repair via homologous recombination Source: UniProtKB
    17. telomere maintenance Source: UniProtKB
    18. telomere maintenance via recombination Source: Reactome
    19. telomere maintenance via semi-conservative replication Source: Reactome
    20. transcription-coupled nucleotide-excision repair Source: Reactome

    Keywords - Biological processi

    DNA damage, DNA recombination, DNA repair, DNA replication

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1095. Activation of the pre-replicative complex.
    REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
    REACT_200744. HSF1 activation.
    REACT_200780. Regulation of HSF1-mediated heat shock response.
    REACT_2055. Processing of DNA double-strand break ends.
    REACT_2141. Assembly of the RAD51-ssDNA nucleoprotein complex.
    REACT_257. Formation of incision complex in GG-NER.
    REACT_27271. Meiotic recombination.
    REACT_311. Dual incision reaction in GG-NER.
    REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
    REACT_408. Presynaptic phase of homologous DNA pairing and strand exchange.
    REACT_6769. Activation of ATR in response to replication stress.
    REACT_70. Removal of the Flap Intermediate.
    REACT_7999. Removal of the Flap Intermediate from the C-strand.

    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
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10290. RPA2.

    Subcellular locationi

    Nucleus. NucleusPML body
    Note: Redistributes to discrete nuclear foci upon DNA damage in an ATR-dependent manner.

    GO - Cellular componenti

    1. DNA replication factor A complex Source: UniProtKB
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB
    4. PML body Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi4 – 41S → A: Increased RAD51 foci formation and homologous recombination efficiency at DNA double-strand breaks; when associated with A-8. 1 Publication
    Mutagenesisi8 – 81S → A: Increased RAD51 foci formation and homologous recombination efficiency at DNA double-strand breaks; when associated with A-4. 2 Publications
    Mutagenesisi8 – 81S → 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 Publications
    Mutagenesisi23 – 231S → 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 Publication
    Mutagenesisi29 – 291S → A: Reduces phosphorylation by CDK1. 2 Publications
    Mutagenesisi29 – 291S → 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 Publications
    Mutagenesisi33 – 331S → 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 Publication

    Organism-specific databases

    PharmGKBiPA34652.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 270270Replication protein A 32 kDa subunitPRO_0000097270Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications
    Modified residuei4 – 41Phosphoserine; by PRKDC1 Publication
    Modified residuei8 – 81Phosphoserine; by PRKDC1 Publication
    Modified residuei21 – 211Phosphothreonine; by PRKDC3 Publications
    Modified residuei23 – 231Phosphoserine; by CDK24 Publications
    Modified residuei29 – 291Phosphoserine; by CDK15 Publications
    Modified residuei33 – 331Phosphoserine; by PRKDC2 Publications

    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

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP15927.
    PaxDbiP15927.
    PRIDEiP15927.

    PTM databases

    PhosphoSiteiP15927.

    Expressioni

    Inductioni

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

    Gene expression databases

    ArrayExpressiP15927.
    BgeeiP15927.
    CleanExiHS_RPA2.
    GenevestigatoriP15927.

    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. 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.15 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC45O754194EBI-621404,EBI-374969
    EIF4EBP3O605163EBI-621404,EBI-746950
    GAPDHP044062EBI-621404,EBI-354056
    RPA1P276944EBI-621404,EBI-621389
    RPA3P352446EBI-621404,EBI-621428
    SERTAD3Q9UJW95EBI-621404,EBI-748621
    SMARCAL1Q9NZC912EBI-621404,EBI-5457961
    TIPINQ9BVW53EBI-621404,EBI-2515360
    UNGP130516EBI-621404,EBI-1025947
    XPAP230254EBI-621404,EBI-295222

    Protein-protein interaction databases

    BioGridi112038. 428 interactions.
    DIPiDIP-24187N.
    IntActiP15927. 53 interactions.
    MINTiMINT-5002459.
    STRINGi9606.ENSP00000363021.

    Structurei

    Secondary structure

    1
    270
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi46 – 483
    Helixi51 – 555
    Beta strandi58 – 625
    Beta strandi64 – 663
    Beta strandi69 – 713
    Beta strandi73 – 8513
    Beta strandi87 – 959
    Beta strandi97 – 1004
    Beta strandi102 – 1076
    Beta strandi125 – 13511
    Beta strandi138 – 14811
    Helixi153 – 17119
    Helixi207 – 21812
    Turni222 – 2243
    Helixi227 – 2337
    Helixi239 – 25214
    Beta strandi254 – 2574
    Beta strandi263 – 2664

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    4OU0X-ray1.40A202-270[»]
    ProteinModelPortaliP15927.
    SMRiP15927. Positions 44-170, 202-270.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15927.

