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Q9UHB4

- NDOR1_HUMAN

UniProt

Q9UHB4 - NDOR1_HUMAN

Protein

NADPH-dependent diflavin oxidoreductase 1

Gene

NDOR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins By similarity. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis. Transfers electrons from NADPH to the Fe/S cluster of CIAPIN1.3 PublicationsUniRule annotation

    Cofactori

    FMN.
    FAD.

    Kineticsi

    1. KM=21 µM for cytochrome c1 Publication

    Vmax=1.2 µmol/min/µg enzyme for cytochrome c reduction1 Publication

    pH dependencei

    Optimum pH is about 8.0.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei132 – 1321FMN1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 165FMN1 PublicationUniRule annotation
    Nucleotide bindingi96 – 10510FMN1 PublicationUniRule annotation
    Nucleotide bindingi242 – 25312FADUniRule annotationAdd
    BLAST
    Nucleotide bindingi379 – 38911FADUniRule annotationAdd
    BLAST
    Nucleotide bindingi454 – 47219NADPUniRule annotationAdd
    BLAST
    Nucleotide bindingi543 – 55917NADPUniRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. flavin adenine dinucleotide binding Source: UniProtKB
    2. FMN binding Source: UniProtKB
    3. iron ion binding Source: InterPro
    4. NADP binding Source: UniProtKB
    5. NADPH-hemoprotein reductase activity Source: RefGenome
    6. oxidoreductase activity Source: UniProtKB
    7. oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen Source: RefGenome
    8. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell death Source: UniProtKB
    2. cellular response to menadione Source: UniProtKB
    3. iron-sulfur cluster assembly Source: UniProtKB-HAMAP
    4. oxidation-reduction process Source: UniProtKB
    5. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, FMN, NADP

    Enzyme and pathway databases

    BRENDAi1.5.1.30. 2681.
    ReactomeiREACT_160176. Cytosolic iron-sulfur cluster assembly.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADPH-dependent diflavin oxidoreductase 1UniRule annotation (EC:1.6.-.-UniRule annotation)
    Alternative name(s):
    NADPH-dependent FMN and FAD-containing oxidoreductaseUniRule annotation
    Novel reductase 1
    Gene namesi
    Name:NDOR1UniRule annotation
    Synonyms:NR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:29838. NDOR1.

    Subcellular locationi

    Cytoplasmperinuclear region 2 PublicationsUniRule annotation
    Note: Concentrated in perinuclear structure.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. intermediate filament cytoskeleton Source: HPA
    4. nucleus Source: HPA
    5. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134885020.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 597597NADPH-dependent diflavin oxidoreductase 1PRO_0000319539Add
    BLAST

    Proteomic databases

    MaxQBiQ9UHB4.
    PaxDbiQ9UHB4.
    PRIDEiQ9UHB4.

    PTM databases

    PhosphoSiteiQ9UHB4.

    Expressioni

    Tissue specificityi

    Low expression in brain, heart, kidney, pancreas, prostate and skeletal muscle. Highest levels in the placenta. Expressed in cancer cell lines including promyelocytic leukemia, HeLaS3, chronic myelagenous leukemia, lymphoblastic leukemia, Burkitt's lymphoma, colorectal adenocarcinoma, lung carcinoma, and melanoma G-361.1 Publication

    Gene expression databases

    ArrayExpressiQ9UHB4.
    BgeeiQ9UHB4.
    CleanExiHS_NDOR1.
    GenevestigatoriQ9UHB4.

    Organism-specific databases

    HPAiHPA024504.

    Interactioni

    Subunit structurei

    Interacts with CIAPIN1. Interacts with DCPS.3 PublicationsUniRule annotation

    Protein-protein interaction databases

    BioGridi118038. 6 interactions.
    STRINGi9606.ENSP00000360576.

    Structurei

    Secondary structure

    1
    597
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 117
    Beta strandi13 – 153
    Helixi16 – 3015
    Beta strandi34 – 396
    Turni40 – 423
    Helixi45 – 506
    Beta strandi52 – 598
    Helixi62 – 643
    Helixi68 – 703
    Helixi71 – 777
    Turni84 – 896
    Beta strandi91 – 988
    Beta strandi102 – 1043
    Helixi107 – 11812
    Beta strandi122 – 1254
    Beta strandi128 – 1314
    Turni135 – 1384
    Helixi139 – 15618

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4H2DX-ray1.80A/B1-161[»]
    ProteinModelPortaliQ9UHB4.
    SMRiQ9UHB4. Positions 4-161, 202-596.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini6 – 150145Flavodoxin-likeUniRule annotationAdd
    BLAST
    Domaini206 – 447242FAD-binding FR-typeUniRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi158 – 1614Poly-Pro

    Sequence similaritiesi

    Belongs to the NADPH-dependent diflavin oxidoreductase NDOR1 family.UniRule annotation
    In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.UniRule annotation
    Contains 1 FAD-binding FR-type domain.UniRule annotation
    Contains 1 flavodoxin-like domain.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0369.
    HOGENOMiHOG000173033.
    HOVERGENiHBG104950.
    OMAiGPSHFQD.
    OrthoDBiEOG7QG44B.
    PhylomeDBiQ9UHB4.
    TreeFamiTF105716.

    Family and domain databases

    Gene3Di1.20.990.10. 1 hit.
    3.40.50.360. 1 hit.
    HAMAPiMF_03178. NDOR1.
    InterProiIPR003097. FAD-binding_1.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR001094. Flavdoxin.
    IPR008254. Flavodoxin/NO_synth.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR029039. Flavoprotein-like.
    IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
    IPR028879. NDOR1.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view]
    PfamiPF00667. FAD_binding_1. 1 hit.
    PF00258. Flavodoxin_1. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    [Graphical view]
    PRINTSiPR00369. FLAVODOXIN.
    PR00371. FPNCR.
    SUPFAMiSSF52218. SSF52218. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEiPS51384. FAD_FR. 1 hit.
    PS50902. FLAVODOXIN_LIKE. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UHB4-1) [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

    MPSPQLLVLF GSQTGTAQDV SERLGREARR RRLGCRVQAL DSYPVVNLIN    50
    EPLVIFVCAT TGQGDPPDNM KNFWRFIFRK NLPSTALCQM DFAVLGLGDS 100
    SYAKFNFVAK KLHRRLLQLG GSALLPVCLG DDQHELGPDA AVDPWLRDLW 150
    DRVLGLYPPP PGLTEIPPGV PLPSKFTLLF LQEAPSTGSE GQRVAHPGSQ 200
    EPPSESKPFL APMISNQRVT GPSHFQDVRL IEFDILGSGI SFAAGDVVLI 250
    QPSNSAAHVQ RFCQVLGLDP DQLFMLQPRE PDVSSPTRLP QPCSMRHLVS 300
    HYLDIASVPR RSFFELLACL SLHELEREKL LEFSSAQGQE ELFEYCNRPR 350
    RTILEVLCDF PHTAAAIPPD YLLDLIPVIR PRAFSIASSL LTHPSRLQIL 400
    VAVVQFQTRL KEPRRGLCSS WLASLDPGQG PVRVPLWVRP GSLAFPETPD 450
    TPVIMVGPGT GVAPFRAAIQ ERVAQGQTGN FLFFGCRWRD QDFYWEAEWQ 500
    ELEKRDCLTL IPAFSREQEQ KVYVQHRLRE LGSLVWELLD RQGAYFYLAG 550
    NAKSMPADVS EALMSIFQEE GGLCSPDAAA YLARLQQTRR FQTETWA 597
    Length:597
    Mass (Da):66,763
    Last modified:May 1, 2000 - v1
    Checksum:i0D1340D7280A4D8F
    GO
    Isoform 2 (identifier: Q9UHB4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         518-518: Q → QPPALFSALQ

    Show »
    Length:606
    Mass (Da):67,688
    Checksum:i82F727F05E64E5DA
    GO
    Isoform 3 (identifier: Q9UHB4-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         138-171: Missing.
         543-597: GAYFYLAGNAKSMPADVSEALMSIFQEEGGLCSPDAAAYLARLQQTRRFQTETWA → ATPSPCQRTSRKP

    Note: No experimental confirmation available.

    Show »
    Length:521
    Mass (Da):58,455
    Checksum:i3070040C37E92223
    GO
    Isoform 4 (identifier: Q9UHB4-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         392-398: Missing.

    Note: Gene prediction based on EST data.

