Version 5.4
Mus musculus Protein: Lipt2
Summary
InnateDB Protein IDBP-201048.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Lipt2
Protein Name lipoyl(octanoyl) transferase 2 (putative)
Synonyms 2610209A20Rik;
Species Mus musculus
Ensembl Protein ENSMUSP00000032967
InnateDB Gene IDBG-201046 (Lipt2)
Protein Structure
UniProt Annotation
Function Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity). {ECO:0000250}.
Subcellular Localization Mitochondrion {ECO:0000305}.
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:0003824 catalytic activity
GO:0005515 protein binding
GO:0016415 octanoyltransferase activity
GO:0016874 ligase activity
GO:0033819 lipoyl(octanoyl) transferase activity
Biological Process
GO:0006464 cellular protein modification process
GO:0008150 biological_process
GO:0009107 lipoate biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
Protein Structure and Domains
PDB ID MGI:1914414
InterPro IPR000544 Octanoyltransferase
IPR004143 Biotin/lipoate A/B protein ligase
PFAM PF03099
PRINTS
PIRSF PIRSF016262
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9D009
PhosphoSite PhosphoSite-Q9D009
TrEMBL
UniProt Splice Variant
Entrez Gene 67164
UniGene Mm.46777
RefSeq NP_080286
MGI ID
MGI Symbol Lipt2
OMIM
CCDS CCDS21494
HPRD
IMGT
EMBL AK008917 AK011925 BC115472 BC115473
GenPept AAI15473 AAI15474 BAB25967 BAB27920

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) 

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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