    Family & Domainsi

    Region

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

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1 – 2929Gly/Ser-richAdd
    BLAST
    Compositional biasi37 – 459Arg/Lys-rich (basic)
    Compositional biasi95 – 12329Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi127 – 14519Arg/Lys-rich (basic)Add
    BLAST
    Compositional biasi247 – 27024Asp/Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Contains 1 OB DNA-binding domain.Curated

    Phylogenomic databases

    eggNOGiCOG5235.
    HOGENOMiHOG000216562.
    HOVERGENiHBG000086.
    KOiK10739.
    OMAiIAREAIF.
    OrthoDBiEOG76X615.
    PhylomeDBiP15927.
    TreeFamiTF105242.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    2.40.50.140. 1 hit.
    InterProiIPR012340. NA-bd_OB-fold.
    IPR004365. NA-bd_OB_tRNA.
    IPR014646. RPA32.
    IPR014892. RPA_C.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF08784. RPA_C. 1 hit.
    PF01336. tRNA_anti-codon. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036949. RPA32. 1 hit.
    SUPFAMiSSF50249. SSF50249. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    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

    MWNSGFESYG SSSYGGAGGY TQSPGGFGSP APSQAEKKSR ARAQHIVPCT    50
    ISQLLSATLV DEVFRIGNVE ISQVTIVGII RHAEKAPTNI VYKIDDMTAA 100
    PMDVRQWVDT DDTSSENTVV PPETYVKVAG HLRSFQNKKS LVAFKIMPLE 150
    DMNEFTTHIL EVINAHMVLS KANSQPSAGR APISNPGMSE AGNFGGNSFM 200
    PANGLTVAQN QVLNLIKACP RPEGLNFQDL KNQLKHMSVS SIKQAVDFLS 250
    NEGHIYSTVD DDHFKSTDAE 270
    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)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti14 – 141Y → S.1 Publication
    Corresponds to variant rs28988896 [ dbSNP | Ensembl ].
    VAR_023300
    Natural varianti15 – 151G → R.1 Publication
    Corresponds to variant rs28988897 [ dbSNP | Ensembl ].
    VAR_023301
    Natural varianti203 – 2031N → S.1 Publication
    Corresponds to variant rs28904899 [ dbSNP | Ensembl ].
    VAR_023302

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 44MWNS → MGRGDRNKRSIR in isoform 2. CuratedVSP_017201
    Alternative sequencei1 – 44MWNS → MWNSNDGGAGWRRKRIAGGF SKRASLGSERRVVAGEEGRE RSWGVWGSPAGRRRGRLGRL GQCLKGRSLREPAGFSEAWD VAQALILLFKTG in isoform 3. CuratedVSP_017202

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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]
    PIRiA43711.
    RefSeqiNP_001273005.1. NM_001286076.1.
    NP_002937.1. NM_002946.4. [P15927-1]
    XP_005246022.1. XM_005245965.1. [P15927-2]
    UniGeneiHs.79411.

    Genome annotation databases

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

    Polymorphism databases

    DMDMi132474.

    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS314.1. [P15927-1 ]
    PIRi A43711.
    RefSeqi NP_001273005.1. NM_001286076.1.
    NP_002937.1. NM_002946.4. [P15927-1 ]
    XP_005246022.1. XM_005245965.1. [P15927-2 ]
    UniGenei Hs.79411.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DPU NMR - A 172-270 [» ]
    1L1O X-ray 2.80 B/E 44-171 [» ]
    1QUQ X-ray 2.50 A/C 43-171 [» ]
    1Z1D NMR - A 172-270 [» ]
    2PI2 X-ray 2.00 A/B/C/D 1-270 [» ]
    2PQA X-ray 2.50 A/C 42-172 [» ]
    2Z6K X-ray 3.00 A/B 1-270 [» ]
    3KDF X-ray 1.98 B/D 41-172 [» ]
    4OU0 X-ray 1.40 A 202-270 [» ]
    ProteinModelPortali P15927.
    SMRi P15927. Positions 44-170, 202-270.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112038. 428 interactions.
    DIPi DIP-24187N.
    IntActi P15927. 53 interactions.
    MINTi MINT-5002459.
    STRINGi 9606.ENSP00000363021.

