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O43920

- NDUS5_HUMAN

UniProt

O43920 - NDUS5_HUMAN

Protein

NADH dehydrogenase [ubiquinone] iron-sulfur protein 5

Gene

NDUFS5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in 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.

    GO - Molecular functioni

    1. 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. small molecule metabolic process Source: Reactome

    Keywords - Biological processi

    Electron transport, Respiratory chain, Transport

    Enzyme and pathway databases

    ReactomeiREACT_22393. Respiratory electron transport.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADH dehydrogenase [ubiquinone] iron-sulfur protein 5
    Alternative name(s):
    Complex I-15 kDa
    Short name:
    CI-15 kDa
    NADH-ubiquinone oxidoreductase 15 kDa subunit
    Gene namesi
    Name:NDUFS5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:7712. NDUFS5.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: Reactome
    2. mitochondrial intermembrane space Source: UniProtKB-SubCell
    3. mitochondrial respiratory chain complex I Source: UniProtKB
    4. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31522.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 106105NADH dehydrogenase [ubiquinone] iron-sulfur protein 5PRO_0000118786Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi33 ↔ 66Sequence Analysis
    Disulfide bondi43 ↔ 56Sequence Analysis

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiO43920.
    PaxDbiO43920.
    PeptideAtlasiO43920.
    PRIDEiO43920.

    PTM databases

    PhosphoSiteiO43920.

    Expressioni

    Gene expression databases

    ArrayExpressiO43920.
    BgeeiO43920.
    CleanExiHS_NDUFS5.
    GenevestigatoriO43920.

    Organism-specific databases

    HPAiHPA042582.

    Interactioni

    Subunit structurei

    Mammalian complex I is composed of 45 different subunits. This is a component of the iron-sulfur (IP) fragment of the enzyme.1 Publication

    Protein-protein interaction databases

    BioGridi110804. 2 interactions.
    IntActiO43920. 4 interactions.
    MINTiMINT-2796423.
    STRINGi9606.ENSP00000362058.

    Structurei

    3D structure databases

    ProteinModelPortaliO43920.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi33 – 4311C-X9-C motif 1Add
    BLAST
    Motifi56 – 6611C-X9-C motif 2Add
    BLAST

    Domaini

    Contains two C-X9-C motifs that are predicted to form a helix-coil-helix structure, permitting the formation of intramolecular disulfide bonds.1 Publication

    Sequence similaritiesi

    Belongs to the complex I NDUFS5 subunit family.Curated

    Phylogenomic databases

    eggNOGiNOG313534.
    HOGENOMiHOG000264236.
    HOVERGENiHBG001646.
    InParanoidiO43920.
    KOiK03938.
    OMAiLRQKTMK.
    OrthoDBiEOG7C8GKB.
    PhylomeDBiO43920.
    TreeFamiTF332111.

    Family and domain databases

    InterProiIPR019342. NADH_UbQ_OxRdtase_FeS-su5.
    [Graphical view]
    PfamiPF10200. Ndufs5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O43920-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPFLDIQKRF GLNIDRWLTI QSGEQPYKMA GRCHAFEKEW IECAHGIGYT    50
    RAEKECKIEY DDFVECLLRQ KTMRRAGTIR KQRDKLIKEG KYTPPPHHIG 100
    KGEPRP 106
    Length:106
    Mass (Da):12,518
    Last modified:January 23, 2007 - v3
    Checksum:i3D55402837DD99EE
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti96 – 961P → S Detected in a patient with mitochondrial complex I deficiency; uncertain pathological significance. 1 Publication
    VAR_064569

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF047434 mRNA. Translation: AAC39878.1.
    AF020352 mRNA. Translation: AAB87866.1.
    BC001884 mRNA. Translation: AAH01884.1.
    CCDSiCCDS434.1.
    RefSeqiNP_001171908.1. NM_001184979.1.
    NP_004543.1. NM_004552.2.
    UniGeneiHs.632385.

    Genome annotation databases

    EnsembliENST00000372967; ENSP00000362058; ENSG00000168653.
    ENST00000372969; ENSP00000362060; ENSG00000168653.
    GeneIDi4725.
    KEGGihsa:4725.
    UCSCiuc001ccx.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF047434 mRNA. Translation: AAC39878.1 .
    AF020352 mRNA. Translation: AAB87866.1 .
    BC001884 mRNA. Translation: AAH01884.1 .
    CCDSi CCDS434.1.
    RefSeqi NP_001171908.1. NM_001184979.1.
    NP_004543.1. NM_004552.2.
    UniGenei Hs.632385.

    3D structure databases

    ProteinModelPortali O43920.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110804. 2 interactions.
    IntActi O43920. 4 interactions.
    MINTi MINT-2796423.
    STRINGi 9606.ENSP00000362058.

    Chemistry

    ChEMBLi CHEMBL2363065.
    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei O43920.

    Proteomic databases

    MaxQBi O43920.
    PaxDbi O43920.
    PeptideAtlasi O43920.
    PRIDEi O43920.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000372967 ; ENSP00000362058 ; ENSG00000168653 .
    ENST00000372969 ; ENSP00000362060 ; ENSG00000168653 .
    GeneIDi 4725.
    KEGGi hsa:4725.
    UCSCi uc001ccx.3. human.

    Organism-specific databases

    CTDi 4725.
    GeneCardsi GC01P039491.
    HGNCi HGNC:7712. NDUFS5.
    HPAi HPA042582.
    MIMi 603847. gene.
    neXtProti NX_O43920.
    PharmGKBi PA31522.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG313534.
    HOGENOMi HOG000264236.
    HOVERGENi HBG001646.
    InParanoidi O43920.
    KOi K03938.
    OMAi LRQKTMK.
    OrthoDBi EOG7C8GKB.
    PhylomeDBi O43920.
    TreeFami TF332111.

    Enzyme and pathway databases

    Reactomei REACT_22393. Respiratory electron transport.

    Miscellaneous databases

    ChiTaRSi NDUFS5. human.
    GeneWikii NDUFS5.
    GenomeRNAii 4725.
    NextBioi 18222.
    PROi O43920.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43920.
    Bgeei O43920.
    CleanExi HS_NDUFS5.
    Genevestigatori O43920.

    Family and domain databases

    InterProi IPR019342. NADH_UbQ_OxRdtase_FeS-su5.
    [Graphical view ]
    Pfami PF10200. Ndufs5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning."
      Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z.
      Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Umbilical cord blood.
    2. "The human NADH:ubiquinone oxidoreductase NDUFS5 (15 kDa) subunit: cDNA cloning, chromosomal localization, tissue distribution and the absence of mutations in isolated complex I-deficient patients."
      Loeffen J., Smeets R., Smeitink J., Triepels R., Sengers R., Trijbels F., van den Heuvel L.
      J. Inherit. Metab. Dis. 22:19-28(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "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: Kidney.
    4. "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.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "NDUFB7 and NDUFA8 are located at the intermembrane surface of complex I."
      Szklarczyk R., Wanschers B.F., Nabuurs S.B., Nouws J., Nijtmans L.G., Huynen M.A.
      FEBS Lett. 585:737-743(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN, MOTIF.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: VARIANT SER-96.

    Entry informationi

    Entry nameiNDUS5_HUMAN
    AccessioniPrimary (citable) accession number: O43920
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 118 of the entry and version 3 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