    Show »
    Length:590
    Mass (Da):65,943
    Checksum:i769AB27A3A4A2379
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti522 – 5221V → I in allele NDOR1*1; shows a decrease in affinity for NADPH and a reduction in ferricyanide reductase activity. 2 Publications
    Corresponds to variant rs62587579 [ dbSNP | Ensembl ].
    VAR_039010

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei138 – 17134Missing in isoform 3. 1 PublicationVSP_046313Add
    BLAST
    Alternative sequencei392 – 3987Missing in isoform 4. CuratedVSP_053807
    Alternative sequencei518 – 5181Q → QPPALFSALQ in isoform 2. 1 PublicationVSP_031487
    Alternative sequencei543 – 59755GAYFY…TETWA → ATPSPCQRTSRKP in isoform 3. 1 PublicationVSP_046314Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF199509 mRNA. Translation: AAF25205.1.
    AY077845 mRNA. Translation: AAL77754.1.
    AK074403 mRNA. No translation available.
    AK290026 mRNA. Translation: BAF82715.1.
    AL929554, BX255925 Genomic DNA. Translation: CAH72886.2.
    BX255925, AL929554 Genomic DNA. Translation: CAM24151.1.
    BC015735 mRNA. Translation: AAH15735.1.
    BC093782 mRNA. Translation: AAH93782.1.
    BC111943 mRNA. Translation: AAI11944.1.
    CCDSiCCDS48061.1. [Q9UHB4-2]
    CCDS48062.1. [Q9UHB4-4]
    CCDS48063.1. [Q9UHB4-3]
    CCDS7036.1. [Q9UHB4-1]
    RefSeqiNP_001137498.1. NM_001144026.2. [Q9UHB4-2]
    NP_001137499.1. NM_001144027.2. [Q9UHB4-3]
    NP_001137500.1. NM_001144028.2. [Q9UHB4-4]
    NP_055249.1. NM_014434.3. [Q9UHB4-1]
    UniGeneiHs.512564.

    Genome annotation databases

    EnsembliENST00000344894; ENSP00000343344; ENSG00000188566. [Q9UHB4-1]
    ENST00000371521; ENSP00000360576; ENSG00000188566. [Q9UHB4-2]
    ENST00000427047; ENSP00000394309; ENSG00000188566. [Q9UHB4-3]
    ENST00000458322; ENSP00000389905; ENSG00000188566. [Q9UHB4-4]
    GeneIDi27158.
    KEGGihsa:27158.
    UCSCiuc004clw.3. human. [Q9UHB4-1]

    Polymorphism databases

    DMDMi74735011.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF199509 mRNA. Translation: AAF25205.1 .
    AY077845 mRNA. Translation: AAL77754.1 .
    AK074403 mRNA. No translation available.
    AK290026 mRNA. Translation: BAF82715.1 .
    AL929554 , BX255925 Genomic DNA. Translation: CAH72886.2 .
    BX255925 , AL929554 Genomic DNA. Translation: CAM24151.1 .
    BC015735 mRNA. Translation: AAH15735.1 .
    BC093782 mRNA. Translation: AAH93782.1 .
    BC111943 mRNA. Translation: AAI11944.1 .
    CCDSi CCDS48061.1. [Q9UHB4-2 ]
    CCDS48062.1. [Q9UHB4-4 ]
    CCDS48063.1. [Q9UHB4-3 ]
    CCDS7036.1. [Q9UHB4-1 ]
    RefSeqi NP_001137498.1. NM_001144026.2. [Q9UHB4-2 ]
    NP_001137499.1. NM_001144027.2. [Q9UHB4-3 ]
    NP_001137500.1. NM_001144028.2. [Q9UHB4-4 ]
    NP_055249.1. NM_014434.3. [Q9UHB4-1 ]
    UniGenei Hs.512564.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4H2D X-ray 1.80 A/B 1-161 [» ]
    ProteinModelPortali Q9UHB4.
    SMRi Q9UHB4. Positions 4-161, 202-596.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118038. 6 interactions.
    STRINGi 9606.ENSP00000360576.

    PTM databases

    PhosphoSitei Q9UHB4.

    Polymorphism databases

    DMDMi 74735011.

    Proteomic databases

    MaxQBi Q9UHB4.
    PaxDbi Q9UHB4.
    PRIDEi Q9UHB4.

