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P16435

- NCPR_HUMAN

UniProt

P16435 - NCPR_HUMAN

Protein

NADPH--cytochrome P450 reductase

Gene

POR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 172 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5.

    Catalytic activityi

    NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein.

    Cofactori

    FAD.
    FMN.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi170 – 20132FMNPROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi314 – 32512FADBy similarityAdd
    BLAST
    Nucleotide bindingi451 – 46111FADBy similarityAdd
    BLAST
    Nucleotide bindingi529 – 54719NADPBy similarityAdd
    BLAST
    Nucleotide bindingi623 – 63917NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. cytochrome-b5 reductase activity, acting on NAD(P)H Source: Ensembl
    2. electron carrier activity Source: Ensembl
    3. flavin adenine dinucleotide binding Source: Ensembl
    4. FMN binding Source: Ensembl
    5. hydrolase activity Source: Ensembl
    6. iron-cytochrome-c reductase activity Source: Ensembl
    7. iron ion binding Source: InterPro
    8. NADP binding Source: Ensembl
    9. NADPH-hemoprotein reductase activity Source: UniProtKB
    10. nitric oxide dioxygenase activity Source: Ensembl
    11. protein binding Source: IntAct

    GO - Biological processi

    1. carnitine metabolic process Source: Ensembl
    2. cellular organofluorine metabolic process Source: BHF-UCL
    3. cellular response to follicle-stimulating hormone stimulus Source: Ensembl
    4. cellular response to peptide hormone stimulus Source: Ensembl
    5. demethylation Source: Ensembl
    6. fatty acid oxidation Source: Ensembl
    7. flavonoid metabolic process Source: Ensembl
    8. internal peptidyl-lysine acetylation Source: Ensembl
    9. negative regulation of apoptotic process Source: Ensembl
    10. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    11. negative regulation of lipase activity Source: Ensembl
    12. nitrate catabolic process Source: Ensembl
    13. nitric oxide catabolic process Source: Ensembl
    14. oxidation-reduction process Source: UniProtKB
    15. positive regulation of cholesterol biosynthetic process Source: Ensembl
    16. positive regulation of chondrocyte differentiation Source: Ensembl
    17. positive regulation of monooxygenase activity Source: BHF-UCL
    18. positive regulation of smoothened signaling pathway Source: Ensembl
    19. positive regulation of steroid hormone biosynthetic process Source: Ensembl
    20. regulation of growth plate cartilage chondrocyte proliferation Source: Ensembl
    21. response to drug Source: Ensembl
    22. response to nutrient Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, FMN, NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:HS05140-MONOMER.
    SABIO-RKP16435.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADPH--cytochrome P450 reductase (EC:1.6.2.4)
    Short name:
    CPR
    Short name:
    P450R
    Gene namesi
    Name:POR
    Synonyms:CYPOR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:9208. POR.

    Subcellular locationi

    Endoplasmic reticulum membrane; Peripheral membrane protein
    Note: Anchored to the ER membrane by its N-terminal hydrophobic region.

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. intracellular membrane-bounded organelle Source: UniProtKB
    3. membrane Source: UniProtKB
    4. mitochondrion Source: Ensembl

