Version 5.4
Mus musculus Protein: Prim2
Summary
InnateDB Protein IDBP-140499.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Prim2
Protein Name DNA primase, p58 subunit
Synonyms AI323589;
Species Mus musculus
Ensembl Protein ENSMUSP00000027312
InnateDB Gene IDBG-140497 (Prim2)
Protein Structure
UniProt Annotation
Function DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication.
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 6 experimentally validated interaction(s) in this database.
Experimentally validated
Total 6 [view]
Protein-Protein 6 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0003677 DNA binding
GO:0003896 DNA primase activity
GO:0016779 nucleotidyltransferase activity
GO:0046872 metal ion binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0006269 DNA replication, synthesis of RNA primer
Cellular Component
GO:1990077 primosome complex
Protein Structure and Domains
PDB ID MGI:97758
InterPro IPR007238 DNA primase large subunit, eukaryotic/archaeal
IPR016558 DNA primase, large subunit, eukaryotic
PFAM PF04104
PRINTS
PIRSF PIRSF009449
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt P33610
PhosphoSite PhosphoSite-P33610
TrEMBL
UniProt Splice Variant
Entrez Gene 19076
UniGene
RefSeq NP_032948
MGI ID
MGI Symbol Prim2
OMIM
CCDS CCDS14862
HPRD
IMGT
EMBL AK076095 AK077760 AK153970 BC019500 D13545 D17385
GenPept AAH19500 BAA02745 BAA04203 BAC36179 BAC36996 BAE32287

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca