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P28331

- NDUS1_HUMAN

UniProt

P28331 - NDUS1_HUMAN

Protein

NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

Gene

NDUFS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 3 (07 Mar 2006)
      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. 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.By similarity

    Catalytic activityi

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

    Cofactori

    Binds 1 2Fe-2S cluster per subunit.By similarity
    Binds 2 4Fe-4S clusters per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi64 – 641Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi75 – 751Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi78 – 781Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi92 – 921Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi124 – 1241Iron-sulfur 2 (4Fe-4S); via pros nitrogenBy similarity
    Metal bindingi128 – 1281Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi131 – 1311Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi137 – 1371Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi176 – 1761Iron-sulfur 3 (4Fe-4S)By similarity
    Metal bindingi179 – 1791Iron-sulfur 3 (4Fe-4S)By similarity
    Metal bindingi182 – 1821Iron-sulfur 3 (4Fe-4S)By similarity
    Metal bindingi226 – 2261Iron-sulfur 3 (4Fe-4S)By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. apoptotic mitochondrial changes Source: UniProtKB
    2. ATP metabolic process Source: UniProtKB
    3. cellular metabolic process Source: Reactome
    4. cellular respiration Source: UniProtKB
    5. mitochondrial electron transport, NADH to ubiquinone Source: UniProtKB
    6. reactive oxygen species metabolic process Source: UniProtKB
    7. regulation of mitochondrial membrane potential Source: UniProtKB
    8. respiratory electron transport chain Source: Reactome
    9. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Respiratory chain, Transport

    Keywords - Ligandi

    2Fe-2S, 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-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial (EC:1.6.5.3, EC:1.6.99.3)
    Alternative name(s):
    Complex I-75kD
    Short name:
    CI-75kD
    Gene namesi
    Name:NDUFS1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:7707. NDUFS1.

    Subcellular locationi

    GO - Cellular componenti

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

    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 varianti241 – 2411R → W in MT-C1D. 1 Publication
    VAR_019532
    Natural varianti252 – 2521D → G in MT-C1D. 1 Publication
    VAR_019533

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi252010. phenotype.
    Orphaneti2609. Isolated NADH-CoQ reductase deficiency.
    255241. Leigh syndrome with leukodystrophy.
    PharmGKBiPA31518.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2323MitochondrionBy similarityAdd
    BLAST
    Chaini24 – 727704NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrialPRO_0000019968Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei84 – 841N6-acetyllysineBy similarity
    Modified residuei467 – 4671N6-acetyllysineBy similarity
    Modified residuei499 – 4991N6-acetyllysineBy similarity
    Modified residuei709 – 7091N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP28331.
    PaxDbiP28331.
    PeptideAtlasiP28331.
    PRIDEiP28331.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00604664.
    P28331.
    UCD-2DPAGEP28331.

    PTM databases

    PhosphoSiteiP28331.

    Miscellaneous databases

    PMAP-CutDBP28331.

    Expressioni

    Gene expression databases

    ArrayExpressiP28331.
    BgeeiP28331.
    CleanExiHS_NDUFS1.
    GenevestigatoriP28331.

    Interactioni

    Subunit structurei

    Complex I is composed of 45 different subunits.1 Publication

    Protein-protein interaction databases

    BioGridi110799. 38 interactions.
    IntActiP28331. 13 interactions.
    MINTiMINT-3011123.
    STRINGi9606.ENSP00000233190.

    Structurei

    3D structure databases

    ProteinModelPortaliP28331.
    SMRiP28331. Positions 31-636.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini30 – 108792Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini245 – 301574Fe-4S Mo/W bis-MGD-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the complex I 75 kDa subunit family.Curated
    Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
    Contains 1 4Fe-4S Mo/W bis-MGD-type domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1034.
    HOGENOMiHOG000031442.
    HOVERGENiHBG003482.
    InParanoidiP28331.
    KOiK03934.
    OMAiKEDWVII.
    OrthoDBiEOG783MTP.
    PhylomeDBiP28331.
    TreeFamiTF105756.

