Version 5.4
Mus musculus Protein: Isca2
Summary
InnateDB Protein IDBP-157123.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Isca2
Protein Name iron-sulfur cluster assembly 2 homolog (S. cerevisiae)
Synonyms 0710001C05Rik; 5730594E03Rik; Hbld1;
Species Mus musculus
Ensembl Protein ENSMUSP00000021667
InnateDB Gene IDBG-157121 (Isca2)
Protein Structure
UniProt Annotation
Function Involved in the maturation of mitochondrial 4Fe-4S proteins functioning late in the iron-sulfur cluster assembly pathway. May be involved in the binding of an intermediate of Fe/S cluster assembly (By similarity). {ECO:0000250}.
Subcellular Localization Mitochondrion {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
GO:0005198 structural molecule activity
GO:0046872 metal ion binding
GO:0051536 iron-sulfur cluster binding
Biological Process
GO:0008150 biological_process
GO:0016226 iron-sulfur cluster assembly
Cellular Component
GO:0005739 mitochondrion
Protein Structure and Domains
PDB ID MGI:1921566
InterPro IPR000361 FeS cluster biogenesis
IPR016092 FeS cluster insertion protein
PFAM PF01521
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9DCB8
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 74316
UniGene Mm.405096
RefSeq NP_083139
MGI ID
MGI Symbol Isca2
OMIM
CCDS CCDS49111
HPRD
IMGT
EMBL AK002936
GenPept BAB22467

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