PRIM2
DNA primase large subunit
Also known as: PRI2_HUMAN, PRIM2A
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P49643
- Gene
- PRIM2
- Ensembl
- ENSG00000146143
- Chromosome
- 6
- Canonical length
- 509 aa
- Protein class
- Plasma proteins, Predicted intracellular proteins
- Subcellular location
- Nucleoplasm
OverviewNCBI Gene
This gene encodes the 58 kilodalton subunit of DNA primase, an enzyme that plays a key role in the replication of DNA. The encoded protein forms a heterodimer with a 49 kilodalton subunit. This heterodimer functions as a DNA-directed RNA polymerase to synthesize small RNA primers that are used to create Okazaki fragments on the lagging strand of the DNA. Alternative splicing of this gene results in multiple transcript variants. This gene has a related pseudogene, which is also present on chromosome 6. [provided by RefSeq, Apr 2014]
Canonical amino-acid sequenceUniProt
509 residues, UniProt reviewed canonical sequence.
>P49643|PRIM2
1 MEFSGRKWRK LRLAGDQRNA SYPHCLQFYL QPPSENISLI EFENLAIDRV KLLKSVENLG
61 VSYVKGTEQY QSKLESELRK LKFSYRENLE DEYEPRRRDH ISHFILRLAY CQSEELRRWF
121 IQQEMDLLRF RFSILPKDKI QDFLKDSQLQ FEAISDEEKT LREQEIVASS PSLSGLKLGF
181 ESIYKIPFAD ALDLFRGRKV YLEDGFAYVP LKDIVAIILN EFRAKLSKAL ALTARSLPAV
241 QSDERLQPLL NHLSHSYTGQ DYSTQGNVGK ISLDQIDLLS TKSFPPCMRQ LHKALRENHH
301 LRHGGRMQYG LFLKGIGLTL EQALQFWKQE FIKGKMDPDK FDKGYSYNIR HSFGKEGKRT
361 DYTPFSCLKI ILSNPPSQGD YHGCPFRHSD PELLKQKLQS YKISPGGISQ ILDLVKGTHY
421 QVACQKYFEM IHNVDDCGFS LNHPNQFFCE SQRILNGGKD IKKEPIQPET PQPKPSVQKT
481 KDASSALASL NSSLEMDMEG LEDYFSEDSLocalizationUniProt · AlphaFold · HPA
Whether an antibody against PRIM2 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Intracellular
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.32
- Highest tissue expression
- 30 nTPM
Expression across tissuesHPA
Tissue
- prostate: 30 nTPM
- thymus: 15 nTPM
- bone marrow: 14 nTPM
- tonsil: 11 nTPM
- lymph node: 10 nTPM
- rectum: 8 nTPM
Single-cell type
- prostatic glandular cells: 480 nCPM
- monocyte progenitors: 235 nCPM
- erythrocyte progenitors: 222 nCPM
- megakaryocyte progenitors: 202 nCPM
- neutrophil progenitors: 180 nCPM
- microglia: 164 nCPM
Immune cell
- naive CD8 T-cell: 5.9 nTPM
- memory CD8 T-cell: 5.6 nTPM
- NK-cell: 5.3 nTPM
- plasmacytoid DC: 5.2 nTPM
- T-reg: 4.8 nTPM
- MAIT T-cell: 4.4 nTPM
Brain region
- white matter: 44 nTPM
- choroid plexus: 30 nTPM
- midbrain: 25 nTPM
- cerebral cortex: 24 nTPM
- hypothalamus: 24 nTPM
- pons: 23 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 1.03
- gnomAD pLI
- 0
- gnomAD missense Z
- 0.76
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 7% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
Molecular functions
Cellular components
Protein domainsUniProt · Pfam · InterPro
- DNA primase large subunit, eukaryotic/archaeal
- DNA primase, large subunit, eukaryotic
- DNA primase, large subunit C-terminal domain, eukaryotic and archaeal
- Eukaryotic and archaeal DNA primase, large subunit C-terminal domain
- Eukaryotic and archaeal DNA primase, large subunit N-terminal domain
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of PRIM2 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads PRIM2 as an antibody target. Whether an autoantibody or antibody against PRIM2 could matter depends on whether native PRIM2 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
PRIM2 is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label PRIM2 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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