    PTM databases

    PhosphoSitei P15927.

    Polymorphism databases

    DMDMi 132474.

    Proteomic databases

    MaxQBi P15927.
    PaxDbi P15927.
    PRIDEi P15927.

    Protocols and materials databases

    DNASUi 6118.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000313433 ; ENSP00000363015 ; ENSG00000117748 . [P15927-3 ]
    ENST00000373909 ; ENSP00000363017 ; ENSG00000117748 . [P15927-2 ]
    ENST00000373912 ; ENSP00000363021 ; ENSG00000117748 . [P15927-1 ]
    GeneIDi 6118.
    KEGGi hsa:6118.
    UCSCi uc001bpe.1. human. [P15927-1 ]

    Organism-specific databases

    CTDi 6118.
    GeneCardsi GC01M028218.
    HGNCi HGNC:10290. RPA2.
    HPAi CAB016538.
    HPA026306.
    HPA026309.
    MIMi 179836. gene.
    neXtProti NX_P15927.
    PharmGKBi PA34652.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5235.
    HOGENOMi HOG000216562.
    HOVERGENi HBG000086.
    KOi K10739.
    OMAi IAREAIF.
    OrthoDBi EOG76X615.
    PhylomeDBi P15927.
    TreeFami TF105242.

    Enzyme and pathway databases

    Reactomei REACT_1095. Activation of the pre-replicative complex.
    REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
    REACT_200744. HSF1 activation.
    REACT_200780. Regulation of HSF1-mediated heat shock response.
    REACT_2055. Processing of DNA double-strand break ends.
    REACT_2141. Assembly of the RAD51-ssDNA nucleoprotein complex.
    REACT_257. Formation of incision complex in GG-NER.
    REACT_27271. Meiotic recombination.
    REACT_311. Dual incision reaction in GG-NER.
    REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
    REACT_408. Presynaptic phase of homologous DNA pairing and strand exchange.
    REACT_6769. Activation of ATR in response to replication stress.
    REACT_70. Removal of the Flap Intermediate.
    REACT_7999. Removal of the Flap Intermediate from the C-strand.

