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FLASH GENE
Symbol RPA1 contributors: mct - updated : 01-06-2019
HGNC name replication protein A1, 70kDa
HGNC id 10289
Location 17p13.3      Physical location : 1.733.272 - 1.802.848
Synonym name
  • G replication protein A,subunit 1
  • RF-A protein 1
  • single-stranded DNA-binding protein
    • Synonym symbol(s) RPA70, REPA1, HSSB, RF-A, RP-A, HSU24186, MGC120333, MGC120334, MST075, MSTP075
    DNA
    TYPE functioning gene
    STRUCTURE 69.58 kb     17 Exon(s)
    10 Kb 5' upstream gene genomic sequence study
    MAPPING cloned Y linked   status confirmed
    Map pter - D17S643 ,(D17S28 , D17S30 ) - RPA1 - PFN1 - SLC2A4 - cen
    Authors Umbricht (94)
    RNA
    TRANSCRIPTS type messenger
    identificationnb exonstypebpproduct
    ProteinkDaAAspecific expressionYearPubmed
    17 - 4345 68.1 616 - 2008 18245774
    EXPRESSION
    Type widely
       expressed in (based on citations)
    organ(s)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Digestiveintestinesmall intestine  highly
    Hearing/Equilibriumear   highly
    Respiratoryrespiratory tractlarynx  highly
    Visualeye    
    cell lineage spermatocytes
    cell lines
    fluid/secretion
    at STAGE
    PROTEIN
    PHYSICAL PROPERTIES
    STRUCTURE
    motifs/domains
  • a N terminal domain containing six ssDNA-binding domains (DBDs), involved in protein interaction, and critical component of the RPA-MRN protein-protein interaction, DBD-F can interact with ssDNA, with multiple proteins, and may play a role in regulating RPA function upon phosphorylation of RPA2
  • a central DNA-binding domain (composed of two copies of a ss-DNA binding motif)
  • three DNA-binding domains (DBD), DBD-A, DBD-B and DBD-C
  • and a DNA helix-destabilization (unwinding) activity,
  • a zinc finger and a C terminal intersubunit interaction domains
    • mono polymer heteromer , trimer
    HOMOLOGY
    Homologene
    FAMILY
  • replication factor A protein 1 family
    • CATEGORY DNA associated
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,nucleus,nucleoplasm,nuclear bodies,PML
    text colocalizes with BRIP1 in nuclear foci after DNA damage
    basic FUNCTION
  • essential for DNA replication and thus for progression through S phase
  • colocalizing with RAD51 on synapsed axes in meiosis and facilitating RAD51 function
  • also colocalizing with BLM in meiotic prophase nuclei of spermatocytes
  • involved in processes including replication, recombination, transcription, telomere maintenance, and in regulation of telomerase (essential for homologous recombination and DNA replication)
  • essential for DNA replication, repair, and recombination
  • roles of RPA1, BRIP1, and other DNA helicases in the metabolism of damaged DNA that can interfere with basic cellular processes of DNA metabolism
  • plays a key role in DNA replication and activation of the ATR checkpoint
  • plays a regulatory role in DNA damage responses via repression of RFC2 ubiquitylation in cells
  • proper orientation of XPA and RPA1 in the stage of preincision was achieved in the absence of ERCC3 and XPG
  • with RPA1, and RPA2, plays essential roles in DNA transactions
  • RPA1 and MEIOB, are essential to ensure the proper stabilization of recombinases which is required for successful homology search and meiotic recombination
  • RPA1 and RPA2 are arranged from 5prime to 3prime along the unfolded telomeric G4, as already described for unstructured single-stranded DNA
  • single-stranded DNA binding protein that plays an essential role in telomere maintenance
  • phosphorylated RPA1 recruits repair factors to stalled forks, thereby enhancing fork integrity during replication stress
    • CELLULAR PROCESS nucleotide, replication
    nucleotide, repair, base excision repair
    nucleotide, repair, nucleotide excision repair
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
  • component of a trimeric single strand binding protein of the replication protein A complex, involved in replication, homologous recombination and nucleotide excision repair