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Antley-Bixler syndrome, with genital anomalies and disordered steroidogenesis (ABS1) [MIM:201750]: A disease characterized by the association of Antley-Bixler syndrome with steroidogenesis defects and abnormal genitalia. Antley-Bixler syndrome is characterized by craniosynostosis, radiohumeral synostosis present from the perinatal period, midface hypoplasia, choanal stenosis or atresia, femoral bowing and multiple joint contractures.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti284 – 2841A → P in ABS1 and DISPORD; significant reduction of activity. 2 Publications
    VAR_021155
    Natural varianti454 – 4541R → H in ABS1 and DISPORD; significant reduction of activity. 4 Publications
    VAR_021156
    Natural varianti489 – 4891V → E in ABS1; significant reduction of activity. 1 Publication
    VAR_021157
    Natural varianti575 – 5751Y → C in ABS1. 1 Publication
    VAR_021159
    Natural varianti609 – 6179LKQDREHLW → R in ABS1.
    VAR_021161
    Disordered steroidogenesis due to cytochrome P450 oxidoreductase deficiency (DISPORD) [MIM:613571]: A disorder resulting in a rare variant of congenital adrenal hyperplasia, with apparent combined P450C17 and P450C21 deficiency and accumulation of steroid metabolites. Affected girls are born with ambiguous genitalia, but their circulating androgens are low and virilization does not progress. Conversely, affected boys are sometimes born undermasculinized. Boys and girls can present with bone malformations, in some cases resembling the pattern seen in patients with Antley-Bixler syndrome.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti178 – 1781Y → D in DISPORD; complete loss of activity. 1 Publication
    VAR_021154
    Natural varianti284 – 2841A → P in ABS1 and DISPORD; significant reduction of activity. 2 Publications
    VAR_021155
    Natural varianti454 – 4541R → H in ABS1 and DISPORD; significant reduction of activity. 4 Publications
    VAR_021156
    Natural varianti566 – 5661C → Y in DISPORD; significant reduction of activity. 2 Publications
    VAR_021158
    Natural varianti605 – 6051V → F in DISPORD; significant reduction of activity. 1 Publication
    VAR_021160

    Keywords - Diseasei

    Congenital adrenal hyperplasia, Craniosynostosis, Disease mutation

    Organism-specific databases

    MIMi201750. phenotype.
    613571. phenotype.
    Orphaneti95699. Congenital adrenal hyperplasia due to cytochrome P450 oxidoreductase deficiency.
    PharmGKBiPA33532.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 677676NADPH--cytochrome P450 reductasePRO_0000167596Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylglycine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP16435.
    PaxDbiP16435.
    PRIDEiP16435.

    PTM databases

    PhosphoSiteiP16435.

    Expressioni

    Gene expression databases

    ArrayExpressiP16435.
    BgeeiP16435.
    CleanExiHS_POR.
    GenevestigatoriP16435.

    Organism-specific databases

    HPAiCAB004372.
    HPA010136.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CYP2C2P001814EBI-726554,EBI-4320576From a different organism.
    PGRMC1O002645EBI-726554,EBI-1045534

    Protein-protein interaction databases

    BioGridi111443. 15 interactions.
    DIPiDIP-29682N.
    IntActiP16435. 5 interactions.
    MINTiMINT-1212161.
    STRINGi9606.ENSP00000265302.

    Structurei

    Secondary structure

    1
    677
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi69 – 768
    Beta strandi79 – 857
    Beta strandi87 – 893
    Helixi90 – 10112
    Helixi102 – 1054
    Beta strandi109 – 1124
    Helixi114 – 1163
    Helixi119 – 1279
    Beta strandi132 – 1387
    Helixi141 – 1433
    Helixi147 – 1493
    Helixi150 – 1589
    Beta strandi167 – 1748
    Beta strandi178 – 1803
    Helixi183 – 19412
    Beta strandi198 – 2014
    Beta strandi204 – 2074
    Helixi212 – 23120
    Beta strandi245 – 2495
    Helixi255 – 2573
    Beta strandi259 – 2613
    Beta strandi263 – 2653
    Turni266 – 2705
    Beta strandi278 – 2803
    Beta strandi282 – 29110
    Beta strandi294 – 2985
    Beta strandi300 – 3067
    Beta strandi319 – 3224
    Helixi328 – 33811
    Beta strandi345 – 3528
    Beta strandi360 – 3667
    Helixi367 – 3737
    Helixi383 – 3897
    Helixi390 – 3923
    Helixi396 – 40611
    Beta strandi407 – 4093
    Helixi410 – 41910
    Turni420 – 4245
    Helixi427 – 4337
    Helixi441 – 4477
    Beta strandi454 – 4574
    Turni462 – 4643
    Beta strandi468 – 4747
    Beta strandi477 – 4793
    Beta strandi485 – 4873
    Helixi489 – 4957
    Beta strandi508 – 5147
    Beta strandi528 – 5314
    Helixi534 – 5374
    Helixi538 – 55316
    Beta strandi560 – 5678
    Turni569 – 5713
    Helixi576 – 5849
    Beta strandi587 – 5959
    Beta strandi598 – 6014
    Helixi605 – 6117
    Helixi613 – 6219
    Beta strandi625 – 6317
    Turni632 – 6343
    Helixi635 – 65016
    Helixi655 – 66713
    Beta strandi670 – 6767

