Hmdb loader
You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Human Metabolome Database.
Identification
HMDB Protein ID HMDBP00162
Secondary Accession Numbers
  • 5394
  • HMDBP03472
Name NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
Synonyms
  1. CI-75kD
  2. Complex I-75kD
Gene Name NDUFS1
Protein Type Unknown
Biological Properties
General Function Involved in electron carrier 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). This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized.
Pathways
  • Alzheimer disease
  • Huntington disease
  • Oxidative phosphorylation
  • Parkinson disease
Reactions
NADH + Coenzyme Q10 → NAD + QH(2) details
NADH + acceptor → NAD + reduced acceptor details
GO Classification
Biological Process
mitochondrial electron transport, NADH to ubiquinone
apoptotic process
reactive oxygen species metabolic process
regulation of mitochondrial membrane potential
ATP metabolic process
Cellular Component
mitochondrial respiratory chain complex I
mitochondrial intermembrane space
Component
membrane
cell part
Function
binding
catalytic activity
nadh dehydrogenase activity
electron carrier activity
nadh dehydrogenase (quinone) activity
nadh dehydrogenase (ubiquinone) activity
metal cluster binding
iron-sulfur cluster binding
oxidoreductase activity
oxidoreductase activity, acting on nadh or nadph
Molecular Function
electron carrier activity
metal ion binding
2 iron, 2 sulfur cluster binding
4 iron, 4 sulfur cluster binding
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
oxidation reduction
Cellular Location
  1. Mitochondrion inner membrane
Gene Properties
Chromosome Location 2
Locus 2q33-q34
SNPs NDUFS1
Gene Sequence
>2184 bp
ATGTTAAGGATACCTGTAAGAAGGGCCTTAGTAGGCCTTTCTAAGTCTCCTAAAGGATGT
GTTCGAACAACTGCCACAGCAGCAAGCAACTTGATTGAAGTATTTGTTGATGGTCAGTCT
GTCATGGTGGAACCGGGAACGACCGTCCTCCAAGCTTGTGAGAAGGTTGGCATGCAGATC
CCTCGATTCTGTTATCATGAAAGGTTGTCTGTTGCTGGAAACTGCAGGATGTGCCTTGTT
GAAATTGAGAAAGCCCCTAAGGTTGTAGCTGCTTGTGCCATGCCAGTAATGAAGGGTTGG
AATATCCTAACAAACTCAGAAAAATCCAAAAAGGCCAGGGAAGGTGTGATGGAGTTCTTA
TTAGCAAATCACCCATTGGACTGTCCTATTTGTGACCAGGGAGGTGAATGTGATCTGCAG
GACCAGTCCATGATGTTTGGAAATGATAGGAGCCGATTTTTAGAGGGGAAGCGTGCTGTG
GAAGACAAGAACATTGGGCCATTGGTAAAGACCATCATGACAAGATGTATACAGTGTACT
CGCTGCATCAGGTTTGCAAGTGAGATTGCAGGAGTAGATGATTTGGGAACAACAGGCAGA
GGAAATGATATGCAAGTTGGCACATACATTGAAAAGATGTTCATGTCTGAACTGTCTGGG
AATATCATTGATATCTGCCCTGTAGGTGCCCTAACCTCTAAGCCCTATGCCTTTACTGCC
CGGCCTTGGGAAACAAGAAAGACAGAATCCATTGATGTAATGGATGCGGTTGGAAGTAAT
ATTGTGGTTAGCACAAGAACTGGAGAAGTGATGAGGATTTTGCCACGTATGCATGAGGAC
ATCAATGAAGAGTGGATCTCTGATAAAACCAGATTTGCCTATGATGGGCTAAAACGTCAA
AGACTTACCGAGCCAATGGTCAGAAATGAAAAAGGGCTTTTAACCTATACTTCTTGGGAG
GATGCTCTCTCTCGCGTAGCTGGAATGTTGCAGAGTTTTCAAGGCAAAGATGTGGCAGCA
ATTGCAGGTGGCTTGGTGGATGCTGAAGCCCTGGTAGCTCTCAAAGATTTGCTTAATAGA
GTGGACTCTGACACCTTATGCACTGAAGAGGTCTTCCCCACTGCAGGAGCTGGCACAGAT
TTGCGTTCCAATTATCTTCTTAATACTACAATTGCTGGTGTGGAAGAGGCAGATGTTGTT
