Version 5.4
Homo sapiens Protein: LIPT2
Summary
InnateDB Protein IDBP-64323.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol LIPT2
Protein Name lipoyl(octanoyl) transferase 2 (putative)
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000309463
InnateDB Gene IDBG-64321 (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: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:0009107 lipoate biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
Protein Structure and Domains
PDB ID
InterPro IPR000544 Octanoyltransferase
IPR004143 Biotin/lipoate A/B protein ligase
PFAM PF03099
PRINTS
PIRSF PIRSF016262
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt A6NK58
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 387787
UniGene Hs.604608
RefSeq NP_001138341
HUGO HGNC:37216
OMIM
CCDS CCDS44679
HPRD
IMGT
EMBL AP001372
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