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O75306

- NDUS2_HUMAN

UniProt

O75306 - NDUS2_HUMAN

Protein

NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial

Gene

NDUFS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (16 Apr 2002)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

    NADH + ubiquinone + 5 H+(In) = NAD+ + ubiquinol + 4 H+(Out).
    NADH + acceptor = NAD+ + reduced acceptor.

    Cofactori

    Binds 1 4Fe-4S cluster.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi326 – 3261Iron-sulfur (4Fe-4S)Sequence Analysis
    Metal bindingi332 – 3321Iron-sulfur (4Fe-4S)Sequence Analysis
    Metal bindingi347 – 3471Iron-sulfur (4Fe-4S)Sequence Analysis

    GO - Molecular functioni

    1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
    2. electron carrier activity Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. NAD binding Source: InterPro
    5. NADH dehydrogenase (ubiquinone) activity Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. quinone binding Source: InterPro

    GO - Biological processi

    1. cellular metabolic process Source: Reactome
    2. mitochondrial electron transport, NADH to ubiquinone Source: UniProtKB
    3. respiratory electron transport chain Source: Reactome
    4. response to oxidative stress Source: UniProtKB
    5. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Respiratory chain, Transport

    Keywords - Ligandi

    4Fe-4S, Iron, Iron-sulfur, Metal-binding, NAD, Ubiquinone

    Enzyme and pathway databases

    ReactomeiREACT_22393. Respiratory electron transport.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial (EC:1.6.5.3, EC:1.6.99.3)
    Alternative name(s):
    Complex I-49kD
    Short name:
    CI-49kD
    NADH-ubiquinone oxidoreductase 49 kDa subunit
    Gene namesi
    Name:NDUFS2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:7708. NDUFS2.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: Reactome
    2. mitochondrial respiratory chain complex I Source: UniProtKB
    3. mitochondrion Source: UniProtKB
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Involvement in diseasei

    Mitochondrial complex I deficiency (MT-C1D) [MIM:252010]: A disorder of the mitochondrial respiratory chain that causes a wide range of clinical manifestations from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti228 – 2281R → Q in MT-C1D. 1 Publication
    VAR_019535
    Natural varianti229 – 2291P → Q in MT-C1D. 1 Publication
    VAR_019536
    Natural varianti413 – 4131S → P in MT-C1D. 1 Publication
    VAR_019537

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi252010. phenotype.
    Orphaneti2609. Isolated NADH-CoQ reductase deficiency.
    PharmGKBiPA31519.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3333MitochondrionBy similarityAdd
    BLAST
    Chaini34 – 463430NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrialPRO_0000019981Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei62 – 621N6-acetyllysineBy similarity
    Modified residuei118 – 1181Symmetric dimethylarginineBy similarity

    Keywords - PTMi

    Acetylation, Methylation

    Proteomic databases

    MaxQBiO75306.
    PaxDbiO75306.
    PeptideAtlasiO75306.
    PRIDEiO75306.

    PTM databases

    PhosphoSiteiO75306.

    Expressioni

    Gene expression databases

    ArrayExpressiO75306.
    BgeeiO75306.
    CleanExiHS_NDUFS2.
    GenevestigatoriO75306.

    Organism-specific databases

    HPAiHPA055140.

    Interactioni

    Subunit structurei

    Complex I is composed of 45 different subunits. Component of the iron-sulfur (IP) fragment of the enzyme. Interacts with NDUFAF3 and NDUFAF7.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NDUFS3O754895EBI-1224806,EBI-1224896

    Protein-protein interaction databases

    BioGridi110800. 27 interactions.
    IntActiO75306. 16 interactions.
    STRINGi9606.ENSP00000356972.

    Structurei

    3D structure databases

    ProteinModelPortaliO75306.
    SMRiO75306. Positions 80-463.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the complex I 49 kDa subunit family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0649.
    HOGENOMiHOG000228264.
    HOVERGENiHBG000760.
    InParanoidiO75306.
    KOiK03935.
    OMAiQCFALAV.
    OrthoDBiEOG7WT411.
    PhylomeDBiO75306.
    TreeFamiTF300370.

