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Q9UHB4

- NDOR1_HUMAN

UniProt

Q9UHB4 - NDOR1_HUMAN

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Protein

NADPH-dependent diflavin oxidoreductase 1

Gene
NDOR1, NR1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 Publications

Cofactori

FMN.2 Publications
FAD.2 Publications

Kineticsi

  1. KM=21 µM for cytochrome c1 Publication

Vmax=1.2 µmol/min/µg enzyme for cytochrome c reduction

pH dependencei

Optimum pH is about 8.0.

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 165FMNUniRule annotation
Nucleotide bindingi96 – 10510FMNUniRule annotation
Nucleotide bindingi242 – 25312FAD By similarityAdd
BLAST
Nucleotide bindingi379 – 38911FAD By similarityAdd
BLAST
Nucleotide bindingi454 – 47219NADP By similarityAdd
BLAST
Nucleotide bindingi543 – 55917NADP By similarityAdd
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
Complete GO annotation...

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 1 (EC:1.6.-.-)
Alternative name(s):
NADPH-dependent FMN and FAD-containing oxidoreductase
Novel reductase 1
Gene namesi
Name:NDOR1
Synonyms:NR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:29838. NDOR1.

Subcellular locationi

Cytoplasmperinuclear region
Note: Concentrated in perinuclear structure.2 Publications

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
Complete GO annotation...

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 1UniRule annotationPRO_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 Publications

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 150145Flavodoxin-likeAdd
BLAST
Domaini206 – 447242FAD-binding FR-typeAdd
BLAST

Compositional bias

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

Sequence similaritiesi

In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.

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. VSP_046313Add
BLAST
Alternative sequencei392 – 3987Missing in isoform 4. VSP_053807
Alternative sequencei518 – 5181Q → QPPALFSALQ in isoform 2. VSP_031487
Alternative sequencei543 – 59755GAYFY…TETWA → ATPSPCQRTSRKP in isoform 3. VSP_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.
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 .
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 112 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

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