MT-ND1

NADH dehydrogenase, subunit 1 (complex I)

Identifiers

ND1; MTND1

External IDs

OMIM: 516000 MGI: 101787 HomoloGene: 5011 GeneCards: ND1 Gene

Gene Ontology
Molecular function	• protein binding • NADH dehydrogenase (ubiquinone) activity • oxidoreductase activity
Cellular component	• mitochondrion • mitochondrial inner membrane • mitochondrial respiratory chain complex I • mitochondrial respiratory chain complex I • membrane • integral to membrane • mitochondrial membrane • respiratory chain
Biological process	• mitochondrial electron transport, NADH to ubiquinone • transport • response to stress • response to organic cyclic compound • respiratory electron transport chain • response to hydroperoxide • response to drug
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

n/a

RefSeq (protein)

Location (UCSC)

PubMed search

MT-ND1 is a mitochondrial gene. It is associated with mitochondrial encephalomyopathy, lactic acidosis, and stroke-like episodes.

Torroni A, Achilli A, Macaulay V, et al. (2006). "Harvesting the fruit of the human mtDNA tree.". Trends Genet. 22 (6): 339–45. doi:10.1016/j.tig.2006.04.001. PMID 16678300.
Bodenteich A, Mitchell LG, Polymeropoulos MH, Merril CR (1993). "Dinucleotide repeat in the human mitochondrial D-loop.". Hum. Mol. Genet. 1 (2): 140. doi:10.1093/hmg/1.2.140-a. PMID 1301157.
Lu X, Walker T, MacManus JP, Seligy VL (1992). "Differentiation of HT-29 human colonic adenocarcinoma cells correlates with increased expression of mitochondrial RNA: effects of trehalose on cell growth and maturation.". Cancer Res. 52 (13): 3718–25. PMID 1377597.
Johns DR, Neufeld MJ, Park RD (1992). "An ND-6 mitochondrial DNA mutation associated with Leber hereditary optic neuropathy.". Biochem. Biophys. Res. Commun. 187 (3): 1551–7. doi:10.1016/0006-291X(92)90479-5. PMID 1417830.
Huoponen K, Vilkki J, Aula P, et al. (1991). "A new mtDNA mutation associated with Leber hereditary optic neuroretinopathy". Am. J. Hum. Genet. 48 (6): 1147–53. PMC 1683111. PMID 1674640. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1683111.
Marzuki S, Noer AS, Lertrit P, et al. (1992). "Normal variants of human mitochondrial DNA and translation products: the building of a reference data base". Hum. Genet. 88 (2): 139–45. PMID 1757091.
Johns DR, Berman J (1991). "Alternative, simultaneous complex I mitochondrial DNA mutations in Leber's hereditary optic neuropathy". Biochem. Biophys. Res. Commun. 174 (3): 1324–30. doi:10.1016/0006-291X(91)91567-V. PMID 1900003.
Howell N, Bindoff LA, McCullough DA, et al. (1991). "Leber hereditary optic neuropathy: identification of the same mitochondrial ND1 mutation in six pedigrees". Am. J. Hum. Genet. 49 (5): 939–50. PMC 1683233. PMID 1928099. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1683233.
Majander A, Huoponen K, Savontaus ML, et al. (1992). "Electron transfer properties of NADH:ubiquinone reductase in the ND1/3460 and the ND4/11778 mutations of the Leber hereditary optic neuroretinopathy (LHON)". FEBS Lett. 292 (1–2): 289–92. doi:10.1016/0014-5793(91)80886-8. PMID 1959619.
Moraes CT, Andreetta F, Bonilla E, et al. (1991). "Replication-competent human mitochondrial DNA lacking the heavy-strand promoter region". Mol. Cell. Biol. 11 (3): 1631–7. PMC 369459. PMID 1996112. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=369459.
Howell N, Kubacka I, Xu M, McCullough DA (1991). "Leber hereditary optic neuropathy: involvement of the mitochondrial ND1 gene and evidence for an intragenic suppressor mutation". Am. J. Hum. Genet. 48 (5): 935–42. PMC 1683051. PMID 2018041. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1683051.
Attardi G, Chomyn A, Doolittle RF, et al. (1987). "Seven unidentified reading frames of human mitochondrial DNA encode subunits of the respiratory chain NADH dehydrogenase". Cold Spring Harb. Symp. Quant. Biol. 51 Pt 1: 103–14. PMID 3472707.
Chomyn A, Cleeter MW, Ragan CI, et al. (1986). "URF6, last unidentified reading frame of human mtDNA, codes for an NADH dehydrogenase subunit". Science 234 (4776): 614–8. doi:10.1126/science.3764430. PMID 3764430.
Chomyn A, Mariottini P, Cleeter MW, et al. (1985). "Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase". Nature 314 (6012): 592–7. doi:10.1038/314592a0. PMID 3921850.
Sanger F, Coulson AR, Barrell BG, et al. (1981). "Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing". J. Mol. Biol. 143 (2): 161–78. doi:10.1016/0022-2836(80)90196-5. PMID 6260957.
Pagani S, Galante YM (1983). "Interaction of rhodanese with mitochondrial NADH dehydrogenase". Biochim. Biophys. Acta 742 (2): 278–84. doi:10.1016/0167-4838(83)90312-6. PMID 6402020.
Anderson S, Bankier AT, Barrell BG, et al. (1981). "Sequence and organization of the human mitochondrial genome". Nature 290 (5806): 457–65. doi:10.1038/290457a0. PMID 7219534.
Montoya J, Ojala D, Attardi G (1981). "Distinctive features of the 5'-terminal sequences of the human mitochondrial mRNAs". Nature 290 (5806): 465–70. doi:10.1038/290465a0. PMID 7219535.
Horai S, Hayasaka K, Kondo R, et al. (1995). "Recent African origin of modern humans revealed by complete sequences of hominoid mitochondrial DNAs". Proc. Natl. Acad. Sci. U.S.A. 92 (2): 532–6. doi:10.1073/pnas.92.2.532. PMC 42775. PMID 7530363. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=42775.
Nakagawa Y, Ikegami H, Yamato E, et al. (1995). "A new mitochondrial DNA mutation associated with non-insulin-dependent diabetes mellitus". Biochem. Biophys. Res. Commun. 209 (2): 664–8. doi:10.1006/bbrc.1995.1550. PMID 7733935.