CTTCTGGTTGGTACAAACCCACGTTTTGAGGCACCACTGTTTAATGCATGGATTCGAAAG
AGCTGGCTGCATAATGACTTAAAAGTGGCCCTTATAGGCAGTCCAGTGGACCTCACTTAC
ACATATGACCACCTGGGAGACTCCCCCAAAATTCTTCAAGACATTGCTTCGGGAAGCCAT
CCATTTAGCCAGGTCCTAAAGGAAGCTAAAAAACCAATGGTGGTTTTAGGCAGTTCTGCA
CTCCAAAGAAATGATGGAGCAGCAATTCTTGCAGCTGTTTCTAGCATTGCACAAAAGATT
CGGATGACTAGTGGTGTTACTGGTGATTGGAAAGTTATGAATATCCTTCATAGGATTGCA
AGTCAAGTAGCTGCTTTGGACCTTGGCTATAAGCCTGGGGTGGAAGCAATTCGGAAGAAC
CCTCCCAAGGTGCTGTTTCTCCTGGGAGCAGATGGAGGTTGTATCACACGACAGGATTTG
CCAAAGGATTGTTTCATTATTTATCAAGGACATCATGGTGATGTTGGGGCTCCCATAGCT
GATGTTATTCTCCCAGGAGCTGCTTACACAGAGAAGTCTGCTACATATGTCAACACTGAG
GGTAGAGCTCAGCAGACTAAGGTAGCAGTGACACCTCCTGGCTTGGCAAGAGAAGACTGG
AAAATTATAAGAGCACTCTCTGAGATTGCTGGAATGACTCTTCCATATGATACTCTGGAT
CAAGTAAGGAACAGATTGGAAGAATTCTCTCCTAATCTTGTTCGATATGATGATATTGAA
GGGGCTAATTACTTCCAGCAAGCAAATGAGCTCTCAAAGCTAGTGAACCAGCAGCTTCTT
GCTGACCCACTTGTTCCACCTCAGCTAACTCTAAAAGACTTCTACATGACAGATTCGATT
AGCAGAGCCTCACAGACAATGGCCAAATGTGTCAAAGCTGTCACAGAGGGTGCCCAGGCA
GTAGAGGAACCATCCATATGCTGA
Protein Properties
Number of Residues 727
Molecular Weight 67523.595
Theoretical pI 5.325
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
MLRIPVRKALVGLSKSPKGCVRTTATAASNLIEVFVDGQSVMVEPGTTVLQACEKVGMQI
PRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSEKSKKAREGVMEFL
LANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCT
RCIRFASEIAGVDDLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTA
RPWETRKTESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLKRQ
RLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSFQGKDVAAIAGGLVDAEALVALKDLLNR
VDSDTLCTEEVFPTAGAGTDLRSNYLLNTTIAGVEEADVVLLVGTNPRFEAPLFNARIRK
SWLHNDLKVALIGSPVDLTYTYDHLGDSPKILQDIASGSHPFSQVLKEAKKPMVVLGSSA
LQRNDGAAILAAVSSIAQKIRMTSGVTGDWKVMNILHRIASQVAALDLGYKPGVEAIRKN
PPKVLFLLGADGGCITRQDLPKDCFIIYQGHHGDVGAPIADVILPGAAYTEKSATYVNTE
GRAQQTKVAVTPPGLAREDWKIIRALSEIAGMTLPYDTLDQVRNRLEEVSPNLVRYDDIE
GANYFQQANELSKLVNQQLLADPLVPPQLTIKDFYMTDSISRASQTMAKCVKAVTEGAQA
VEEPSIC
GenBank ID Protein 38079
UniProtKB/Swiss-Prot ID P28331
UniProtKB/Swiss-Prot Entry Name NDUS1_HUMAN
PDB IDs Not Available
GenBank Gene ID X61100
GeneCard ID NDUFS1
GenAtlas ID NDUFS1
HGNC ID HGNC:7707
References
General References
  1. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed:15815621 ]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  3. 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 ]
  4. Chow W, Ragan I, Robinson BH: Determination of the cDNA sequence for the human mitochondrial 75-kDa Fe-S protein of NADH-coenzyme Q reductase. Eur J Biochem. 1991 Nov 1;201(3):547-50. [PubMed:1935949 ]
  5. Benit P, Chretien D, Kadhom N, de Lonlay-Debeney P, Cormier-Daire V, Cabral A, Peudenier S, Rustin P, Munnich A, Rotig A: Large-scale deletion and point mutations of the nuclear NDUFV1 and NDUFS1 genes in mitochondrial complex I deficiency. Am J Hum Genet. 2001 Jun;68(6):1344-52. Epub 2001 May 7. [PubMed:11349233 ]