My NCBISign In

Display Settings:

Format

Send to:

Choose Destination

    NDUFS1 NADH dehydrogenase (ubiquinone) Fe-S protein 1, 75kDa (NADH-coenzyme Q reductase) [ Homo sapiens ]

    Gene ID: 4719, updated on 20-May-2012
    Help top of page

    Summary

    Official Symbol
    NDUFS1provided by HGNC
    Official Full Name
    NADH dehydrogenase (ubiquinone) Fe-S protein 1, 75kDa (NADH-coenzyme Q reductase)provided by HGNC
    Primary source
    HGNC:7707
    See related
    Ensembl:ENSG00000023228; HPRD:01145; MIM:157655; Vega:OTTHUMG00000132892
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Homo sapiens
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
    Also known as
    CI-75k; CI-75Kd; PRO1304; MGC26839
    Summary
    The protein encoded by this gene belongs to the complex I 75 kDa subunit family. Mammalian complex I is composed of 45 different subunits. It locates at the mitochondrial inner membrane. This protein has NADH dehydrogenase activity and oxidoreductase activity. It transfers electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. This protein 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. Mutations in this gene are associated with complex I deficiency. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2011]
    Help top of page

    Genomic context

    Location :
    2q33-q34
    Sequence :
    Chromosome: 2; NC_000002.11 (206987803..207024243, complement)
    See NDUFS1 in Epigenomics, MapViewer

    Chromosome 2 - NC_000002.11Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC100507380 Neighboring gene glycine cleavage system protein H (aminomethyl carrier) pseudogene 3 Neighboring gene eukaryotic translation elongation factor 1 beta 2 Neighboring gene small nucleolar RNA, C/D box 51 Neighboring gene small nucleolar RNA, H/ACA box 41

    Help top of page

    Genomic regions, transcripts, and products

    Go to nucleotideGraphics FASTA GenBank

    Go to reference sequence details
    Helptop of page

    Bibliography

    Related articles in PubMed

    1. Proteomic analysis identifies dysfunction in cellular transport, energy, and protein metabolism in different brain regions of atypical frontotemporal lobar degeneration. Martins-de-Souza D, et al. J Proteome Res, 2012 Apr 6. PMID 22360420.
    2. Systematic and quantitative assessment of the ubiquitin-modified proteome. Kim W, et al. Mol Cell, 2011 Oct 21. PMID 21906983.
    3. Analysis of the mitochondrial complex I-V enzyme activities of peripheral leukocytes in oxidative phosphorylation disorders. Ma YY, et al. J Child Neurol, 2011 Aug. PMID 21540367.
    4. Purification and identification of endogenous polySUMO conjugates. Bruderer R, et al. EMBO Rep, 2011 Feb. PMID 21252943.
    5. Progressive cavitating leukoencephalopathy associated with respiratory chain complex I deficiency and a novel mutation in NDUFS1. Ferreira M, et al. Neurogenetics, 2011 Feb. PMID 21203893.

    See all (34) citations in PubMed

    See citations in PubMed for homologs of this gene provided by HomoloGene

    GeneRIFs: Gene References Into Functions What's a GeneRIF?

    1. The peripheral leukocyte oxidative phosphorylation enzyme activity assay was found to be a reliable method for the diagnosis of mitochondrial diseases.
      Title: Analysis of the mitochondrial complex I-V enzyme activities of peripheral leukocytes in oxidative phosphorylation disorders.
    2. A protein encoded by this locus was found to be differentially expressed in postmortem brains from patients with atypical frontotemporal lobar degeneration.
      Title: Proteomic analysis identifies dysfunction in cellular transport, energy, and protein metabolism in different brain regions of atypical frontotemporal lobar degeneration.
    3. homozygous c.1783A>G (p.Thr595Ala) mutation in NDUFS1 in two inbred siblings with isolated complex I deficiency associated to a progressive cavitating leukoencephalopathy
      Title: Progressive cavitating leukoencephalopathy associated with respiratory chain complex I deficiency and a novel mutation in NDUFS1.
    4. data suggest that gamma oscillations are especially energy demanding and require both high complex I expression and strong functional performance of mitochondria.
      Title: Gamma oscillations in the hippocampus require high complex I gene expression and strong functional performance of mitochondria.
    5. report 3 patients with low residual complex I activity who displayed novel mutations in the NDUFS1 gene. One mutation introduces a premature stop codon, 3 mutations cause a substitution of amino acids and another mutation a deletion of one amino acid.
      Title: Novel mutations in the NDUFS1 gene cause low residual activities in human complex I deficiencies.
    6. Mutations in electron Transport Complex I is associated with Leber hereditary optic neuropathy failing to compensate for impaired oxidative phosphorylation.
      Title: Patients with Leber hereditary optic neuropathy fail to compensate impaired oxidative phosphorylation.
    7. This protein has been found differentially expressed in the Wernicke's Area from patients with schizophrenia.
      Title: Proteome analysis of schizophrenia patients Wernicke's area reveals an energy metabolism dysregulation.
    8. Observational study of gene-disease association. (HuGE Navigator)
      Title: Genetic variants in nuclear-encoded mitochondrial genes influence AIDS progression.
    9. A patient with Leigh syndrome had a mutation in the NDUFS1 protein of Complex I of the Respiratory Chain. Identifying nuclear mutations will help us understand how molecular defects can lead to complex I deficiency.
      Title: Leigh syndrome associated with mitochondrial complex I deficiency due to a novel mutation in the NDUFS1 gene.
    10. mutations in the NDUFS1 and NDUFS4 genes of complex I cause dysfunction in cellular oxidative metabolism
      Title: Dysfunctions of cellular oxidative metabolism in patients with mutations in the NDUFS1 and NDUFS4 genes of complex I.
    Submit: New GeneRIF Correction
    Help top of page