    Family and domain databases

    Gene3Di1.10.645.10. 1 hit.
    HAMAPiMF_01358. NDH1_NuoD.
    InterProiIPR001135. NADH_Q_OxRdtase_suD.
    IPR014029. NADH_UbQ_OxRdtase_49kDa_CS.
    IPR022885. NDH1_su_D/H.
    IPR029014. NiFe_Hase-like.
    [Graphical view]
    PfamiPF00346. Complex1_49kDa. 1 hit.
    [Graphical view]
    SUPFAMiSSF56762. SSF56762. 1 hit.
    TIGRFAMsiTIGR01962. NuoD. 1 hit.
    PROSITEiPS00535. COMPLEX1_49K. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75306-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAALRALCGF RGVAAQVLRP GAGVRLPIQP SRGVRQWQPD VEWAQQFGGA    50
    VMYPSKETAH WKPPPWNDVD PPKDTIVKNI TLNFGPQHPA AHGVLRLVME 100
    LSGEMVRKCD PHIGLLHRGT EKLIEYKTYL QALPYFDRLD YVSMMCNEQA 150
    YSLAVEKLLN IRPPPRAQWI RVLFGEITRL LNHIMAVTTH ALDLGAMTPF 200
    FWLFEEREKM FEFYERVSGA RMHAAYIRPG GVHQDLPLGL MDDIYQFSKN 250
    FSLRLDELEE LLTNNRIWRN RTIDIGVVTA EEALNYGFSG VMLRGSGIQW 300
    DLRKTQPYDV YDQVEFDVPV GSRGDCYDRY LCRVEEMRQS LRIIAQCLNK 350
    MPPGEIKVDD AKVSPPKRAE MKTSMESLIH HFKLYTEGYQ VPPGATYTAI 400
    EAPKGEFGVY LVSDGSSRPY RCKIKAPGFA HLAGLDKMSK GHMLADVVAI 450
    IGTQDIVFGE VDR 463
    Length:463
    Mass (Da):52,546
    Last modified:April 16, 2002 - v2
    Checksum:iA2BF56F008B6312C
    GO
    Isoform 2 (identifier: O75306-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         454-463: QDIVFGEVDR → RPIV

    Note: No experimental confirmation available.

    Show »
    Length:457
    Mass (Da):51,852
    Checksum:i312C97A91028FF66
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti24 – 241V → G in AAC34362. (PubMed:9585441)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti20 – 201P → T.
    Corresponds to variant rs11538340 [ dbSNP | Ensembl ].
    VAR_034150
    Natural varianti228 – 2281R → Q in MT-C1D. 1 Publication
    VAR_019535
    Natural varianti229 – 2291P → A.
    Corresponds to variant rs16827493 [ dbSNP | Ensembl ].
    VAR_034151
    Natural varianti229 – 2291P → Q in MT-C1D. 1 Publication
    VAR_019536
    Natural varianti352 – 3521P → A.
    Corresponds to variant rs11576415 [ dbSNP | Ensembl ].
    VAR_034152
    Natural varianti413 – 4131S → P in MT-C1D. 1 Publication
    VAR_019537

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei454 – 46310QDIVFGEVDR → RPIV in isoform 2. CuratedVSP_046466

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF050640 mRNA. Translation: AAC27453.1.
    AF013160 mRNA. Translation: AAC34362.1.
    AK314807 mRNA. No translation available.
    AL590714 Genomic DNA. Translation: CAH72148.1.
    CH471121 Genomic DNA. Translation: EAW52625.1.
    CH471121 Genomic DNA. Translation: EAW52626.1.
    BC000170 mRNA. Translation: AAH00170.1.
    BC001456 mRNA. Translation: AAH01456.1.
    BC008868 mRNA. Translation: AAH08868.1.
    CCDSiCCDS1224.1. [O75306-1]
    CCDS53404.1. [O75306-2]
    PIRiJE0193.
    RefSeqiNP_001159631.1. NM_001166159.1. [O75306-2]
    NP_004541.1. NM_004550.4. [O75306-1]
    XP_005245265.1. XM_005245208.1. [O75306-1]
    UniGeneiHs.173611.

    Genome annotation databases

    EnsembliENST00000367993; ENSP00000356972; ENSG00000158864. [O75306-1]
    ENST00000392179; ENSP00000376018; ENSG00000158864. [O75306-2]
    GeneIDi4720.
    KEGGihsa:4720.
    UCSCiuc001fyv.3. human. [O75306-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF050640 mRNA. Translation: AAC27453.1 .
    AF013160 mRNA. Translation: AAC34362.1 .
    AK314807 mRNA. No translation available.
    AL590714 Genomic DNA. Translation: CAH72148.1 .
    CH471121 Genomic DNA. Translation: EAW52625.1 .
    CH471121 Genomic DNA. Translation: EAW52626.1 .
    BC000170 mRNA. Translation: AAH00170.1 .
    BC001456 mRNA. Translation: AAH01456.1 .
    BC008868 mRNA. Translation: AAH08868.1 .
    CCDSi CCDS1224.1. [O75306-1 ]
    CCDS53404.1. [O75306-2 ]
    PIRi JE0193.
    RefSeqi NP_001159631.1. NM_001166159.1. [O75306-2 ]
    NP_004541.1. NM_004550.4. [O75306-1 ]
    XP_005245265.1. XM_005245208.1. [O75306-1 ]
    UniGenei Hs.173611.

    3D structure databases

    ProteinModelPortali O75306.
    SMRi O75306. Positions 80-463.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110800. 27 interactions.
    IntActi O75306. 16 interactions.
    STRINGi 9606.ENSP00000356972.