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B1CX-ray1.93A61-241[»]
    3FJOX-ray2.50A232-677[»]
    3QE2X-ray1.75A/B64-677[»]
    3QFCX-ray1.80A/B64-677[»]
    3QFRX-ray2.40A/B64-677[»]
    3QFSX-ray1.40A241-677[»]
    3QFTX-ray1.40A241-677[»]
    ProteinModelPortaliP16435.
    SMRiP16435. Positions 66-677.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16435.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini80 – 224145Flavodoxin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini279 – 521243FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.Curated
    Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
    Contains 1 flavodoxin-like domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0369.
    HOGENOMiHOG000282027.
    HOVERGENiHBG000432.
    InParanoidiP16435.
    KOiK00327.
    OrthoDBiEOG7HQN7J.
    PhylomeDBiP16435.
    TreeFamiTF105719.

    Family and domain databases

    Gene3Di1.20.990.10. 1 hit.
    3.40.50.360. 1 hit.
    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.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR023208. P450R.
    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]
    PIRSFiPIRSF000208. P450R. 1 hit.
    PRINTSiPR00369. FLAVODOXIN.
    PR00371. FPNCR.
    SUPFAMiSSF52218. SSF52218. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEiPS51384. FAD_FR. 1 hit.
    PS50902. FLAVODOXIN_LIKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P16435-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGDSHVDTSS TVSEAVAEEV SLFSMTDMIL FSLIVGLLTY WFLFRKKKEE    50
    VPEFTKIQTL TSSVRESSFV EKMKKTGRNI IVFYGSQTGT AEEFANRLSK 100
    DAHRYGMRGM SADPEEYDLA DLSSLPEIDN ALVVFCMATY GEGDPTDNAQ 150
    DFYDWLQETD VDLSGVKFAV FGLGNKTYEH FNAMGKYVDK RLEQLGAQRI 200
    FELGLGDDDG NLEEDFITWR EQFWPAVCEH FGVEATGEES SIRQYELVVH 250
    TDIDAAKVYM GEMGRLKSYE NQKPPFDAKN PFLAAVTTNR KLNQGTERHL 300
    MHLELDISDS KIRYESGDHV AVYPANDSAL VNQLGKILGA DLDVVMSLNN 350
    LDEESNKKHP FPCPTSYRTA LTYYLDITNP PRTNVLYELA QYASEPSEQE 400
    LLRKMASSSG EGKELYLSWV VEARRHILAI LQDCPSLRPP IDHLCELLPR 450
    LQARYYSIAS SSKVHPNSVH ICAVVVEYET KAGRINKGVA TNWLRAKEPA 500
    GENGGRALVP MFVRKSQFRL PFKATTPVIM VGPGTGVAPF IGFIQERAWL 550
    RQQGKEVGET LLYYGCRRSD EDYLYREELA QFHRDGALTQ LNVAFSREQS 600
    HKVYVQHLLK QDREHLWKLI EGGAHIYVCG DARNMARDVQ NTFYDIVAEL 650
    GAMEHAQAVD YIKKLMTKGR YSLDVWS 677
    Length:677
    Mass (Da):76,690
    Last modified:January 23, 2007 - v2
    Checksum:i2F7D4B9CDFDF5A74
    GO