    Phenotypes

    Find tests for this gene in the NIH Genetic Testing Registry (GTR)

    Review eQTL and phenotype association data in this region using PheGenI

    Mitochondrial complex I deficiency

    Help top of page

    Interactions

    Products Interactant Other Gene Complex Source Pubs Description
    NP_004997.4 NP_004337.2 CASP3    BIND  PubMed NDUFS1 interacts with caspase-3. This interaction was modeled on a demonstrated interaction between human NDUSF1 and caspase-3 from an unspecified source. 
    P28331 P40926 MDH2    HPRD  PubMed  
    BioGRID:110799 BioGRID:107286 CASP3    BioGRID  PubMed Biochemical Activity 
    BioGRID:110799 BioGRID:109622 ICT1    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:110799 BioGRID:110694 MYC    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:110799 BioGRID:112497 SUMO2    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:110799 BioGRID:112983 TNFAIP3    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:110799 BioGRID:113164 UBC    BioGRID  PubMed Affinity Capture-MS 
    Help top of page

    General gene information

    Markers

    Genotypes

    Homology

    • Homologs of the NDUFS1 gene: The NDUFS1 gene is conserved in chimpanzee, , dog, cow, mouse, rat, chicken, zebrafish, fruit fly, mosquito, C.elegans, , N.crassa, A.thaliana, and rice.
    • Map Viewer (Mouse, Rat)

    Pathways from BioSystems

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    2 iron, 2 sulfur cluster binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    4 iron, 4 sulfur cluster binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    contributes_to NADH dehydrogenase (ubiquinone) activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    NADH dehydrogenase (ubiquinone) activity NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    NADH dehydrogenase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    electron carrier activity NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    ATP metabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    ATP synthesis coupled electron transport IEA
    Inferred from Electronic Annotation
    more info
    		  
    apoptotic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    cellular respiration IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    mitochondrial electron transport, NADH to ubiquinone NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    reactive oxygen species metabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    regulation of mitochondrial membrane potential IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    respiratory electron transport chain TAS
    Traceable Author Statement
    more info
    		  
    small molecule metabolic process TAS
    Traceable Author Statement
    more info
    		  
    transport IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    mitochondrial inner membrane TAS
    Traceable Author Statement
    more info
    		  
    mitochondrial intermembrane space IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    mitochondrial respiratory chain complex I IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    mitochondrial respiratory chain complex I IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    mitochondrial respiratory chain complex I NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    mitochondrion IEA
    Inferred from Electronic Annotation
    more info
    		  
    respiratory chain IEA
    Inferred from Electronic Annotation
    more info
    		  
    Help top of page

    General protein information

    Preferred Names
    NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
    Names
    NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
    complex I 75kDa subunit
    complex I, mitochondrial respiratory chain, 75-kD subunit
    mitochondrial NADH-ubiquinone oxidoreductase 75 kDa subunit
    NP_001186910.1
    NP_001186911.1
    NP_001186912.1
    NP_001186913.1
    NP_004997.4
    Help top of page

    NCBI Reference Sequences (RefSeq)

    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    Genomic

    1. NG_009248.1 RefSeqGene

      Range
      4945..41385
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001199981.1 → NP_001186910.1  NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial isoform 2 precursor

      Status: REVIEWED

      Description
      Transcript Variant: This variant (2) lacks an alternate in-frame exon compared to variant 1. The resulting isoform (2) has the same N- and C-termini but is shorter compared to isoform 1.
      Source sequence(s)
      AA150435, AK295705, AW074155, BC018900, CA419316, DC413278
      Consensus CDS
      CCDS56164.1
      UniProtKB/TrEMBL
      B4DIN9
      UniProtKB/TrEMBL
      E7ENF3
      Related
      ENSP00000409766, OTTHUMP00000206342, ENST00000440274, OTTHUMT00000336448
      Conserved Domains (4) summary
      cd02773
      Location:213 – 594
      Blast Score: 1606
      MopB_Res-Cmplx1_Nad11; MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase ...
      PRK09130
      Location:31 – 687
      Blast Score: 2517
      PRK09130; NADH dehydrogenase subunit G; Validated
      pfam09326
      Location:621 – 674
      Blast Score: 155
      DUF1982; Domain of unknown function (DUF1982)
      cl11210
      Location:77 – 117
      Blast Score: 200
      NADH-G_4Fe-4S_3; NADH-ubiquinone oxidoreductase-G iron-sulfur binding region