    Family and domain databases

    Gene3Di3.10.20.30. 1 hit.
    InterProiIPR001041. 2Fe-2S_ferredoxin-type.
    IPR012675. Beta-grasp_dom.
    IPR006656. Mopterin_OxRdtase.
    IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
    IPR000283. NADH_UbQ_OxRdtase_75kDa_su_CS.
    IPR010228. NADH_UbQ_OxRdtase_Gsu.
    IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
    IPR015405. NuoG_C.
    [Graphical view]
    PfamiPF09326. DUF1982. 1 hit.
    PF00384. Molybdopterin. 1 hit.
    PF10588. NADH-G_4Fe-4S_3. 1 hit.
    [Graphical view]
    SMARTiSM00929. NADH-G_4Fe-4S_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF54292. SSF54292. 1 hit.
    TIGRFAMsiTIGR01973. NuoG. 1 hit.
    PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
    PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
    PS00641. COMPLEX1_75K_1. 1 hit.
    PS00642. COMPLEX1_75K_2. 1 hit.
    PS00643. COMPLEX1_75K_3. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P28331-1) [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

    MLRIPVRKAL VGLSKSPKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL    50
    QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVVA ACAMPVMKGW 100
    NILTNSEKSK KAREGVMEFL LANHPLDCPI CDQGGECDLQ DQSMMFGNDR 150
    SRFLEGKRAV EDKNIGPLVK TIMTRCIQCT RCIRFASEIA GVDDLGTTGR 200
    GNDMQVGTYI EKMFMSELSG NIIDICPVGA LTSKPYAFTA RPWETRKTES 250
    IDVMDAVGSN IVVSTRTGEV MRILPRMHED INEEWISDKT RFAYDGLKRQ 300
    RLTEPMVRNE KGLLTYTSWE DALSRVAGML QSFQGKDVAA IAGGLVDAEA 350
    LVALKDLLNR VDSDTLCTEE VFPTAGAGTD LRSNYLLNTT IAGVEEADVV 400
    LLVGTNPRFE APLFNARIRK SWLHNDLKVA LIGSPVDLTY TYDHLGDSPK 450
    ILQDIASGSH PFSQVLKEAK KPMVVLGSSA LQRNDGAAIL AAVSSIAQKI 500
    RMTSGVTGDW KVMNILHRIA SQVAALDLGY KPGVEAIRKN PPKVLFLLGA 550
    DGGCITRQDL PKDCFIIYQG HHGDVGAPIA DVILPGAAYT EKSATYVNTE 600
    GRAQQTKVAV TPPGLAREDW KIIRALSEIA GMTLPYDTLD QVRNRLEEVS 650
    PNLVRYDDIE GANYFQQANE LSKLVNQQLL ADPLVPPQLT IKDFYMTDSI 700
    SRASQTMAKC VKAVTEGAQA VEEPSIC 727
    Length:727
    Mass (Da):79,468
    Last modified:March 7, 2006 - v3
    Checksum:i9C35F4B8294771FB
    GO
    Isoform 2 (identifier: P28331-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MRIRGSSGTLSRINM

    Note: No experimental confirmation available.

    Show »
    Length:741
    Mass (Da):80,997
    Checksum:iEB7CA8F41E3DF6E2
    GO
    Isoform 3 (identifier: P28331-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-2: ML → MW
         3-113: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:616
    Mass (Da):67,524
    Checksum:i16CA2EF571877D03
    GO
    Isoform 4 (identifier: P28331-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-57: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:670
    Mass (Da):73,527
    Checksum:iC8B37BF8C954187F
    GO
    Isoform 5 (identifier: P28331-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         52-87: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:691
    Mass (Da):75,375
    Checksum:i522872E0D6EB9E09
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81K → R in CAA43412. (PubMed:1935949)Curated
    Sequence conflicti417 – 4171R → W in CAA43412. (PubMed:1935949)Curated
    Sequence conflicti572 – 5721H → L in BAG58551. (PubMed:14702039)Curated
    Sequence conflicti691 – 6911I → L in CAA43412. (PubMed:1935949)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti241 – 2411R → Q.1 Publication
    Corresponds to variant rs17856901 [ dbSNP | Ensembl ].
    VAR_025511
    Natural varianti241 – 2411R → W in MT-C1D. 1 Publication
    VAR_019532
    Natural varianti252 – 2521D → G in MT-C1D. 1 Publication
    VAR_019533
    Natural varianti253 – 2531V → G.1 Publication
    VAR_069506
    Natural varianti649 – 6491V → F.1 Publication
    Corresponds to variant rs1044049 [ dbSNP | Ensembl ].
    VAR_018463

