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O00217

- NDUS8_HUMAN

UniProt

O00217 - NDUS8_HUMAN

Protein

NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial

Gene

NDUFS8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      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. May donate electrons to ubiquinone.By similarity

    Catalytic activityi

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

    Cofactori

    Binds 2 4Fe-4S clusters per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi111 – 1111Iron-sulfur 1 (4Fe-4S)By similarity
    Metal bindingi114 – 1141Iron-sulfur 1 (4Fe-4S)By similarity
    Metal bindingi117 – 1171Iron-sulfur 1 (4Fe-4S)By similarity
    Metal bindingi121 – 1211Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi150 – 1501Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi153 – 1531Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi156 – 1561Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi160 – 1601Iron-sulfur 1 (4Fe-4S)By similarity

    GO - Molecular functioni

    1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. NADH dehydrogenase (ubiquinone) activity Source: UniProtKB

    GO - Biological processi

    1. cellular metabolic process Source: Reactome
    2. mitochondrial electron transport, NADH to ubiquinone Source: UniProtKB
    3. mitochondrial respiratory chain complex I assembly Source: UniProtKB
    4. respiratory electron transport chain Source: Reactome
    5. response to oxidative stress Source: UniProtKB
    6. 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 8, mitochondrial (EC:1.6.5.3, EC:1.6.99.3)
    Alternative name(s):
    Complex I-23kD
    Short name:
    CI-23kD
    NADH-ubiquinone oxidoreductase 23 kDa subunit
    TYKY subunit
    Gene namesi
    Name:NDUFS8
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:7715. NDUFS8.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Leigh syndrome (LS) [MIM:256000]: An early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti79 – 791P → L in LS. 1 Publication
    Corresponds to variant rs28939679 [ dbSNP | Ensembl ].
    VAR_019538
    Natural varianti102 – 1021R → H in LS. 1 Publication
    VAR_019539

    Keywords - Diseasei

    Disease mutation, Leigh syndrome

    Organism-specific databases

    MIMi256000. phenotype.
    Orphaneti2609. Isolated NADH-CoQ reductase deficiency.
    255241. Leigh syndrome with leukodystrophy.
    PharmGKBiPA31525.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3434MitochondrionBy similarityAdd
    BLAST
    Chaini35 – 210176NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrialPRO_0000020012Add
    BLAST

    Proteomic databases

    MaxQBiO00217.
    PaxDbiO00217.
    PeptideAtlasiO00217.
    PRIDEiO00217.

    2D gel databases

    OGPiO00217.

    PTM databases

    PhosphoSiteiO00217.

    Expressioni

    Gene expression databases

    ArrayExpressiO00217.
    BgeeiO00217.
    CleanExiHS_NDUFS8.
    GenevestigatoriO00217.

    Organism-specific databases

    HPAiHPA018524.

    Interactioni

    Subunit structurei

    Mammalian complex I is composed of 45 different subunits.1 Publication

    Protein-protein interaction databases

    BioGridi110806. 28 interactions.
    IntActiO00217. 5 interactions.
    MINTiMINT-2997478.
    STRINGi9606.ENSP00000315774.

    Structurei

    3D structure databases

    ProteinModelPortaliO00217.
    SMRiO00217. Positions 84-189.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini102 – 131304Fe-4S ferredoxin-type 1Add
    BLAST
    Domaini141 – 170304Fe-4S ferredoxin-type 2Add
    BLAST

    Sequence similaritiesi

    Belongs to the complex I 23 kDa subunit family.Curated
    Contains 2 4Fe-4S ferredoxin-type domains.Curated

    Keywords - Domaini

    Repeat, Transit peptide

    Phylogenomic databases

    eggNOGiCOG1143.
    HOGENOMiHOG000228289.
    HOVERGENiHBG006547.
    InParanoidiO00217.
    KOiK03941.
    OMAiTYKYVNL.
    OrthoDBiEOG7J9VQT.
    PhylomeDBiO00217.
    TreeFamiTF105610.

    Family and domain databases

    HAMAPiMF_01351. NDH1_NuoI.
    InterProiIPR001450. 4Fe4S-bd_dom.
    IPR017896. 4Fe4S_Fe-S-bd.
    IPR017900. 4Fe4S_Fe_S_CS.
    IPR010226. NADH_quinone_OxRdtase_chainI.
    [Graphical view]
    PfamiPF12838. Fer4_7. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01971. NuoI. 1 hit.
    PROSITEiPS00198. 4FE4S_FER_1. 2 hits.
    PS51379. 4FE4S_FER_2. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O00217-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRCLTTPMLL RALAQAARAG PPGGRSLHSS AVAATYKYVN MQDPEMDMKS    50
    VTDRAARTLL WTELFRGLGM TLSYLFREPA TINYPFEKGP LSPRFRGEHA 100
    LRRYPSGEER CIACKLCEAI CPAQAITIEA EPRADGSRRT TRYDIDMTKC 150
    IYCGFCQEAC PVDAIVEGPN FEFSTETHEE LLYNKEKLLN NGDKWEAEIA 200
    ANIQADYLYR 210
    Length:210
    Mass (Da):23,705
    Last modified:July 1, 1997 - v1
    Checksum:i8C3EBD205BFA0112
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti79 – 791P → L in LS. 1 Publication
    Corresponds to variant rs28939679 [ dbSNP | Ensembl ].
    VAR_019538
    Natural varianti102 – 1021R → H in LS. 1 Publication
    VAR_019539

