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NADH-ubiquinone oxidoreductase chain 2

NameNADH-ubiquinone oxidoreductase chain 2
Synonyms
  • 1.6.5.3
  • MTND2
  • NADH dehydrogenase subunit 2
  • NADH2
  • ND2
Gene NameMT-ND2
OrganismHuman
Amino acid sequence
>lcl|BSEQ0001306|NADH-ubiquinone oxidoreductase chain 2
MNPLAQPVIYSTIFAGTLITALSSHWFFTWVGLEMNMLAFIPVLTKKMNPRSTEAAIKYF
LTQATASMILLMAILFNNMLSGQWTMTNTTNQYSSLMIMMAMAMKLGMAPFHFWVPEVTQ
GTPLTSGLLLLTWQKLAPISIMYQISPSLNVSLLLTLSILSIMAGSWGGLNQTQLRKILA
YSSITHMGWMMAVLPYNPNMTILNLTIYIILTTTAFLLLNLNSSTTTLLLSRTWNKLTWL
TPLIPSTLLSLGGLPPLTGFLPKWAIIEEFTKNNSLIIPTIMATITLLNLYFYLRLIYST
SITLLPMSNNVKMKWQFEHTKPTPFLPTLIALTTLLLPISPFMLMIL
Number of residues347
Molecular Weight38960.47
Theoretical pI10.3
GO Classification
Functions
  • NADH dehydrogenase (ubiquinone) activity
Processes
  • cellular metabolic process
  • respiratory electron transport chain
  • mitochondrial electron transport, NADH to ubiquinone
  • reactive oxygen species metabolic process
  • small molecule metabolic process
Components
  • mitochondrial respiratory chain complex I
  • postsynaptic density
  • mitochondrial inner membrane
  • integral component of membrane
General FunctionNadh dehydrogenase (ubiquinone) activity
Specific FunctionCore 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).
Pfam Domain Function
Transmembrane Regions13-33 56-76 96-116 123-143 149-169 178-198 201-221 247-267 274-294 326-346
GenBank Protein ID2052363
UniProtKB IDP03891
UniProtKB Entry NameNU2M_HUMAN
Cellular LocationMitochondrion inner membrane
Gene sequence
>lcl|BSEQ0016165|NADH-ubiquinone oxidoreductase chain 2 (MT-ND2)
ATTAATCCCCTGGCCCAACCCGTCATCTACTCTACCATCTTTGCAGGCACACTCATCACA
GCGCTAAGCTCGCACTGATTTTTTACCTGAGTAGGCCTAGAAATAAACATGCTAGCTTTT
ATTCCAGTTCTAACCAAAAAAATAAACCCTCGTTCCACAGAAGCTGCCATCAAGTATTTC
CTCACGCAAGCAACCGCATCCATAATCCTTCTAATAGCTATCCTCTTCAACAATATACTC
TCCGGACAATGAACCATAACCAATACTACCAATCAATACTCATCATTAATAATCATAATA
GCTATAGCAATAAAACTAGGAATAGCCCCCTTTCACTTCTGAGTCCCAGAGGTTACCCAA
GGCACCCCTCTGACATCCGGCCTGCTTCTTCTCACATGACAAAAACTAGCCCCCATCTCA
ATCATATACCAAATCTCTCCCTCACTAAACGTAAGCCTTCTCCTCACTCTCTCAATCTTA
TCCATCATAGCAGGCAGTTGAGGTGGATTAAACCAAACCCAGCTACGCAAAATCTTAGCA
TACTCCTCAATTACCCACATAGGATGAATAATAGCAGTTCTACCGTACAACCCTAACATA
ACCATTCTTAATTTAACTATTTATATTATCCTAACTACTACCGCATTCCTACTACTCAAC
TTAAACTCCAGCACCACGACCCTACTACTATCTCGCACCTGAAACAAGCTAACATGACTA
ACACCCTTAATTCCATCCACCCTCCTCTCCCTAGGAGGCCTGCCCCCGCTAACCGGCTTT
TTGCCCAAATGGGCCATTATCGAAGAATTCACAAAAAACAATAGCCTCATCATCCCCACC
ATCATAGCCACCATCACCCTCCTTAACCTCTACTTCTACCTACGCCTAATCTACTCCACC
TCAATCACACTACTCCCCATATCTAACAACGTAAAAATAAAATGACAGTTTGAACATACA
AAACCCACCCCATTCCTCCCCACACTCATCGCCCTTACCACGCTACTCCTACCTATCTCC
CCTTTTATACTAATAATCTTAT
GenBank Gene IDJ01415
GeneCard IDNot Available
GenAtlas IDMT-ND2
HGNC IDHGNC:7456
Chromosome LocationNot Available
Locus-
References
  1. 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. 7219534
  2. 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. 6260957
  3. 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. 9475751
  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. 7530363
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  9. 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. 3921850
  10. 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. 12611891
  11. 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. 19690332
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  13. 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. 1900003
  14. 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. 1757091
  15. 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. 1732158
  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. 1370613
  17. 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. 9461455