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5757Missing in isoform 4. 1 PublicationVSP_043727Add
    BLAST
    Alternative sequencei1 – 22ML → MW in isoform 3. 1 PublicationVSP_043728
    Alternative sequencei1 – 11M → MRIRGSSGTLSRINM in isoform 2. CuratedVSP_042682
    Alternative sequencei3 – 113111Missing in isoform 3. 1 PublicationVSP_043729Add
    BLAST
    Alternative sequencei52 – 8736Missing in isoform 5. 1 PublicationVSP_045864Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61100 mRNA. Translation: CAA43412.1.
    AK295705 mRNA. Translation: BAG58551.1.
    AK295987 mRNA. Translation: BAG58762.1.
    AK298320 mRNA. Translation: BAG60573.1.
    AK300585 mRNA. Translation: BAG62283.1.
    AC007383 Genomic DNA. Translation: AAY15061.1.
    CH471063 Genomic DNA. Translation: EAW70379.1.
    BC022368 mRNA. Translation: AAH22368.1.
    BC030833 mRNA. Translation: AAH30833.1.
    CCDSiCCDS2366.1. [P28331-1]
    CCDS56162.1. [P28331-4]
    CCDS56163.1. [P28331-3]
    CCDS56164.1. [P28331-5]
    CCDS56165.1. [P28331-2]
    PIRiS17854.
    RefSeqiNP_001186910.1. NM_001199981.1. [P28331-5]
    NP_001186911.1. NM_001199982.1. [P28331-3]
    NP_001186912.1. NM_001199983.1. [P28331-4]
    NP_001186913.1. NM_001199984.1. [P28331-2]
    NP_004997.4. NM_005006.6. [P28331-1]
    UniGeneiHs.471207.
    Hs.598436.

    Genome annotation databases

    EnsembliENST00000233190; ENSP00000233190; ENSG00000023228. [P28331-1]
    ENST00000423725; ENSP00000397760; ENSG00000023228. [P28331-4]
    ENST00000432169; ENSP00000409689; ENSG00000023228. [P28331-3]
    ENST00000440274; ENSP00000409766; ENSG00000023228. [P28331-5]
    ENST00000449699; ENSP00000399912; ENSG00000023228. [P28331-1]
    ENST00000455934; ENSP00000392709; ENSG00000023228. [P28331-2]
    GeneIDi4719.
    KEGGihsa:4719.
    UCSCiuc002vbe.3. human. [P28331-1]
    uc010ziq.2. human. [P28331-2]
    uc010zit.2. human. [P28331-3]

    Polymorphism databases

    DMDMi92090799.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61100 mRNA. Translation: CAA43412.1 .
    AK295705 mRNA. Translation: BAG58551.1 .
    AK295987 mRNA. Translation: BAG58762.1 .
    AK298320 mRNA. Translation: BAG60573.1 .
    AK300585 mRNA. Translation: BAG62283.1 .
    AC007383 Genomic DNA. Translation: AAY15061.1 .
    CH471063 Genomic DNA. Translation: EAW70379.1 .
    BC022368 mRNA. Translation: AAH22368.1 .
    BC030833 mRNA. Translation: AAH30833.1 .
    CCDSi CCDS2366.1. [P28331-1 ]
    CCDS56162.1. [P28331-4 ]
    CCDS56163.1. [P28331-3 ]
    CCDS56164.1. [P28331-5 ]
    CCDS56165.1. [P28331-2 ]
    PIRi S17854.
    RefSeqi NP_001186910.1. NM_001199981.1. [P28331-5 ]
    NP_001186911.1. NM_001199982.1. [P28331-3 ]
    NP_001186912.1. NM_001199983.1. [P28331-4 ]
    NP_001186913.1. NM_001199984.1. [P28331-2 ]
    NP_004997.4. NM_005006.6. [P28331-1 ]
    UniGenei Hs.471207.
    Hs.598436.

    3D structure databases

    ProteinModelPortali P28331.
    SMRi P28331. Positions 31-636.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110799. 38 interactions.
    IntActi P28331. 13 interactions.
    MINTi MINT-3011123.
    STRINGi 9606.ENSP00000233190.

    Chemistry

    ChEMBLi CHEMBL2363065.
    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei P28331.

    Polymorphism databases

    DMDMi 92090799.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00604664.
    P28331.
    UCD-2DPAGE P28331.

