Version 5.4
Mus musculus Protein: Ccdc62
Summary
InnateDB Protein IDBP-200118.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Ccdc62
Protein Name coiled-coil domain containing 62
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000091878
InnateDB Gene IDBG-200116 (Ccdc62)
Protein Structure
UniProt Annotation
Function Nuclear receptor coactivator that can enhance preferentially estrogen receptors ESR1 and ESR2 transactivation. Modulates also progesterone/PGR, glucocorticoid/NR3C1 and androgen/AR receptors transactivation, although at lower level; little effect on vitamin D receptor/VDR (By similarity). {ECO:0000250}.
Subcellular Localization Cytoplasm {ECO:0000250}. Nucleus. Note=Mainly nuclear. {ECO:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
Biological Process
GO:0008150 biological_process
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005886 plasma membrane
Protein Structure and Domains
PDB ID MGI:2684996
InterPro IPR009053 Prefoldin
PFAM
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt E9PVD1
PhosphoSite PhosphoSite-E9PVD1
TrEMBL
UniProt Splice Variant
Entrez Gene 208908
UniGene Mm.412587
RefSeq XP_006530319
MGI ID
MGI Symbol Ccdc62
OMIM
CCDS CCDS51646
HPRD
IMGT
EMBL AC122753
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