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U65579 mRNA. Translation: AAB51776.1.
    AF038406 Genomic DNA. Translation: AAC34273.1.
    AK314546 mRNA. Translation: BAG37133.1.
    BC119754 mRNA. Translation: AAI19755.1.
    CCDSiCCDS8176.1.
    RefSeqiNP_002487.1. NM_002496.3.
    XP_005274070.1. XM_005274013.1.
    XP_005274071.1. XM_005274014.1.
    UniGeneiHs.90443.

    Genome annotation databases

    EnsembliENST00000313468; ENSP00000315774; ENSG00000110717.
    GeneIDi4728.
    KEGGihsa:4728.
    UCSCiuc001onc.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U65579 mRNA. Translation: AAB51776.1 .
    AF038406 Genomic DNA. Translation: AAC34273.1 .
    AK314546 mRNA. Translation: BAG37133.1 .
    BC119754 mRNA. Translation: AAI19755.1 .
    CCDSi CCDS8176.1.
    RefSeqi NP_002487.1. NM_002496.3.
    XP_005274070.1. XM_005274013.1.
    XP_005274071.1. XM_005274014.1.
    UniGenei Hs.90443.

    3D structure databases

    ProteinModelPortali O00217.
    SMRi O00217. Positions 84-189.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110806. 28 interactions.
    IntActi O00217. 5 interactions.
    MINTi MINT-2997478.
    STRINGi 9606.ENSP00000315774.

    Chemistry

    BindingDBi O00217.
    ChEMBLi CHEMBL2363065.
    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei O00217.

    2D gel databases

    OGPi O00217.

    Proteomic databases

    MaxQBi O00217.
    PaxDbi O00217.
    PeptideAtlasi O00217.
    PRIDEi O00217.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000313468 ; ENSP00000315774 ; ENSG00000110717 .
    GeneIDi 4728.
    KEGGi hsa:4728.
    UCSCi uc001onc.3. human.

    Organism-specific databases

    CTDi 4728.
    GeneCardsi GC11P067798.
    HGNCi HGNC:7715. NDUFS8.
    HPAi HPA018524.
    MIMi 256000. phenotype.
    602141. gene.
    neXtProti NX_O00217.
    Orphaneti 2609. Isolated NADH-CoQ reductase deficiency.
    255241. Leigh syndrome with leukodystrophy.
    PharmGKBi PA31525.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1143.
    HOGENOMi HOG000228289.
    HOVERGENi HBG006547.
    InParanoidi O00217.
    KOi K03941.
    OMAi TYKYVNL.
    OrthoDBi EOG7J9VQT.
    PhylomeDBi O00217.
    TreeFami TF105610.

    Enzyme and pathway databases

    Reactomei REACT_22393. Respiratory electron transport.

    Miscellaneous databases

    GeneWikii NDUFS8.
    GenomeRNAii 4728.
    NextBioi 18230.
    PROi O00217.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00217.
    Bgeei O00217.
    CleanExi HS_NDUFS8.
    Genevestigatori O00217.

    Family and domain databases

    HAMAPi MF_01351. NDH1_NuoI.
    InterProi IPR001450. 4Fe4S-bd_dom.
    IPR017896. 4Fe4S_Fe-S-bd.
    IPR017900. 4Fe4S_Fe_S_CS.
    IPR010226. NADH_quinone_OxRdtase_chainI.
    [Graphical view ]
    Pfami PF12838. Fer4_7. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01971. NuoI. 1 hit.
    PROSITEi PS00198. 4FE4S_FER_1. 2 hits.
    PS51379. 4FE4S_FER_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA sequence and chromosomal localization of the NDUFS8 human gene coding for the 23 kDa subunit of the mitochondrial complex I."
      Procaccio V., Depetris D., Soularue P., Mattei M.-G., Lunardi J., Issartel J.-P.
      Biochim. Biophys. Acta 1351:37-41(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. "Genomic structure of the human NDUFS8 gene coding for the iron-sulfur TYKY subunit of the mitochondrial NADH:ubiquinone oxidoreductase."
      de Sury R., Martinez P., Procaccio V., Lunardi J., Issartel J.-P.
      Gene 215:1-10(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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].
      Tissue: Uterus.
    4. "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].
    5. "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.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. Cited for: VARIANTS LS LEU-79 AND HIS-102.

    Entry informationi

    Entry nameiNDUS8_HUMAN
    AccessioniPrimary (citable) accession number: O00217
    Secondary accession number(s): B2RB86, Q0VDA8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 143 of the entry and version 1 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 11
      Human chromosome 11: 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