    Protocols and materials databases

    DNASUi 27158.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000344894 ; ENSP00000343344 ; ENSG00000188566 . [Q9UHB4-1 ]
    ENST00000371521 ; ENSP00000360576 ; ENSG00000188566 . [Q9UHB4-2 ]
    ENST00000427047 ; ENSP00000394309 ; ENSG00000188566 . [Q9UHB4-3 ]
    ENST00000458322 ; ENSP00000389905 ; ENSG00000188566 . [Q9UHB4-4 ]
    GeneIDi 27158.
    KEGGi hsa:27158.
    UCSCi uc004clw.3. human. [Q9UHB4-1 ]

    Organism-specific databases

    CTDi 27158.
    GeneCardsi GC09P140100.
    HGNCi HGNC:29838. NDOR1.
    HPAi HPA024504.
    MIMi 606073. gene.
    neXtProti NX_Q9UHB4.
    PharmGKBi PA134885020.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0369.
    HOGENOMi HOG000173033.
    HOVERGENi HBG104950.
    OMAi GPSHFQD.
    OrthoDBi EOG7QG44B.
    PhylomeDBi Q9UHB4.
    TreeFami TF105716.

    Enzyme and pathway databases

    BRENDAi 1.5.1.30. 2681.
    Reactomei REACT_160176. Cytosolic iron-sulfur cluster assembly.

    Miscellaneous databases

    ChiTaRSi NDOR1. human.
    GeneWikii NDOR1.
    GenomeRNAii 27158.
    NextBioi 49931.
    PROi Q9UHB4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UHB4.
    Bgeei Q9UHB4.
    CleanExi HS_NDOR1.
    Genevestigatori Q9UHB4.

    Family and domain databases

    Gene3Di 1.20.990.10. 1 hit.
    3.40.50.360. 1 hit.
    HAMAPi MF_03178. NDOR1.
    InterProi IPR003097. FAD-binding_1.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR001094. Flavdoxin.
    IPR008254. Flavodoxin/NO_synth.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR029039. Flavoprotein-like.
    IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
    IPR028879. NDOR1.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view ]
    Pfami PF00667. FAD_binding_1. 1 hit.
    PF00258. Flavodoxin_1. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00369. FLAVODOXIN.
    PR00371. FPNCR.
    SUPFAMi SSF52218. SSF52218. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEi PS51384. FAD_FR. 1 hit.
    PS50902. FLAVODOXIN_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a novel human dual flavin reductase."
      Paine M.J., Garner A.P., Powell D., Sibbald J., Sales M., Pratt N., Smith T., Tew D.G., Wolf C.R.
      J. Biol. Chem. 275:1471-1478(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
    2. "Coordinate expression of NADPH-dependent flavin reductase, Fre-1, and Hint-related 7meGMP-directed hydrolase, DCS-1."
      Kwasnicka D.A., Krakowiak A., Thacker C., Brenner C., Vincent S.R.
      J. Biol. Chem. 278:39051-39058(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Brain.
    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] (ISOFORMS 1 AND 3).
      Tissue: Hippocampus and Umbilical vein endothelial cell.
    4. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      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 ILE-522.
      Tissue: Brain and Skin.
    6. "Role of a novel dual flavin reductase (NR1) and an associated histidine triad protein (DCS-1) in menadione-induced cytotoxicity."
      Kwasnicka-Crawford D.A., Vincent S.R.
      Biochem. Biophys. Res. Commun. 336:565-571(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DCPS, CYTOTOXICITY.
    7. "Tah18 transfers electrons to Dre2 in cytosolic iron-sulfur protein biogenesis."
      Netz D.J., Stumpfig M., Dore C., Muhlenhoff U., Pierik A.J., Lill R.
      Nat. Chem. Biol. 6:758-765(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CIAPIN1.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-161 IN COMPLEX WITH FMN, FUNCTION, COFACTOR, INTERACTION WITH CIAPIN1.
    10. "Identification of a functionally impaired allele of human novel oxidoreductase 1 (NDOR1), NDOR1*1."
      Finn R.D., Wilkie M., Smith G., Paine M.J.
      Pharmacogenet. Genomics 15:381-386(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ILE-522, CHARACTERIZATION OF VARIANT ILE-522.

    Entry informationi

    Entry nameiNDOR1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UHB4
    Secondary accession number(s): D3YTG6
    , D3YTH9, Q5VSG4, Q86US9, Q96BC6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 113 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

    Miscellaneous

    Overexpression enhanced cytotoxicity of menadione, and consequently induced cell death, coexpression with DCPS reduced this toxicity.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3