    Miscellaneous databases

    ChiTaRSi RPA2. human.
    EvolutionaryTracei P15927.
    GeneWikii RPA2.
    GenomeRNAii 6118.
    NextBioi 23759.
    PROi P15927.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15927.
    Bgeei P15927.
    CleanExi HS_RPA2.
    Genevestigatori P15927.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    2.40.50.140. 1 hit.
    InterProi IPR012340. NA-bd_OB-fold.
    IPR004365. NA-bd_OB_tRNA.
    IPR014646. RPA32.
    IPR014892. RPA_C.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF08784. RPA_C. 1 hit.
    PF01336. tRNA_anti-codon. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036949. RPA32. 1 hit.
    SUPFAMi SSF50249. SSF50249. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The primary structure of the 32-kDa subunit of human replication protein A."
      Erdile L.F., Wold M.S., Kelly T.J.
      J. Biol. Chem. 265:3177-3182(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, FUNCTION IN DNA REPLICATION, IDENTIFICATION IN RPA COMPLEX.
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. NIEHS SNPs program
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-14; ARG-15 AND SER-203.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Kidney, Lung and Muscle.
    6. "Cell-cycle-regulated phosphorylation of DNA replication factor A from human and yeast cells."
      Din S., Brill S.J., Fairman M.P., Stillman B.
      Genes Dev. 4:968-977(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: CELL CYCLE-DEPENDENT PHOSPHORYLATION.
    7. "cdc2 family kinases phosphorylate a human cell DNA replication factor, RPA, and activate DNA replication."
      Dutta A., Stillman B.
      EMBO J. 11:2189-2199(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA DAMAGE-INDUCED PHOSPHORYLATION, PHOSPHORYLATION AT SER-23 AND SER-29.
    8. "The ionizing radiation-induced replication protein A phosphorylation response differs between ataxia telangiectasia and normal human cells."
      Liu V.F., Weaver D.T.
      Mol. Cell. Biol. 13:7222-7231(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-23 AND SER-29.
    9. "Mammalian DNA nucleotide excision repair reconstituted with purified protein components."
      Aboussekhra A., Biggerstaff M., Shivji M.K., Vilpo J.A., Moncollin V., Podust V.N., Protic M., Huebscher U., Egly J.M., Wood R.D.
      Cell 80:859-868(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NUCLEOTIDE EXCISION REPAIR.
    10. "RPA involvement in the damage-recognition and incision steps of nucleotide excision repair."
      He Z., Henricksen L.A., Wold M.S., Ingles C.J.
      Nature 374:566-569(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NUCLEOTIDE EXCISION REPAIR, INTERACTION WITH XPA.
    11. "Physical interaction between human RAD52 and RPA is required for homologous recombination in mammalian cells."
      Park M.S., Ludwig D.L., Stigger E., Lee S.H.
      J. Biol. Chem. 271:18996-19000(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HOMOLOGOUS RECOMBINATION, INTERACTION WITH RAD52.
    12. "Mapping of amino acid residues in the p34 subunit of human single-stranded DNA-binding protein phosphorylated by DNA-dependent protein kinase and Cdc2 kinase in vitro."
      Niu H., Erdjument-Bromage H., Pan Z.-Q., Lee S.-H., Tempst P., Hurwitz J.
      J. Biol. Chem. 272:12634-12641(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT MET-1, PHOSPHORYLATION AT THR-21; SER-29 AND SER-33, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-29.
    13. "Sites of UV-induced phosphorylation of the p34 subunit of replication protein A from HeLa cells."
      Zernik-Kobak M., Vasunia K., Connelly M., Anderson C.W., Dixon K.
      J. Biol. Chem. 272:23896-23904(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-21; SER-23; SER-29 AND SER-33.
    14. "The evolutionarily conserved zinc finger motif in the largest subunit of human replication protein A is required for DNA replication and mismatch repair but not for nucleotide excision repair."
      Lin Y.L., Shivji M.K., Chen C., Kolodner R., Wood R.D., Dutta A.
      J. Biol. Chem. 273:1453-1461(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DNA REPLICATION, FUNCTION IN DNA MISMATCH REPAIR, FUNCTION IN NUCLEOTIDE EXCISION REPAIR.
    15. "Replication protein A stimulates long patch DNA base excision repair."
      DeMott M.S., Zigman S., Bambara R.A.
      J. Biol. Chem. 273:27492-27498(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN BASE EXCISION REPAIR.
    16. "RBT1, a novel transcriptional co-activator, binds the second subunit of replication protein A."
      Cho J.M., Song D.J., Bergeron J., Benlimame N., Wold M.S., Alaoui-Jamali M.A.
      Nucleic Acids Res. 28:3478-3485(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SERTAD3, SUBCELLULAR LOCATION.
    17. "ATR kinase activity regulates the intranuclear translocation of ATR and RPA following ionizing radiation."
      Barr S.M., Leung C.G., Chang E.E., Cimprich K.A.
      Curr. Biol. 13:1047-1051(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY ATR, SUBCELLULAR LOCATION.
    18. "Coordinated regulation of replication protein A activities by its subunits p14 and p32."
      Weisshart K., Pestryakov P., Smith R.W.P., Hartmann H., Kremmer E., Lavrik O., Nasheuer H.-P.
      J. Biol. Chem. 279:35368-35376(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DNA REPLICATION.
    19. "Mammalian TIMELESS and Tipin are evolutionarily conserved replication fork-associated factors."
