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Identification
HMDB Protein ID HMDBP00154
Secondary Accession Numbers
  • 5386
  • HMDBP03480
Name NADH-ubiquinone oxidoreductase chain 2
Synonyms
  1. NADH dehydrogenase subunit 2
Gene Name MT-ND2
Protein Type Unknown
Biological Properties
General Function Involved in NADH dehydrogenase (ubiquinone) activity
Specific Function Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Pathways
  • Oxidative phosphorylation
  • Parkinson's disease
Reactions
NADH + Coenzyme Q10 → NAD + QH(2) details
QH2 + Acceptor → Ubiquinone-2 + Reduced acceptor details
GO Classification
Biological Process
small molecule metabolic process
mitochondrial electron transport, NADH to ubiquinone
Cellular Component
mitochondrial respiratory chain complex I
integral to membrane
Function
catalytic activity
nadh dehydrogenase activity
nadh dehydrogenase (quinone) activity
nadh dehydrogenase (ubiquinone) activity
oxidoreductase activity
oxidoreductase activity, acting on nadh or nadph
Molecular Function
NADH dehydrogenase (ubiquinone) activity
Process
metabolic process
generation of precursor metabolites and energy
electron transport chain
respiratory electron transport chain
atp synthesis coupled electron transport
cellular metabolic process
mitochondrial electron transport, nadh to ubiquinone
oxidation reduction
Cellular Location
  1. Mitochondrion inner membrane
  2. Multi-pass membrane protein
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs MT-ND2
Gene Sequence
>1042 bp
ATTAATCCCCTGGCCCAACCCGTCATCTACTCTACCATCTTTGCAGGCACACTCATCACA
GCGCTAAGCTCGCACTGATTTTTTACCTGAGTAGGCCTAGAAATAAACATGCTAGCTTTT
ATTCCAGTTCTAACCAAAAAAATAAACCCTCGTTCCACAGAAGCTGCCATCAAGTATTTC
CTCACGCAAGCAACCGCATCCATAATCCTTCTAATAGCTATCCTCTTCAACAATATACTC
TCCGGACAATGAACCATAACCAATACTACCAATCAATACTCATCATTAATAATCATAATA
GCTATAGCAATAAAACTAGGAATAGCCCCCTTTCACTTCTGAGTCCCAGAGGTTACCCAA
GGCACCCCTCTGACATCCGGCCTGCTTCTTCTCACATGACAAAAACTAGCCCCCATCTCA
ATCATATACCAAATCTCTCCCTCACTAAACGTAAGCCTTCTCCTCACTCTCTCAATCTTA
TCCATCATAGCAGGCAGTTGAGGTGGATTAAACCAAACCCAGCTACGCAAAATCTTAGCA
TACTCCTCAATTACCCACATAGGATGAATAATAGCAGTTCTACCGTACAACCCTAACATA
ACCATTCTTAATTTAACTATTTATATTATCCTAACTACTACCGCATTCCTACTACTCAAC
TTAAACTCCAGCACCACGACCCTACTACTATCTCGCACCTGAAACAAGCTAACATGACTA
ACACCCTTAATTCCATCCACCCTCCTCTCCCTAGGAGGCCTGCCCCCGCTAACCGGCTTT
TTGCCCAAATGGGCCATTATCGAAGAATTCACAAAAAACAATAGCCTCATCATCCCCACC
ATCATAGCCACCATCACCCTCCTTAACCTCTACTTCTACCTACGCCTAATCTACTCCACC
TCAATCACACTACTCCCCATATCTAACAACGTAAAAATAAAATGACAGTTTGAACATACA
AAACCCACCCCATTCCTCCCCACACTCATCGCCCTTACCACGCTACTCCTACCTATCTCC
CCTTTTATACTAATAATCTTAT
Protein Properties
Number of Residues 347
Molecular Weight 38960.47
Theoretical pI 9.839
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>NADH-ubiquinone oxidoreductase chain 2
MNPLAQPVIYSTIFAGTLITALSSHWFFTWVGLEMNMLAFIPVLTKKMNPRSTEAAIKYF
LTQATASMILLMAILFNNMLSGQWTMTNTTNQYSSLMIMMAMAMKLGMAPFHFWVPEVTQ
GTPLTSGLLLLTWQKLAPISIMYQISPSLNVSLLLTLSILSIMAGSWGGLNQTQLRKILA
YSSITHMGWMMAVLPYNPNMTILNLTIYIILTTTAFLLLNLNSSTTTLLLSRTWNKLTWL
TPLIPSTLLSLGGLPPLTGFLPKWAIIEEFTKNNSLIIPTIMATITLLNLYFYLRLIYST
SITLLPMSNNVKMKWQFEHTKPTPFLPTLIALTTLLLPISPFMLMIL
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P03891
UniProtKB/Swiss-Prot Entry Name NU2M_HUMAN
PDB IDs Not Available
GenBank Gene ID J01415
GeneCard ID MT-ND2
GenAtlas ID MT-ND2
HGNC ID HGNC:7456
References
General References