    Proteomic databases

    MaxQBi P28331.
    PaxDbi P28331.
    PeptideAtlasi P28331.
    PRIDEi P28331.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000233190 ; ENSP00000233190 ; ENSG00000023228 . [P28331-1 ]
    ENST00000423725 ; ENSP00000397760 ; ENSG00000023228 . [P28331-4 ]
    ENST00000432169 ; ENSP00000409689 ; ENSG00000023228 . [P28331-3 ]
    ENST00000440274 ; ENSP00000409766 ; ENSG00000023228 . [P28331-5 ]
    ENST00000449699 ; ENSP00000399912 ; ENSG00000023228 . [P28331-1 ]
    ENST00000455934 ; ENSP00000392709 ; ENSG00000023228 . [P28331-2 ]
    GeneIDi 4719.
    KEGGi hsa:4719.
    UCSCi uc002vbe.3. human. [P28331-1 ]
    uc010ziq.2. human. [P28331-2 ]
    uc010zit.2. human. [P28331-3 ]

    Organism-specific databases

    CTDi 4719.
    GeneCardsi GC02M206986.
    HGNCi HGNC:7707. NDUFS1.
    MIMi 157655. gene.
    252010. phenotype.
    neXtProti NX_P28331.
    Orphaneti 2609. Isolated NADH-CoQ reductase deficiency.
    255241. Leigh syndrome with leukodystrophy.
    PharmGKBi PA31518.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1034.
    HOGENOMi HOG000031442.
    HOVERGENi HBG003482.
    InParanoidi P28331.
    KOi K03934.
    OMAi KEDWVII.
    OrthoDBi EOG783MTP.
    PhylomeDBi P28331.
    TreeFami TF105756.

    Enzyme and pathway databases

    Reactomei REACT_22393. Respiratory electron transport.

    Miscellaneous databases

    ChiTaRSi NDUFS1. human.
    GeneWikii NDUFS1.
    GenomeRNAii 4719.
    NextBioi 18202.
    PMAP-CutDB P28331.
    PROi P28331.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P28331.
    Bgeei P28331.
    CleanExi HS_NDUFS1.
    Genevestigatori P28331.

    Family and domain databases

    Gene3Di 3.10.20.30. 1 hit.
    InterProi IPR001041. 2Fe-2S_ferredoxin-type.
    IPR012675. Beta-grasp_dom.
    IPR006656. Mopterin_OxRdtase.
    IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
    IPR000283. NADH_UbQ_OxRdtase_75kDa_su_CS.
    IPR010228. NADH_UbQ_OxRdtase_Gsu.
    IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
    IPR015405. NuoG_C.
    [Graphical view ]
    Pfami PF09326. DUF1982. 1 hit.
    PF00384. Molybdopterin. 1 hit.
    PF10588. NADH-G_4Fe-4S_3. 1 hit.
    [Graphical view ]
    SMARTi SM00929. NADH-G_4Fe-4S_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54292. SSF54292. 1 hit.
    TIGRFAMsi TIGR01973. NuoG. 1 hit.
    PROSITEi PS51085. 2FE2S_FER_2. 1 hit.
    PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
    PS00641. COMPLEX1_75K_1. 1 hit.
    PS00642. COMPLEX1_75K_2. 1 hit.
    PS00643. COMPLEX1_75K_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Determination of the cDNA sequence for the human mitochondrial 75-kDa Fe-S protein of NADH-coenzyme Q reductase."
      Chow W., Ragan I., Robinson B.H.
      Eur. J. Biochem. 201:547-550(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PHE-649.
    2. "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] (ISOFORMS 1; 3; 4 AND 5).
      Tissue: Hippocampus, Kidney and Substantia nigra.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., 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 E.A., 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 S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1), VARIANT GLN-241.
      Tissue: Brain and Liver.
    6. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 185-200; 247-266; 277-289; 312-325; 361-382; 451-467; 471-499; 519-538; 544-557 AND 625-655, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Large-scale deletion and point mutations of the nuclear NDUFV1 and NDUFS1 genes in mitochondrial complex I deficiency."
      Benit P., Chretien D., Kadhom N., de Lonlay-Debeney P., Cormier-Daire V., Cabral A., Peudenier S., Rustin P., Munnich A., Roetig A.
      Am. J. Hum. Genet. 68:1344-1352(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MT-C1D TRP-241 AND GLY-252.
    10. "Genomic analysis of mitochondrial diseases in a consanguineous population reveals novel candidate disease genes."
      Shamseldin H.E., Alshammari M., Al-Sheddi T., Salih M.A., Alkhalidi H., Kentab A., Repetto G.M., Hashem M., Alkuraya F.S.
      J. Med. Genet. 49:234-241(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GLY-253.

    Entry informationi

    Entry nameiNDUS1_HUMAN
    AccessioniPrimary (citable) accession number: P28331
    Secondary accession number(s): B4DIN9
    , B4DJA0, B4DPG1, B4DUC1, E7ENF3, Q53TR8, Q8N1C4, Q8TCC9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: March 7, 2006
    Last modified: October 1, 2014
    This is version 162 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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