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P35244

- RFA3_HUMAN

UniProt

P35244 - RFA3_HUMAN

Protein

Replication protein A 14 kDa subunit

Gene

RPA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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 (PubMed:9430682). 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 (PubMed:7697716). Plays also a role in base excision repair (BER), probably through interaction with UNG (PubMed:9765279). 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. RPA3 has its own single-stranded DNA-binding activity and may be responsible for polarity of the binding of the complex to DNA (PubMed:19010961). As part of the alternative replication protein A complex, aRPA, binds single-stranded DNA and probably plays a role in DNA repair. Compared to the RPA2-containing, canonical RPA complex, may not support chromosomal DNA replication and cell cycle progression through S-phase. The aRPA may not promote efficient priming by DNA polymerase alpha but could support DNA polymerase delta synthesis in the presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange (PubMed:19996105).6 Publications

    GO - Molecular functioni

    1. damaged DNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. single-stranded DNA 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. nucleotide-excision repair Source: UniProtKB
    12. nucleotide-excision repair, DNA damage removal Source: Reactome
    13. nucleotide-excision repair, DNA gap filling Source: Reactome
    14. telomere maintenance Source: Reactome
    15. telomere maintenance via recombination Source: Reactome
    16. telomere maintenance via semi-conservative replication Source: Reactome
    17. transcription-coupled nucleotide-excision repair Source: Reactome

    Keywords - Biological processi

    DNA damage, DNA recombination, DNA repair, DNA replication

    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 14 kDa subunit
    Short name:
    RP-A p14
    Alternative name(s):
    Replication factor A protein 3
    Short name:
    RF-A protein 3
    Gene namesi
    Name:RPA3
    Synonyms:REPA3, RPA14
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:10291. RPA3.

    Subcellular locationi

    GO - Cellular componenti

    1. DNA replication factor A complex Source: UniProtKB
    2. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34653.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 121120Replication protein A 14 kDa subunitPRO_0000097276Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylvaline3 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP35244.
    PaxDbiP35244.
    PeptideAtlasiP35244.
    PRIDEiP35244.

    PTM databases

    PhosphoSiteiP35244.

    Expressioni

    Gene expression databases

    ArrayExpressiP35244.
    BgeeiP35244.
    CleanExiHS_RPA3.
    GenevestigatoriP35244.

    Organism-specific databases

    HPAiHPA005708.

    Interactioni

    Subunit structurei

    Component of the canonical replication protein A complex (RPA), an heterotrimer composed of RPA1, RPA2 and RPA3. Also component of the aRPA, the alternative replication protein A complex, a trimeric complex similar to the replication protein A complex/RPA but where RPA1 and RPA3 are associated with RPA4 instead of RPA2.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RAD52P433512EBI-621428,EBI-706448
    RPA1P276944EBI-621428,EBI-621389
    RPA2P159276EBI-621428,EBI-621404

    Protein-protein interaction databases

    BioGridi112039. 376 interactions.
    DIPiDIP-24190N.
    IntActiP35244. 10 interactions.
    MINTiMINT-5002568.
    STRINGi9606.ENSP00000223129.

    Structurei

    Secondary structure

    1
    121
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 63
    Beta strandi10 – 123
    Helixi14 – 207
    Beta strandi24 – 3411
    Beta strandi38 – 447
    Beta strandi50 – 545
    Beta strandi65 – 739
    Beta strandi79 – 868
    Beta strandi90 – 923
    Helixi96 – 10813
    Helixi110 – 1123

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1L1OX-ray2.80A/D1-121[»]
    1QUQX-ray2.50B/D1-121[»]
    2PI2X-ray2.00E/F/G/H1-121[»]
    2PQAX-ray2.50B/D1-121[»]
    2Z6KX-ray3.00C/D1-121[»]
    3KDFX-ray1.98A/C1-121[»]
    ProteinModelPortaliP35244.
    SMRiP35244. Positions 2-118.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35244.

    Family & Domainsi

    Phylogenomic databases

    eggNOGiNOG42188.
    HOGENOMiHOG000252930.
    HOVERGENiHBG003004.
    InParanoidiP35244.
    KOiK10740.
    OMAiDQPVCFV.
    OrthoDBiEOG77WWFG.
    PhylomeDBiP35244.
    TreeFamiTF105243.

    Family and domain databases

    Gene3Di2.40.50.140. 1 hit.
    InterProiIPR012340. NA-bd_OB-fold.
    IPR013970. Rep_factor-A_3.
    [Graphical view]
    PfamiPF08661. Rep_fac-A_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P35244-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVDMMDLPRS RINAGMLAQF IDKPVCFVGR LEKIHPTGKM FILSDGEGKN    50
    GTIELMEPLD EEISGIVEVV GRVTAKATIL CTSYVQFKED SHPFDLGLYN 100
    EAVKIIHDFP QFYPLGIVQH D 121
    Length:121
    Mass (Da):13,569
    Last modified:February 1, 1994 - v1
    Checksum:i3FD99851959FB498
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07493 mRNA. Translation: AAA58350.1.
    BT007320 mRNA. Translation: AAP35984.1.
    DQ003136 Genomic DNA. Translation: AAX84517.1.
    AC004948 Genomic DNA. Translation: AAQ96878.1.
    BC005264 mRNA. Translation: AAH05264.1.
    BC009868 mRNA. Translation: AAH09868.1.
    CCDSiCCDS5356.1.
    PIRiA46008.
    RefSeqiNP_002938.1. NM_002947.3.
    UniGeneiHs.487540.

