# PRIM1

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Protein-coding gene in the species Homo sapiens

PRIM1 Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4BPU, 4BPW, 4BPX, 4LIK, 4LIL, 4MHQ, 4RR2, 5EXR Identifiers Aliases PRIM1, p49, primase (DNA) subunit 1, DNA primase subunit 1 External IDs OMIM: 176635; MGI: 97757; HomoloGene: 730; GeneCards: PRIM1; OMA:PRIM1 - orthologs Gene location (Human) Chr. Chromosome 12 (human)[1] Band 12q13.3 Start 56,731,296 bp[1] End 56,752,374 bp[1] Gene location (Mouse) Chr. Chromosome 10 (mouse)[2] Band 10 76.39 cM|10 D3 Start 127,851,037 bp[2] End 127,865,906 bp[2] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gonad testicle ganglionic eminence ventricular zone bone marrow bone marrow cell 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 Species Human Mouse 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 Mb Chr 10: 127.85 – 127.87 Mb PubMed search [3] [4] Wikidata View/Edit Human View/Edit Mouse

**DNA primase small subunit** is in humans is encoded by the *PRIM1* [gene](/source/Gene) and is part of the [enzyme](/source/Enzyme) [DNA polymerase alpha](/source/DNA_polymerase_alpha).[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***](#cite_ref-refGRCh38Ensembl_1-0) [***b***](#cite_ref-refGRCh38Ensembl_1-1) [***c***](#cite_ref-refGRCh38Ensembl_1-2) [GRCh38: Ensembl release 89: ENSG00000198056](http://May2017.archive.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000198056) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. ^ [***a***](#cite_ref-refGRCm38Ensembl_2-0) [***b***](#cite_ref-refGRCm38Ensembl_2-1) [***c***](#cite_ref-refGRCm38Ensembl_2-2) [GRCm38: Ensembl release 89: ENSMUSG00000025395](http://May2017.archive.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000025395) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. **[^](#cite_ref-3)** ["Human PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=5557). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-4)** ["Mouse PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=19075). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-pmid8530050_5-0)** 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](/source/Doi_(identifier)):[10.1006/geno.1995.1155](https://doi.org/10.1006%2Fgeno.1995.1155). [PMID](/source/PMID_(identifier)) [8530050](https://pubmed.ncbi.nlm.nih.gov/8530050).

## Further reading

- Stadlbauer F, Brueckner A, Rehfuess C, et al. (1994). ["DNA replication in vitro by recombinant DNA-polymerase-alpha-primase"](https://doi.org/10.1111%2Fj.1432-1033.1994.tb18925.x). *Eur. J. Biochem*. **222** (3): 781–93. [doi](/source/Doi_(identifier)):[10.1111/j.1432-1033.1994.tb18925.x](https://doi.org/10.1111%2Fj.1432-1033.1994.tb18925.x). [PMID](/source/PMID_(identifier)) [8026492](https://pubmed.ncbi.nlm.nih.gov/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](/source/Doi_(identifier)):[10.1016/0378-1119(94)90802-8](https://doi.org/10.1016%2F0378-1119%2894%2990802-8). [PMID](/source/PMID_(identifier)) [8125298](https://pubmed.ncbi.nlm.nih.gov/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](/source/Doi_(identifier)):[10.1016/S0378-1119(97)00411-3](https://doi.org/10.1016%2FS0378-1119%2897%2900411-3). [PMID](/source/PMID_(identifier)) [9373149](https://pubmed.ncbi.nlm.nih.gov/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"](https://doi.org/10.1074%2Fjbc.273.34.21608). *J. Biol. Chem*. **273** (34): 21608–15. [doi](/source/Doi_(identifier)):[10.1074/jbc.273.34.21608](https://doi.org/10.1074%2Fjbc.273.34.21608). [PMID](/source/PMID_(identifier)) [9705292](https://pubmed.ncbi.nlm.nih.gov/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](/source/Doi_(identifier)):[10.1021/bi9908991](https://doi.org/10.1021%2Fbi9908991). [PMID](/source/PMID_(identifier)) [10504261](https://pubmed.ncbi.nlm.nih.gov/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](/source/Doi_(identifier)):[10.1016/S0014-5793(02)03197-6](https://doi.org/10.1016%2FS0014-5793%2802%2903197-6). [PMID](/source/PMID_(identifier)) [12220650](https://pubmed.ncbi.nlm.nih.gov/12220650). [S2CID](/source/S2CID_(identifier)) [27852377](https://api.semanticscholar.org/CorpusID:27852377).

## External links

- Overview of all the structural information available in the [PDB](/source/Protein_Data_Bank) for [UniProt](/source/UniProt): *[P49642](https://www.ebi.ac.uk/pdbe/pdbe-kb/proteins/P49642)* (Human DNA primase small subunit (PRIM1)) at the [PDBe-KB](/source/PDBe-KB).

v t e DNA replication (comparing prokaryotic to eukaryotic) Initiation Prokaryotic (initiation) Pre-replication complex dnaC Helicase dnaA dnaB T7 Primase dnaG Eukaryotic (preparation in G1 phase) Pre-replication complex Origin recognition complex ORC1 ORC2 ORC3 ORC4 ORC5 ORC6 Cdc6 Cdt1 Minichromosome maintenance MCM2 MCM3 MCM4 MCM5 MCM6 MCM7 Licensing factor Autonomously replicating sequence Single-strand binding protein SSBP2 SSBP3 SSBP4 RNase H RNASEH1 RNASEH2A Helicase: HFM1 Primase: PRIM1 PRIM2 Both Origin of replication/Ori/Replicon Replication fork Lagging and leading strands Okazaki fragments Primer Replication Prokaryotic (elongation) DNA polymerase III holoenzyme dnaC dnaE dnaH dnaN dnaQ dnaT dnaX holA holB holC holD holE Replisome DNA ligase DNA clamp Topoisomerase DNA gyrase Prokaryotic DNA polymerase: DNA polymerase I Klenow fragment Eukaryotic (synthesis in S phase) Replication factor C RFC1 Flap endonuclease FEN1 Topoisomerase Replication protein A RPA1 Eukaryotic DNA polymerase: alpha POLA1 POLA2 PRIM1 PRIM2 delta POLD1 POLD2 POLD3 POLD4 epsilon POLE POLE2 POLE3 POLE4 DNA clamp PCNA Control of chromosome duplication Both Movement: Processivity DNA ligase Termination Telomere: Telomerase TERT TERC DKC1

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