Version 5.4
Homo sapiens Gene: DNAJC7
Summary
InnateDB Gene IDBG-50158.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol DNAJC7
Gene Name DnaJ (Hsp40) homolog, subfamily C, member 7
Synonyms DJ11; DJC7; TPR2; TTC2
Species Homo sapiens
Ensembl Gene ENSG00000168259
Encoded Proteins
IDBP-50160
DnaJ (Hsp40) homolog, subfamily C, member 7
IDBP-378468
DnaJ (Hsp40) homolog, subfamily C, member 7
IDBP-378470
DnaJ (Hsp40) homolog, subfamily C, member 7
IDBP-763941
IDBP-760872
IDBP-759294
IDBP-763727
IDBP-763339
IDBP-763474
IDBP-760848
IDBP-757785
IDBP-761001
IDBP-758856
IDBP-759762
IDBP-764837
IDBP-761899
Protein Structure
Useful resources Stemformatics EHFPI ImmGen
Entrez Gene
Summary This gene encodes a member of the DNAJ heat shock protein 40 family of proteins that is characterized by two N-terminal tetratricopeptide repeat domains and a C-terminal DNAJ domain. This protein binds the chaperone proteins heat shock proteins 70 and 90 in an ATP-dependent manner and may function as a co-chaperone. Pseudogenes of this gene are found on chromosomes 1 and 6. Alternate splicing results in multiple transcript variants.[provided by RefSeq, Oct 2009]
Gene Information
Type Protein coding
Genomic Location Chromosome 17:41976433-42021376
Strand Reverse strand
Band q21.2
Transcripts
ENST00000316603 ENSP00000313311
ENST00000457167 ENSP00000406463
ENST00000426588 ENSP00000394327
ENST00000589547
ENST00000586335 ENSP00000464993
ENST00000586240
ENST00000590348 ENSP00000464756
ENST00000585693
ENST00000590847
ENST00000587380
ENST00000590774 ENSP00000465340
ENST00000589810 ENSP00000467477
ENST00000585866 ENSP00000466877
ENST00000589576 ENSP00000468102
ENST00000590197
ENST00000589773 ENSP00000465228
ENST00000588814 ENSP00000466114
ENST00000588641 ENSP00000468805
ENST00000591787 ENSP00000465140
ENST00000591153
ENST00000589586 ENSP00000466748
ENST00000590886 ENSP00000465399
ENST00000587727 ENSP00000467702
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 48 experimentally validated interaction(s) in this database.
They are also associated with 1 interaction(s) predicted by orthology.
Experimentally validated
Total 48 [view]
Protein-Protein 45 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 3 [view]
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 1 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0005515 protein binding
GO:0031072 heat shock protein binding
Biological Process
GO:0006457 protein folding
GO:0070389 chaperone cofactor-dependent protein refolding
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005856 cytoskeleton
GO:0016020 membrane
GO:0070062 extracellular vesicular exosome
Orthologs
Species
Mus musculus
Bos taurus
Gene ID
Gene Order
ENSMUSG00000014195
View Gene Order
ENSBTAG00000002654
Not yet available
Cross-References
SwissProt
TrEMBL K7ENB7
UniProt Splice Variant
Entrez Gene 7266
UniGene Hs.500156 Hs.663572 Hs.737592 Hs.739162 Hs.743841
RefSeq NM_001144766 NM_003315
HUGO HGNC:12392
OMIM 601964
CCDS CCDS45677 CCDS45678
HPRD
IMGT
EMBL AC105024 AC125257
GenPept
RNA Seq Atlas 102724375 7266

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