NDUFA10
| NDUFA10 | |||
|---|---|---|---|
| Identifiers | |||
Gene ontology | |||
| Molecular function | |||
| Cellular component | |||
| Biological process | |||
| Sources:Amigo / QuickGO | |||
Ensembl | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| UniProt | |||||||||
| RefSeq (mRNA) | |||||||||
| RefSeq (protein) | |||||||||
| Location (UCSC) | Chr 2: 239.89 – 240.03 Mb | Chr 1: 92.37 – 92.4 Mb | |||||||
| PubMed search | [3] | [4] | |||||||
| View/Edit Human | View/Edit Mouse |
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10 is an
squamous cell carcinoma and may be related to other forms of cancer.[9]
Structure
The NDUFA10 gene is located on the q arm of
secondary structure is primarily alpha helix, but the carboxy-terminal half of the protein has high potential to adopt a coiled-coil form. The amino-terminal part contains a putative beta sheet rich in hydrophobic amino acids that may serve as mitochondrial import signal.[5][8][13]
Function
The human NDUFA10 gene codes for a subunit of
isoalloxazine ring of the flavin mononucleotide (FMN) prosthetic arm to form FMNH2. The electrons are transferred through a series of iron-sulfur (Fe-S) clusters in the prosthetic arm and finally to coenzyme Q10 (CoQ), which is reduced to ubiquinol (CoQH2). The flow of electrons changes the redox state of the protein, resulting in a conformational change and pK shift of the ionizable side chain, which pumps four hydrogen ions out of the mitochondrial matrix.[7]
Clinical significance
NDUFA10 demonstrated significantly downregulated mRNA expression levels in human
tumor suppressor genes through promoter hypermethylation, among other mechanisms.[9] Mutations in NDUFA10 have also been associated with Leigh disease resulting from complex I deficiency.[14]
Interactions
NDUFA10 has been shown to have 56 binary protein-protein interactions including 55 co-complex interactions. NDUFA10 appears to interact with RAB8A.[15]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000130414 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026260 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ a b c d e "Entrez Gene: NDUFA10 NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, 10".
- PMID 9878551.
- ^ ISBN 978-0-470-54784-7.
- ^ S2CID 46818955.
- ^ PMID 22461910.
- PMID 23965338.
- ^ "NDUFA10 - NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB).
- ^ "NDUFA10 - NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10". UniProt.org. The UniProt Consortium.
- PMID 9425316.
- PMID 21150889.
- ^ "56 binary interactions found for search term NDUFA10". IntAct Molecular Interaction Database. EMBL-EBI. Retrieved 2018-08-25.
Further reading
- Smeitink J, van den Heuvel L (June 1999). "Human mitochondrial complex I in health and disease". American Journal of Human Genetics. 64 (6): 1505–10. PMID 10330338.
- Ma J, Dempsey AA, Stamatiou D, Marshall KW, Liew CC (March 2007). "Identifying leukocyte gene expression patterns associated with plasma lipid levels in human subjects". Atherosclerosis. 191 (1): 63–72. PMID 16806233.
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (May 2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology. 21 (5): 566–9. S2CID 23783563.
- Baens M, Chaffanet M, Aerssens J, Cassiman JJ, Marynen P (May 1994). "Assignment of the gene for the human proliferating cell nucleolar protein P120 (NOL1) to chromosome 12p13 by fluorescence in situ hybridization and polymerase chain reaction with somatic cell hybrids". Genomics. 21 (1): 296–7. PMID 8088812.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.