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FLASH GENE
Symbol PRIMPOL contributors: mct - updated : 10-10-2019
HGNC name primase and DNA directed polymerase
HGNC id 26575
Corresponding disease
MYP22 Myopia 22, autosomal dominant
Location 4q35.1      Physical location : -
Synonym name
  • coiled-coil domain containing 111
  • Synonym symbol(s) FLJ33167, CCDC111, MYP22, Primpol1
    DNA
    TYPE functioning gene
    STRUCTURE 45.28 kb     14 Exon(s)
    MAPPING cloned Y linked N status provisional
    RNA
    TRANSCRIPTS type messenger
    identificationnb exonstypebpproduct
    ProteinkDaAAspecific expressionYearPubmed
    14 - 2164 64 560 - 2018 29608762
    15 - 2203 - 573 - 2018 29608762
    15 - 2200 - 572 - 2018 29608762
    12 - 2161 - 559 - 2018 29608762
    12 - 1912 - 476 - 2018 29608762
    14 - 2073 - 341 - 2018 29608762
    13 - 2034 - 328 - 2018 29608762
    13 - 2031 - 327 - 2018 29608762
    12 - 1886 - 385 - 2018 29608762
    14 - 2161 - 560 - 2018 29608762
    15 - 2197 - 572 - 2018 29608762
    14 - 2158 - 559 - 2018 29608762
    13 - 1925 - 431 - 2018 29608762
    12 - 1795 - 328 - 2018 29608762
    EXPRESSION
    Type
       expressed in (based on citations)
    organ(s)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Cardiovascularheart    
    Hearing/Equilibriumear    
    Urinarybladder    
    tissue
    SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
    Connective    
    cell lineage
    cell lines
    fluid/secretion
    at STAGE
    PROTEIN
    PHYSICAL PROPERTIES
    STRUCTURE
    motifs/domains
  • an Archeal-Eukaryotic Primases (AEP) core
  • a C-terminal Zn finger-containing domain (ZnFD), that is exclusively required for primer formation and for PRIMPOL function, and is also essential in the subsequent translocation/elongation events during DNA primer synthesis
  • a coiled-coil domain
  • HOMOLOGY
    Homologene
    FAMILY
    CATEGORY DNA associated
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,cytoplasm,organelle,mitochondria,matrix
    intracellular,nucleus
    text
  • DNA-dependent DNA primase and translesion synthesis DNA polymerase found in the nucleus and mitochondria
  • basic FUNCTION
  • is a novel factor involved in the response to DNA replication stress
  • is a highly error-prone polymerase regulated by single-stranded DNA binding protein
  • / PRIMPOL implicated in promoting restart of DNA synthesis downstream of, but closely coupled to, G4 replication impediments
  • ability of PRIMPOL to function as a DNA primase stems from a simple but remarkable feature-almost complete lack of contacts to the DNA primer strand
  • is capable of acting as a DNA polymerase, with the ability to extend primers and also bypass a variety of oxidative and photolesions
  • is a human deoxyribonucleic acid (DNA) polymerase that also possesses primase activity and is involved in DNA damage tolerance, the prevention of genome instability and mitochondrial DNA maintenance
  • can reinitiate stalled mtDNA replication and can prime mtDNA replication from nonconventional origins
  • is a monomeric enzyme whose DNA primase activity is required to rescue stalled replication forks during nuclear and mitochondrial DNA replication
  • is an enzyme that maintains efficient DNA duplication by repriming replication restart downstream of replicase stalling lesions and structures
  • importance of PRIMPOL for maintaining efficient DNA replication in unperturbed cells and its complementary roles, with POLH, in damage tolerance in human cells
  • is a primase/polymerase specialized in re-starting stalled forks by repriming beyond lesions such as pyrimidine dimers, and replication-perturbing structures including G-quadruplexes and R-loops
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
  • WRNIP1 and PRIMPOL form a complex in cells
  • INTERACTION
    DNA
    RNA
    small molecule
    protein
  • POLDIP2 stimulates the polymerase activity of PRIMPOL, enhancing both its capacity to bind DNA and the processivity of the catalytic domain
  • WRNIP1 is involved in the degradation of PRIMPOL via the proteasome
  • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    corresponding disease(s) MYP22
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    ANIMAL & CELL MODELS