    2. NM_001199982.1 → NP_001186911.1  NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial isoform 3

      Status: REVIEWED

      Description
      Transcript Variant: This variant (3) lacks an alternate coding segment compared to variant 1, that causes a frameshift. The resulting isoform (3) has a shorter and distinct N-terminus compared to isoform 1.
      Source sequence(s)
      AA150435, AK298320, AW074155, BC018900, CA419316, DC413278
      Consensus CDS
      CCDS56163.1
      Related
      ENSP00000409689, OTTHUMP00000206341, ENST00000432169, OTTHUMT00000336447
      Conserved Domains (4) summary
      cd02773
      Location:138 – 519
      Blast Score: 1606
      MopB_Res-Cmplx1_Nad11; MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase ...
      PTZ00305
      Location:3 – 120
      Blast Score: 284
      PTZ00305; NADH:ubiquinone oxidoreductase; Provisional
      pfam09326
      Location:546 – 599
      Blast Score: 155
      DUF1982; Domain of unknown function (DUF1982)
      cl11210
      Location:4 – 42
      Blast Score: 192
      NADH-G_4Fe-4S_3; NADH-ubiquinone oxidoreductase-G iron-sulfur binding region

    3. NM_001199983.1 → NP_001186912.1  NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial isoform 4

      Status: REVIEWED

      Description
      Transcript Variant: This variant (4) lacks an alternate coding exon compared to variant 1, that causes a frameshift. The resulting isoform (4) is shorter at the N-terminus compared to isoform 1.
      Source sequence(s)
      AA150435, AK300585, AW074155, BC018900, CA419316, DC413278
      Consensus CDS
      CCDS56162.1
      Related
      ENSP00000397760, OTTHUMP00000206344, ENST00000423725, OTTHUMT00000336450
      Conserved Domains (5) summary
      cd02773
      Location:192 – 573
      Blast Score: 1612
      MopB_Res-Cmplx1_Nad11; MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase ...
      PRK09130
      Location:2 – 666
      Blast Score: 2685
      PRK09130; NADH dehydrogenase subunit G; Validated
      pfam09326
      Location:600 – 653
      Blast Score: 155
      DUF1982; Domain of unknown function (DUF1982)
      cl00159
      Location:3 – 50
      Blast Score: 102
      fer2; 2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis ...
      cl11210
      Location:56 – 96
      Blast Score: 197
      NADH-G_4Fe-4S_3; NADH-ubiquinone oxidoreductase-G iron-sulfur binding region

    4. NM_001199984.1 → NP_001186913.1  NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial isoform 5

      Status: REVIEWED

      Description
      Transcript Variant: This variant (5) differs in the 5' UTR and coding sequence compared to variant 1. The resulting isoform (5) has a longer and distinct N-terminus compared to isoform 1.
      Source sequence(s)
      AA150435, AK295987, AW074155, BC018900, CA419316
      Consensus CDS
      CCDS56165.1
      UniProtKB/Swiss-Prot
      P28331
      Related
      ENSP00000392709, ENST00000455934
      Conserved Domains (5) summary
      cd00207
      Location:46 – 116
      Blast Score: 125
      fer2; 2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis ...
      cd02773
      Location:263 – 644
      Blast Score: 1613
      MopB_Res-Cmplx1_Nad11; MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase ...
      PRK09130
      Location:45 – 737
      Blast Score: 2780
      PRK09130; NADH dehydrogenase subunit G; Validated
      pfam09326
      Location:671 – 724
      Blast Score: 155
      DUF1982; Domain of unknown function (DUF1982)
      cl11210
      Location:127 – 167
      Blast Score: 198
      NADH-G_4Fe-4S_3; NADH-ubiquinone oxidoreductase-G iron-sulfur binding region