External links

GeneReviews/NCBI/NIH/UW entry on Mitochondrial DNA-Associated Leigh Syndrome and NARP

Mitochondrial proteins

Outer membrane	fatty acid degradation (Carnitine palmitoyltransferase I, Long fatty acyl CoA synthetase) tryptophan metabolism (Kynureninase) monoamine neurotransmitter metabolism (Monoamine oxidase)

Intermembrane space	Adenylate kinase - Creatine kinase

Inner membrane	oxidative phosphorylation (Coenzyme Q - cytochrome c reductase, Cytochrome c, NADH dehydrogenase, Succinate dehydrogenase) pyrimidine metabolism (Dihydroorotate dehydrogenase) mitochondrial shuttle (Malate-aspartate shuttle, Glycerol phosphate shuttle) other (Glutamate aspartate transporter, Glycerol-3-phosphate dehydrogenase, ATP synthase, Carnitine palmitoyltransferase II, Uncoupling protein)

Matrix	citric acid cycle (Citrate synthase, Aconitase, Isocitrate dehydrogenase, Oxoglutarate dehydrogenase, Succinyl coenzyme A synthetase, Fumarase, Malate dehydrogenase) anaplerotic reactions (Aspartate transaminase, Glutamate dehydrogenase, Pyruvate dehydrogenase complex) urea cycle (Carbamoyl phosphate synthetase I, Ornithine transcarbamylase, N-Acetylglutamate synthase) alcohol metabolism (ALDH2) PMPCB

Other/to be sorted	steroidogenesis (Cholesterol side-chain cleavage enzyme, Steroid 11-beta-hydroxylase, Aldosterone synthase), Frataxin Mitochondrial membrane transport protein (Mitochondrial permeability transition pore, Mitochondrial carrier)

Mitochondrial DNA	Complex I (MT-ND1, MT-ND2, MT-ND3, MT-ND4, MT-ND4L, MT-ND5, MT-ND6) - Complex III (MT-CYB) - Complex IV (MT-CO1, MT-CO2, MT-CO3) ATP synthase (MT-ATP6, MT-ATP8) tRNA (MT-TA, MT-TC, MT-TD, MT-TE, MT-TF, MT-TG, MT-TH, MT-TI, MT-TK, MT-TL1, MT-TL2, MT-TM, MT-TN, MT-TP, MT-TQ, MT-TR, MT-TS1, MT-TS2, MT-TT, MT-TV, MT-TW, MT-TY)

see also mitochondrial diseases B strc: edmb (perx), skel (ctrs), epit, cili, mito, nucl (chro)

MT-ND1

Further reading

External links