Version 5.4
Mus musculus Protein: Gins1
Summary
InnateDB Protein IDBP-209424.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Gins1
Protein Name GINS complex subunit 1 (Psf1 homolog)
Synonyms 2810418N01Rik; Gins4; mKIAA0186; PSF1;
Species Mus musculus
Ensembl Protein ENSMUSP00000028948
InnateDB Gene IDBG-209422 (Gins1)
Protein Structure
UniProt Annotation
Function The GINS complex plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS complex seems to bind preferentially to single- stranded DNA. GINS1 is essential for function (By similarity). {ECO:0000250}.
Subcellular Localization Nucleus {ECO:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 1 experimentally validated interaction(s) in this database.
They are also associated with 6 interaction(s) predicted by orthology.
Experimentally validated
Total 1 [view]
Protein-Protein 1 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 6 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0005515 protein binding
Biological Process
GO:0001833 inner cell mass cell proliferation
GO:0006260 DNA replication
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
Protein Structure and Domains
PDB ID MGI:1916520
InterPro
PFAM
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9CZ15
PhosphoSite PhosphoSite-Q9CZ15
TrEMBL
UniProt Splice Variant
Entrez Gene 69270
UniGene Mm.271603
RefSeq NP_081290
MGI ID
MGI Symbol Gins1
OMIM
CCDS CCDS50743
HPRD
IMGT
EMBL AK013116
GenPept BAB28658

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