Version 5.4
Mus musculus Protein: Hsph1
Summary
InnateDB Protein IDBP-539194.3
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Hsph1
Protein Name heat shock 105kDa/110kDa protein 1
Synonyms 105kDa; AI790491; hsp-E7I; Hsp105; Hsp110;
Species Mus musculus
Ensembl Protein ENSMUSP00000116818
InnateDB Gene IDBG-209442 (Hsph1)
Protein Structure
UniProt Annotation
Function
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 20 experimentally validated interaction(s) in this database.
They are also associated with 28 interaction(s) predicted by orthology.
Experimentally validated
Total 20 [view]
Protein-Protein 20 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 28 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0005515 protein binding
Biological Process
GO:0000902 cell morphogenesis
GO:0051085 chaperone mediated protein folding requiring cofactor
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
Protein Structure and Domains
PDB ID MGI:105053
InterPro IPR004753 Cell shape determining protein MreB/Mrl
IPR013126 Heat shock protein 70 family
PFAM PF06723
PF00012
PRINTS PR01652
PR00301
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt
PhosphoSite PhosphoSite-
TrEMBL D3Z3I9
UniProt Splice Variant
Entrez Gene 15505
UniGene Mm.489443
RefSeq
MGI ID
MGI Symbol Hsph1
OMIM
CCDS
HPRD
IMGT
EMBL AC119856
GenPept

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