    Genome annotation databases

    EnsembliENST00000223129; ENSP00000223129; ENSG00000106399.
    ENST00000396682; ENSP00000379914; ENSG00000106399.
    GeneIDi6119.
    KEGGihsa:6119.
    UCSCiuc003sri.3. human.

    Polymorphism databases

    DMDMi464608.

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07493 mRNA. Translation: AAA58350.1 .
    BT007320 mRNA. Translation: AAP35984.1 .
    DQ003136 Genomic DNA. Translation: AAX84517.1 .
    AC004948 Genomic DNA. Translation: AAQ96878.1 .
    BC005264 mRNA. Translation: AAH05264.1 .
    BC009868 mRNA. Translation: AAH09868.1 .
    CCDSi CCDS5356.1.
    PIRi A46008.
    RefSeqi NP_002938.1. NM_002947.3.
    UniGenei Hs.487540.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1L1O X-ray 2.80 A/D 1-121 [» ]
    1QUQ X-ray 2.50 B/D 1-121 [» ]
    2PI2 X-ray 2.00 E/F/G/H 1-121 [» ]
    2PQA X-ray 2.50 B/D 1-121 [» ]
    2Z6K X-ray 3.00 C/D 1-121 [» ]
    3KDF X-ray 1.98 A/C 1-121 [» ]
    ProteinModelPortali P35244.
    SMRi P35244. Positions 2-118.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112039. 376 interactions.
    DIPi DIP-24190N.
    IntActi P35244. 10 interactions.
    MINTi MINT-5002568.
    STRINGi 9606.ENSP00000223129.

    PTM databases

    PhosphoSitei P35244.

    Polymorphism databases

    DMDMi 464608.

    Proteomic databases

    MaxQBi P35244.
    PaxDbi P35244.
    PeptideAtlasi P35244.
    PRIDEi P35244.

    Protocols and materials databases

    DNASUi 6119.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000223129 ; ENSP00000223129 ; ENSG00000106399 .
    ENST00000396682 ; ENSP00000379914 ; ENSG00000106399 .
    GeneIDi 6119.
    KEGGi hsa:6119.
    UCSCi uc003sri.3. human.

    Organism-specific databases

    CTDi 6119.
    GeneCardsi GC07M007643.
    HGNCi HGNC:10291. RPA3.
    HPAi HPA005708.
    MIMi 179837. gene.
    neXtProti NX_P35244.
    PharmGKBi PA34653.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG42188.
    HOGENOMi HOG000252930.
    HOVERGENi HBG003004.
    InParanoidi P35244.
    KOi K10740.
    OMAi DQPVCFV.
    OrthoDBi EOG77WWFG.
    PhylomeDBi P35244.
    TreeFami TF105243.

    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 RPA3. human.
    EvolutionaryTracei P35244.
    GeneWikii RPA3.
    GenomeRNAii 6119.
    NextBioi 23763.
    PROi P35244.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35244.
    Bgeei P35244.
    CleanExi HS_RPA3.
    Genevestigatori P35244.

    Family and domain databases

    Gene3Di 2.40.50.140. 1 hit.
    InterProi IPR012340. NA-bd_OB-fold.
    IPR013970. Rep_factor-A_3.
    [Graphical view ]
    Pfami PF08661. Rep_fac-A_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50249. SSF50249. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, overexpression, and genomic mapping of the 14-kDa subunit of human replication protein A."
      Umbricht C.B., Kelly T.J.
      J. Biol. Chem. 268:6131-6138(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. NIEHS SNPs program
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [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].
      Tissue: Kidney and Lung.
    6. "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.
    7. "Rpa4, a homolog of the 34-kilodalton subunit of the replication protein A complex."
      Keshav K.F., Chen C., Dutta A.
      Mol. Cell. Biol. 15:3119-3128(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RPA4.
    8. "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.
    9. "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.
    10. "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 VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. "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: IDENTIFICATION IN THE ARPA COMPLEX, FUNCTION OF THE ARPA COMPLEX.
    12. "Evidence for direct contact between the RPA3 subunit of the human replication protein A and single-stranded DNA."
      Salas T.R., Petruseva I., Lavrik O., Saintome C.
      Nucleic Acids Res. 37:38-46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SINGLE-STRANDED DNA-BINDING.
    13. "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: FUNCTION OF THE ARPA COMPLEX.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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) IN COMPLEX WITH RPA1 AND RPA2.

    Entry informationi

    Entry nameiRFA3_HUMAN
    AccessioniPrimary (citable) accession number: P35244
    Secondary accession number(s): Q549U6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 136 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, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3