    Chemistry

    BindingDBi O75306.
    ChEMBLi CHEMBL2363065.
    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei O75306.

    Proteomic databases

    MaxQBi O75306.
    PaxDbi O75306.
    PeptideAtlasi O75306.
    PRIDEi O75306.

    Protocols and materials databases

    DNASUi 4720.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367993 ; ENSP00000356972 ; ENSG00000158864 . [O75306-1 ]
    ENST00000392179 ; ENSP00000376018 ; ENSG00000158864 . [O75306-2 ]
    GeneIDi 4720.
    KEGGi hsa:4720.
    UCSCi uc001fyv.3. human. [O75306-1 ]

    Organism-specific databases

    CTDi 4720.
    GeneCardsi GC01P161166.
    HGNCi HGNC:7708. NDUFS2.
    HPAi HPA055140.
    MIMi 252010. phenotype.
    602985. gene.
    neXtProti NX_O75306.
    Orphaneti 2609. Isolated NADH-CoQ reductase deficiency.
    PharmGKBi PA31519.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0649.
    HOGENOMi HOG000228264.
    HOVERGENi HBG000760.
    InParanoidi O75306.
    KOi K03935.
    OMAi QCFALAV.
    OrthoDBi EOG7WT411.
    PhylomeDBi O75306.
    TreeFami TF300370.

    Enzyme and pathway databases

    Reactomei REACT_22393. Respiratory electron transport.

    Miscellaneous databases

    ChiTaRSi NDUFS2. human.
    GeneWikii NDUFS2.
    GenomeRNAii 4720.
    NextBioi 18206.
    PROi O75306.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75306.
    Bgeei O75306.
    CleanExi HS_NDUFS2.
    Genevestigatori O75306.

    Family and domain databases

    Gene3Di 1.10.645.10. 1 hit.
    HAMAPi MF_01358. NDH1_NuoD.
    InterProi IPR001135. NADH_Q_OxRdtase_suD.
    IPR014029. NADH_UbQ_OxRdtase_49kDa_CS.
    IPR022885. NDH1_su_D/H.
    IPR029014. NiFe_Hase-like.
    [Graphical view ]
    Pfami PF00346. Complex1_49kDa. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56762. SSF56762. 1 hit.
    TIGRFAMsi TIGR01962. NuoD. 1 hit.
    PROSITEi PS00535. COMPLEX1_49K. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA sequence and chromosomal localization of the remaining three human nuclear encoded iron sulphur protein (IP) subunits of complex I: the human IP fraction is completed."
      Loeffen J., van den Heuvel L., Smeets R., Triepels R., Sengers R., Trijbels F., Smeitink J.
      Biochem. Biophys. Res. Commun. 247:751-758(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Mapping to 1q23 of the human gene (NDUFS2) encoding the 49-kDa subunit of the mitochondrial respiratory complex I and immunodetection of the mature protein in mitochondria."
      Procaccio V., de Sury R., Martinez P., Depetris D., Rabilloud T., Soularue P., Lunardi J., Issartel J.-P.
      Mamm. Genome 9:482-484(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Muscle and Placenta.
    7. "The subunit composition of the human NADH dehydrogenase obtained by rapid one-step immunopurification."
      Murray J., Zhang B., Taylor S.W., Oglesbee D., Fahy E., Marusich M.F., Ghosh S.S., Capaldi R.A.
      J. Biol. Chem. 278:13619-13622(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    8. "Mutations in NDUFAF3 (C3ORF60), encoding an NDUFAF4 (C6ORF66)-interacting complex I assembly protein, cause fatal neonatal mitochondrial disease."
      Saada A., Vogel R.O., Hoefs S.J., van den Brand M.A., Wessels H.J., Willems P.H., Venselaar H., Shaag A., Barghuti F., Reish O., Shohat M., Huynen M.A., Smeitink J.A.M., van den Heuvel L.P., Nijtmans L.G.
      Am. J. Hum. Genet. 84:718-727(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NDUFAF3.
    9. Cited for: INTERACTION WITH NDUFAF7.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Mutations in the complex I NDUFS2 gene of patients with cardiomyopathy and encephalomyopathy."
      Loeffen J., Elpeleg O., Smeitink J., Smeets R., Stoeckler-Ipsiroglu S., Mandel H., Sengers R., Trijbels F., van den Heuvel L.
      Ann. Neurol. 49:195-201(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MT-C1D GLN-228; GLN-229 AND PRO-413.

    Entry informationi

    Entry nameiNDUS2_HUMAN
    AccessioniPrimary (citable) accession number: O75306
    Secondary accession number(s): D3DVG7
    , J3KPM7, Q5VTW0, Q969P3, Q9UEV3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: April 16, 2002
    Last modified: October 1, 2014
    This is version 150 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3