PRIM1

Protein-coding gene in the species Homo sapiens
PRIM1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4BPU, 4BPW, 4BPX, 4LIK, 4LIL, 4MHQ, 4RR2, 5EXR

Identifiers
AliasesPRIM1, p49, primase (DNA) subunit 1, DNA primase subunit 1
External IDsOMIM: 176635; MGI: 97757; HomoloGene: 730; GeneCards: PRIM1; OMA:PRIM1 - orthologs
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for PRIM1
Genomic location for PRIM1
Band12q13.3Start56,731,296 bp[1]
End56,752,374 bp[1]
Gene location (Mouse)
Chromosome 10 (mouse)
Chr.Chromosome 10 (mouse)[2]
Chromosome 10 (mouse)
Genomic location for PRIM1
Genomic location for PRIM1
Band10 76.39 cM|10 D3Start127,851,037 bp[2]
End127,865,906 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • gonad

  • testicle

  • ganglionic eminence

  • ventricular zone

  • bone marrow

  • bone marrow cells

  • rectum

  • Achilles tendon

  • lymph node

  • islet of Langerhans
Top expressed in
  • medial ganglionic eminence

  • fetal liver hematopoietic progenitor cell

  • genital tubercle

  • vas deferens

  • maxillary prominence

  • primitive streak

  • mandibular prominence

  • internal carotid artery

  • condyle

  • tail of embryo
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • DNA-directed 5'-3' RNA polymerase activity
  • transferase activity
  • nucleotidyltransferase activity
  • metal ion binding
  • single-stranded DNA binding
  • DNA primase activity
Cellular component
  • membrane
  • nucleoplasm
  • alpha DNA polymerase:primase complex
  • primosome complex
Biological process
  • DNA replication
  • G1 phase
  • DNA replication initiation
  • DNA replication, synthesis of RNA primer
  • telomere maintenance via semi-conservative replication
  • G1/S transition of mitotic cell cycle
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5557

19075

Ensembl

ENSG00000198056

ENSMUSG00000025395

UniProt

P49642

P20664

RefSeq (mRNA)

NM_000946

NM_008921

RefSeq (protein)

NP_000937

NP_032947

Location (UCSC)Chr 12: 56.73 – 56.75 MbChr 10: 127.85 – 127.87 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

DNA primase small subunit is an enzyme that in humans is encoded by the PRIM1 gene.[5]

The replication of DNA in eukaryotic cells is carried out by a complex chromosomal replication apparatus, in which DNA polymerase alpha and primase are two key enzymatic components. Primase, which is a heterodimer of a small subunit and a large subunit, synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication. The protein encoded by this gene is the small, 49 kDa primase subunit.

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000198056 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025395 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Shiratori A, Okumura K, Nogami M, Taguchi H, Onozaki T, Inoue T, Ando T, Shibata T, Izumi M, Miyazawa H, et al. (Feb 1996). "Assignment of the 49-kDa (PRIM1) and 58-kDa (PRIM2A and PRIM2B) subunit genes of the human DNA primase to chromosome bands 1q44 and 6p11.1-p12". Genomics. 28 (2): 350–3. doi:10.1006/geno.1995.1155. PMID 8530050.

Further reading

  • Stadlbauer F, Brueckner A, Rehfuess C, et al. (1994). "DNA replication in vitro by recombinant DNA-polymerase-alpha-primase". Eur. J. Biochem. 222 (3): 781–93. doi:10.1111/j.1432-1033.1994.tb18925.x. PMID 8026492.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Schneider A, Smith RW, Kautz AR, et al. (1998). "Primase activity of human DNA polymerase alpha-primase. Divalent cations stabilize the enzyme activity of the p48 subunit". J. Biol. Chem. 273 (34): 21608–15. doi:10.1074/jbc.273.34.21608. PMID 9705292.
  • Arezi B, Kirk BW, Copeland WC, Kuchta RD (1999). "Interactions of DNA with human DNA primase monitored with photoactivatable cross-linking agents: implications for the role of the p58 subunit". Biochemistry. 38 (39): 12899–907. doi:10.1021/bi9908991. PMID 10504261.
  • Smith RW, Nasheuer HP (2002). "Control of complex formation of DNA polymerase alpha-primase and cell-free DNA replication by the C-terminal amino acids of the largest subunit p180". FEBS Lett. 527 (1–3): 143–6. doi:10.1016/S0014-5793(02)03197-6. PMID 12220650. S2CID 27852377.

External links

  • Overview of all the structural information available in the PDB for UniProt: P49642 (Human DNA primase small subunit (PRIM1)) at the PDBe-KB.
  • v
  • t
  • e
Initiation
Prokaryotic
(initiation)
Eukaryotic
(preparation in
G1 phase)
Both
Replication
Prokaryotic
(elongation)
Eukaryotic
(synthesis in
S phase)
Both
Termination


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