      Gotter A.L., Suppa C., Emanuel B.S.
      J. Mol. Biol. 366:36-52(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TIMELESS AND TIPIN.
    20. "RPA mediates recombination repair during replication stress and is displaced from DNA by checkpoint signalling in human cells."
      Sleeth K.M., Sorensen C.S., Issaeva N., Dziegielewski J., Bartek J., Helleday T.
      J. Mol. Biol. 373:38-47(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HOMOLOGOUS RECOMBINATION REPAIR, INTERACTION WITH RAD52.
    21. "The human Tim/Tipin complex coordinates an Intra-S checkpoint response to UV that slows replication fork displacement."
      Uensal-Kacmaz K., Chastain P.D., Qu P.-P., Minoo P., Cordeiro-Stone M., Sancar A., Kaufmann W.K.
      Mol. Cell. Biol. 27:3131-3142(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TIPIN.
    22. "Replication protein A prevents accumulation of single-stranded telomeric DNA in cells that use alternative lengthening of telomeres."
      Grudic A., Jul-Larsen A., Haring S.J., Wold M.S., Loenning P.E., Bjerkvig R., Boee S.O.
      Nucleic Acids Res. 35:7267-7278(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TELOMERE MAINTENANCE, SUBCELLULAR LOCATION.
    23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "The annealing helicase HARP is recruited to DNA repair sites via an interaction with RPA."
      Yusufzai T., Kong X., Yokomori K., Kadonaga J.T.
      Genes Dev. 23:2400-2404(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMARCAL1.
    26. "The annealing helicase SMARCAL1 maintains genome integrity at stalled replication forks."
      Bansbach C.E., Betous R., Lovejoy C.A., Glick G.G., Cortez D.
      Genes Dev. 23:2405-2414(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMARCAL1.
    27. "The SIOD disorder protein SMARCAL1 is an RPA-interacting protein involved in replication fork restart."
      Ciccia A., Bredemeyer A.L., Sowa M.E., Terret M.E., Jallepalli P.V., Harper J.W., Elledge S.J.
      Genes Dev. 23:2415-2425(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMARCAL1.
    28. "An alternative form of replication protein a prevents viral replication in vitro."
      Mason A.C., Haring S.J., Pryor J.M., Staloch C.A., Gan T.F., Wold M.S.
      J. Biol. Chem. 284:5324-5331(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS PART OF THE RPA COMPLEX.
    29. "An alternative form of replication protein a expressed in normal human tissues supports DNA repair."
      Kemp M.G., Mason A.C., Carreira A., Reardon J.T., Haring S.J., Borgstahl G.E., Kowalczykowski S.C., Sancar A., Wold M.S.
      J. Biol. Chem. 285:4788-4797(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    30. "A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombination."
      Lee D.H., Pan Y., Kanner S., Sung P., Borowiec J.A., Chowdhury D.
      Nat. Struct. Mol. Biol. 17:365-372(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DNA REPAIR, PHOSPHORYLATION, DEPHOSPHORYLATION BY PP4, INTERACTION WITH PPP4C; PPP4R2 AND RAD51, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-8; SER-23; SER-29 AND SER-33.
    31. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND SER-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    32. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    33. "E3 ligase RFWD3 participates in replication checkpoint control."
      Gong Z., Chen J.
      J. Biol. Chem. 286:22308-22313(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REPLICATION CHECKPOINT, INTERACTION WITH RFWD3, SUBCELLULAR LOCATION.
    34. "RING finger and WD repeat domain 3 (RFWD3) associates with replication protein A (RPA) and facilitates RPA-mediated DNA damage response."
      Liu S., Chu J., Yucer N., Leng M., Wang S.Y., Chen B.P., Hittelman W.N., Wang Y.
      J. Biol. Chem. 286:22314-22322(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RFWD3, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-21.
    35. "DNA-PK-dependent RPA2 hyperphosphorylation facilitates DNA repair and suppresses sister chromatid exchange."
      Liaw H., Lee D., Myung K.
      PLoS ONE 6:E21424-E21424(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-4 AND SER-8 BY PRKDC, MUTAGENESIS OF SER-4 AND SER-8.
    36. "Translational regulation of RPA2 via internal ribosomal entry site and by eIF3a."
      Yin J.Y., Dong Z.Z., Liu R.Y., Chen J., Liu Z.Q., Zhang J.T.
      Carcinogenesis 34:1224-1231(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY DNA DAMAGE.
    37. "The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding."
      Bochkarev A., Bochkareva E., Frappier L., Edwards A.M.
      EMBO J. 18:4498-4504(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 43-171 IN COMPLEX WITH RPA1 AND RPA3.
    38. "Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA."
      Mer G., Bochkarev A., Gupta R., Bochkareva E., Frappier L., Ingles C.J., Edwards A.M., Chazin W.J.
      Cell 103:449-456(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 172-270, INTERACTION WITH RAD52; UNG AND XPA, REGION.
    39. "Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA."
      Bochkareva E., Korolev S., Lees-Miller S.P., Bochkarev A.
      EMBO J. 21:1855-1863(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 44-171.

    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: October 1, 2014
    This is version 160 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

    External Data

    Dasty 3