    5. NM_005006.6 → NP_004997.4  NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial isoform 1

      Status: REVIEWED

      Description
      Transcript Variant: This variant (1) represents the longest and predominant transcript. Variant 1 encodes isoform 1.
      Source sequence(s)
      AA150435, AW074155, BC018900, CA419316, DC413278
      Consensus CDS
      CCDS2366.1
      UniProtKB/TrEMBL
      E5KRK5
      UniProtKB/Swiss-Prot
      P28331
      Related
      ENSP00000233190, OTTHUMP00000163806, ENST00000233190, OTTHUMT00000256391
      Conserved Domains (5) summary
      cd00207
      Location:32 – 102
      Blast Score: 124
      fer2; 2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis ...
      cd02773
      Location:249 – 630
      Blast Score: 1613
      MopB_Res-Cmplx1_Nad11; MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase ...
      PRK09130
      Location:31 – 723
      Blast Score: 2779
      PRK09130; NADH dehydrogenase subunit G; Validated
      pfam09326
      Location:657 – 710
      Blast Score: 155
      DUF1982; Domain of unknown function (DUF1982)
      cl11210
      Location:113 – 153
      Blast Score: 198
      NADH-G_4Fe-4S_3; NADH-ubiquinone oxidoreductase-G iron-sulfur binding region

    RefSeqs of Annotated Genomes: Build 37.3

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference GRCh37.p5 Primary Assembly

    Genomic

    1. NC_000002.11 Reference GRCh37.p5 Primary Assembly

      Range
      206987803..207024243, complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    Alternate HuRef

    Genomic

    1. AC_000134.1 Alternate HuRef

      Range
      198836332..198872823, complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)
    Help top of page

    Related Sequences

    Nucleotide Protein
    Heading Accession and Version
    genomic AC007383.4 AAY15061.1
    genomic CH471063.1 EAW70379.1
      EAW70380.1
    genomic HQ205706.1 ADP91534.1
    genomic HQ205707.1 ADP91535.1
    genomic HQ205708.1 ADP91536.1
    genomic HQ205709.1 ADP91537.1
    genomic HQ205710.1 ADP91538.1
    genomic HQ205711.1 ADP91539.1
    genomic HQ205712.1 ADP91540.1
    genomic HQ205713.1 ADP91541.1
    genomic HQ205714.1 ADP91542.1
    genomic HQ205715.1 ADP91543.1
    genomic HQ205716.1 ADP91544.1
    genomic HQ205717.1 ADP91545.1
    genomic HQ205718.1 ADP91546.1
    genomic HQ205719.1 ADP91547.1
    genomic HQ205720.1 ADP91548.1
    genomic HQ205721.1 ADP91549.1
    genomic HQ205722.1 ADP91550.1
    genomic HQ205723.1 ADP91551.1
    genomic HQ205724.1 ADP91552.1
    genomic HQ205725.1 ADP91553.1
    genomic HQ205726.1 ADP91554.1
    genomic HQ205727.1 ADP91555.1
    genomic HQ205728.1 ADP91556.1
    genomic HQ205729.1 ADP91557.1
    genomic HQ205730.1 ADP91558.1
    genomic HQ205731.1 ADP91559.1
    genomic HQ205732.1 ADP91560.1
    genomic HQ205733.1 ADP91561.1
    genomic HQ205734.1 ADP91562.1
    genomic HQ205735.1 ADP91563.1
    genomic HQ205736.1 ADP91564.1
    genomic HQ205737.1 ADP91565.1
    genomic HQ205738.1 ADP91566.1
    genomic HQ205739.1 ADP91567.1
    genomic HQ205740.1 ADP91568.1
    genomic HQ205741.1 ADP91569.1
    genomic HQ205742.1 ADP91570.1
    genomic HQ205743.1 ADP91571.1
    genomic HQ205744.1 ADP91572.1
    genomic HQ205745.1 ADP91573.1
    mRNA AA150435.1 None
    mRNA AK098395.1 None
    mRNA AK295705.1 BAG58551.1
    mRNA AK295966.1 BAG58743.1
    mRNA AK295987.1 BAG58762.1
    mRNA AK298320.1 BAG60573.1
    mRNA AK300585.1 BAG62283.1
    mRNA AW074155.1 None
    mRNA BC004133.2 None
    mRNA BC012068.1 AAH12068.1
    mRNA BC018900.1 None
    mRNA BC022368.1 AAH22368.1
    mRNA BC030833.1 AAH30833.1
    mRNA BQ882763.1 None
    mRNA CA419316.1 None
    mRNA DC413278.1 None
    mRNA X61100.1 CAA43412.1
    Protein Accession Links
    GenPept Link UniProtKB Link
    P28331.3 GenPept UniProtKB/Swiss-Prot:P28331
    Q9P1A0 GenPept UniProtKB/TrEMBL:Q9P1A0
    Help top of page

    Additional Links

    Additional Links

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

    Chemical Information
    Medical
    Molecular Biology Databases
    Research Materials
    Tools
    Miscellaneous

      Supplemental Content

      Table of contents

      Links

      Links to other resources

      General information

      Related sites

      Feedback

      Subscription

      Recent activity

      Clear Turn Off Turn On

      Your browsing activity is empty.

      Activity recording is turned off.

      Turn recording back on

      See more...