  • three subunits: RPA1, RPA2, and RPA3)
  • HSF1-RPA1 complex leads to preloading of RNA polymerase II and opens the chromatin structure by recruiting a histone chaperone SSRP1
    • INTERACTION
    DNA binding
    RNA
    small molecule
    protein
  • RBT1
  • NOS3 repressor of mutated NOS3
  • interacting with XRCC3 and RAD52
  • interaction with WRN or BLM helicases plays an important role in the mechanism for RPA stimulation of helicase-catalyzed DNA unwinding
  • first regulatory partner of BRIP1 (FANCJ) (BRIP1-RPA1 interaction is likely to be important for the role of the helicase to more efficiently unwind DNA repair intermediates to maintain genomic stability
  • direct interaction between RPA1 with both NBS1 and MRE11
  • PAXIP1 and RPA1, both involved in DNA replication and DNA repair, are HLTF-interacting proteins although cells depleted of HLTF did not show defects in cellular responses to DNA damage
  • interacts with the specific proteins among those that play roles in the regulation of the replication fork progression
  • upon replication blockage, WRN and RPA1 functionally interact and cooperate to help properly resolve replication forks and maintain genome stability
  • interacting with DMRT2 (potent inhibitor of the RPA1 displacing activity of HNRNPA1)
  • BID associates with RPA1 and stimulates the recruitment and/or stabilization of ATR-ATRIP to the DNA damage sensor complex
  • recruits UNG to sites of deamination and keeps DNA in a single stranded conformation, thus avoiding error-free base excision repair of the deaminated cytosine
  • interaction between the wing motif of HSF1 and replication protein A (RPA1), which is involved in DNA metabolism
  • HSF1 access to nucleosomal DNA requires its interaction with RPA1, which plays a major role in DNA replication and repair
  • RPAIN is the nuclear transporter of RPA1
  • direct binding of both ssDNA and the transactivation domain 2 of TP53 (TP53TAD2) to DBD-F, as well as DBD-F-directed dsDNA strand separation by RPA1
  • AJUBA protects against unscheduled ATR signaling by preventing inappropriate RPA1 phosphorylation
  • ATR signals the accumulation of replication protein A (RPA1)-covered single-stranded DNA (ssDNA), which is caused by replication obstacles
  • ATR-mediated suppression of dormant origins shields active forks against irreversible breakage via preventing exhaustion of nuclear RPA1
  • BCAS2 and PRPF19 subunits of the PSO4 complex directly interact and colocalize with replication protein A (RPA1)
  • partnerships between RPA1 and interacting human DNA helicases may greatly enhance their ability to dislodge proteins bound to duplex DNA, an activity that is likely to be highly relevant to their biological roles in DNA metabolism
  • BRIP1 was able to displace TERF2 from the telomeric substrate in an RPA1-dependent manner
  • FAN1 possesses the ability to promote the ICL repair of 5'-flapped DNA covered by RPA1
  • ability of phosphorylated RPA1 to stimulate fork recovery is mediated through the PALB2 tumor suppressor protein
  • SHFM1 acts as a DNA mimic to attenuate the affinity of RPA1 for ssDNA
  • flexibly-tethered DNA2-RPA1 interaction that recruits DNA2 to RPA1-coated DNA
  • flexibly-tethered DNA2-RPA1 interaction that recruits DNA2 to RPA1-coated DNA
  • SLFN11 interacts directly with RPA1 and is recruited to sites of DNA damage in an RPA1-dependent manner
  • CHTF8 interacts with replication protein A (RPA1) in response to replication stress
  • specifically interacts with RPA1 (Replication protein A) via two conserved RPA-binding domains and is therefore recruited to stalled replication forks
  • EXO5 is epistatic to BLM at stalled replication forks, and its nuclease activity is enhanced by BLM and RPA1
  • prominent RPA1-interacting partners are the tumor suppressor protein TP53, RAD51, ATRIP and ETAA1
    • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    ANIMAL & CELL MODELS