    Sequence cautioni

    The sequence AAH34277.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti405 – 4051M → L in BAB18572. 1 PublicationCurated
    Sequence conflicti518 – 5181F → L in AAB21814. (PubMed:1550342)Curated
    Sequence conflicti518 – 5181F → L in BAB18572. 1 PublicationCurated
    Sequence conflicti537 – 5382VA → WH in AAB21814. (PubMed:1550342)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti178 – 1781Y → D in DISPORD; complete loss of activity. 1 Publication
    VAR_021154
    Natural varianti225 – 2251P → L.2 Publications
    VAR_047885
    Natural varianti252 – 2521D → N.1 Publication
    VAR_047886
    Natural varianti284 – 2841A → P in ABS1 and DISPORD; significant reduction of activity. 2 Publications
    VAR_021155
    Natural varianti454 – 4541R → H in ABS1 and DISPORD; significant reduction of activity. 4 Publications
    VAR_021156
    Natural varianti489 – 4891V → E in ABS1; significant reduction of activity. 1 Publication
    VAR_021157
    Natural varianti500 – 5001A → V.4 Publications
    Corresponds to variant rs1057868 [ dbSNP | Ensembl ].
    VAR_004617
    Natural varianti551 – 5511R → Q.
    VAR_004618
    Natural varianti566 – 5661C → Y in DISPORD; significant reduction of activity. 2 Publications
    VAR_021158
    Natural varianti575 – 5751Y → C in ABS1. 1 Publication
    VAR_021159
    Natural varianti605 – 6051V → F in DISPORD; significant reduction of activity. 1 Publication
    VAR_021160
    Natural varianti609 – 6179LKQDREHLW → R in ABS1.
    VAR_021161

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S90469 mRNA. Translation: AAB21814.1.
    AF258341 mRNA. Translation: AAG09798.1.
    AB051763 mRNA. Translation: BAB18572.1.
    DQ640499 Genomic DNA. Translation: ABF70199.1.
    AC005067 Genomic DNA. Translation: AAD45961.1.
    AC006330 Genomic DNA. No translation available.
    BC034277 mRNA. Translation: AAH34277.1. Different initiation.
    PIRiA33421. A60557.
    RefSeqiNP_000932.3. NM_000941.2.
    UniGeneiHs.354056.

    Genome annotation databases

    EnsembliENST00000394893; ENSP00000378355; ENSG00000127948.
    ENST00000412064; ENSP00000404731; ENSG00000127948.
    ENST00000412521; ENSP00000409238; ENSG00000127948.
    ENST00000414186; ENSP00000399327; ENSG00000127948.
    ENST00000418341; ENSP00000389719; ENSG00000127948.
    ENST00000432753; ENSP00000389409; ENSG00000127948.
    ENST00000439963; ENSP00000390540; ENSG00000127948.
    ENST00000449920; ENSP00000399556; ENSG00000127948.
    ENST00000453773; ENSP00000395813; ENSG00000127948.
    ENST00000454934; ENSP00000414263; ENSG00000127948.
    ENST00000461988; ENSP00000419970; ENSG00000127948.
    GeneIDi5447.
    KEGGihsa:5447.
    UCSCiuc011kge.2. human.