  1. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  2. Murray J, Zhang B, Taylor SW, Oglesbee D, Fahy E, Marusich MF, Ghosh SS, Capaldi RA: The subunit composition of the human NADH dehydrogenase obtained by rapid one-step immunopurification. J Biol Chem. 2003 Apr 18;278(16):13619-22. Epub 2003 Feb 28. [PubMed:12611891 ]
  3. Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, Schreier PH, Smith AJ, Staden R, Young IG: Sequence and organization of the human mitochondrial genome. Nature. 1981 Apr 9;290(5806):457-65. [PubMed:7219534 ]
  4. Horai S, Hayasaka K, Kondo R, Tsugane K, Takahata N: Recent African origin of modern humans revealed by complete sequences of hominoid mitochondrial DNAs. Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):532-6. [PubMed:7530363 ]
  5. Moilanen JS, Finnila S, Majamaa K: Lineage-specific selection in human mtDNA: lack of polymorphisms in a segment of MTND5 gene in haplogroup J. Mol Biol Evol. 2003 Dec;20(12):2132-42. Epub 2003 Aug 29. [PubMed:12949126 ]
  6. Ingman M, Kaessmann H, Paabo S, Gyllensten U: Mitochondrial genome variation and the origin of modern humans. Nature. 2000 Dec 7;408(6813):708-13. [PubMed:11130070 ]
  7. Ingman M, Gyllensten U: Mitochondrial genome variation and evolutionary history of Australian and New Guinean aborigines. Genome Res. 2003 Jul;13(7):1600-6. [PubMed:12840039 ]
  8. Coble MD, Just RS, O'Callaghan JE, Letmanyi IH, Peterson CT, Irwin JA, Parsons TJ: Single nucleotide polymorphisms over the entire mtDNA genome that increase the power of forensic testing in Caucasians. Int J Legal Med. 2004 Jun;118(3):137-46. Epub 2004 Feb 4. [PubMed:14760490 ]
  9. Sanger F, Coulson AR, Barrell BG, Smith AJ, Roe BA: Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing. J Mol Biol. 1980 Oct 25;143(2):161-78. [PubMed:6260957 ]
  10. Chomyn A, Mariottini P, Cleeter MW, Ragan CI, Matsuno-Yagi A, Hatefi Y, Doolittle RF, Attardi G: Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase. Nature. 1985 Apr 18-24;314(6012):592-7. [PubMed:3921850 ]
  11. Johns DR, Berman J: Alternative, simultaneous complex I mitochondrial DNA mutations in Leber's hereditary optic neuropathy. Biochem Biophys Res Commun. 1991 Feb 14;174(3):1324-30. [PubMed:1900003 ]
  12. Marzuki S, Noer AS, Lertrit P, Thyagarajan D, Kapsa R, Utthanaphol P, Byrne E: Normal variants of human mitochondrial DNA and translation products: the building of a reference data base. Hum Genet. 1991 Dec;88(2):139-45. [PubMed:1757091 ]
  13. Brown MD, Voljavec AS, Lott MT, Torroni A, Yang CC, Wallace DC: Mitochondrial DNA complex I and III mutations associated with Leber's hereditary optic neuropathy. Genetics. 1992 Jan;130(1):163-73. [PubMed:1732158 ]
  14. Rieder MJ, Taylor SL, Tobe VO, Nickerson DA: Automating the identification of DNA variations using quality-based fluorescence re-sequencing: analysis of the human mitochondrial genome. Nucleic Acids Res. 1998 Feb 15;26(4):967-73. [PubMed:9461455 ]
  15. Wise CA, Sraml M, Easteal S: Departure from neutrality at the mitochondrial NADH dehydrogenase subunit 2 gene in humans, but not in chimpanzees. Genetics. 1998 Jan;148(1):409-21. [PubMed:9475751 ]
  16. Lin FH, Lin R, Wisniewski HM, Hwang YW, Grundke-Iqbal I, Healy-Louie G, Iqbal K: Detection of point mutations in codon 331 of mitochondrial NADH dehydrogenase subunit 2 in Alzheimer's brains. Biochem Biophys Res Commun. 1992 Jan 15;182(1):238-46. [PubMed:1370613 ]