    Polymorphism databases

    DMDMi2851393.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S90469 mRNA. Translation: AAB21814.1 .
    AF258341 mRNA. Translation: AAG09798.1 .
    AB051763 mRNA. Translation: BAB18572.1 .
    DQ640499 Genomic DNA. Translation: ABF70199.1 .
    AC005067 Genomic DNA. Translation: AAD45961.1 .
    AC006330 Genomic DNA. No translation available.
    BC034277 mRNA. Translation: AAH34277.1 . Different initiation.
    PIRi A33421. A60557.
    RefSeqi NP_000932.3. NM_000941.2.
    UniGenei Hs.354056.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B1C X-ray 1.93 A 61-241 [» ]
    3FJO X-ray 2.50 A 232-677 [» ]
    3QE2 X-ray 1.75 A/B 64-677 [» ]
    3QFC X-ray 1.80 A/B 64-677 [» ]
    3QFR X-ray 2.40 A/B 64-677 [» ]
    3QFS X-ray 1.40 A 241-677 [» ]
    3QFT X-ray 1.40 A 241-677 [» ]
    ProteinModelPortali P16435.
    SMRi P16435. Positions 66-677.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111443. 15 interactions.
    DIPi DIP-29682N.
    IntActi P16435. 5 interactions.
    MINTi MINT-1212161.
    STRINGi 9606.ENSP00000265302.

    Chemistry

    ChEMBLi CHEMBL2169731.
    DrugBanki DB00865. Benzphetamine.
    DB00694. Daunorubicin.
    DB00166. Lipoic Acid.
    DB00170. Menadione.
    DB01028. Methoxyflurane.
    DB00305. Mitomycin.
    DB00665. Nilutamide.

    PTM databases

    PhosphoSitei P16435.

    Polymorphism databases

    DMDMi 2851393.

    Proteomic databases

    MaxQBi P16435.
    PaxDbi P16435.
    PRIDEi P16435.

    Protocols and materials databases

    DNASUi 5447.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000394893 ; ENSP00000378355 ; ENSG00000127948 .
    ENST00000412064 ; ENSP00000404731 ; ENSG00000127948 .
    ENST00000412521 ; ENSP00000409238 ; ENSG00000127948 .
    ENST00000414186 ; ENSP00000399327 ; ENSG00000127948 .
    ENST00000418341 ; ENSP00000389719 ; ENSG00000127948 .
    ENST00000432753 ; ENSP00000389409 ; ENSG00000127948 .
    ENST00000439963 ; ENSP00000390540 ; ENSG00000127948 .
    ENST00000449920 ; ENSP00000399556 ; ENSG00000127948 .
    ENST00000453773 ; ENSP00000395813 ; ENSG00000127948 .
    ENST00000454934 ; ENSP00000414263 ; ENSG00000127948 .
    ENST00000461988 ; ENSP00000419970 ; ENSG00000127948 .
    GeneIDi 5447.
    KEGGi hsa:5447.
    UCSCi uc011kge.2. human.

    Organism-specific databases

    CTDi 5447.
    GeneCardsi GC07P075528.
    GeneReviewsi POR.
    HGNCi HGNC:9208. POR.
    HPAi CAB004372.
    HPA010136.
    MIMi 124015. gene.
    201750. phenotype.
    613571. phenotype.
    neXtProti NX_P16435.
    Orphaneti 95699. Congenital adrenal hyperplasia due to cytochrome P450 oxidoreductase deficiency.
    PharmGKBi PA33532.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0369.
    HOGENOMi HOG000282027.
    HOVERGENi HBG000432.
    InParanoidi P16435.
    KOi K00327.
    OrthoDBi EOG7HQN7J.
    PhylomeDBi P16435.
    TreeFami TF105719.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS05140-MONOMER.
    SABIO-RK P16435.

    Miscellaneous databases

    ChiTaRSi POR. human.
    EvolutionaryTracei P16435.
    GeneWikii Cytochrome_P450_reductase.
    GenomeRNAii 5447.
    NextBioi 21083.
    PROi P16435.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16435.
    Bgeei P16435.
    CleanExi HS_POR.
    Genevestigatori P16435.

    Family and domain databases

    Gene3Di 1.20.990.10. 1 hit.
    3.40.50.360. 1 hit.
    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.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR023208. P450R.
    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 ]
    PIRSFi PIRSF000208. P450R. 1 hit.
    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. "Quantification of cytochrome P450 reductase gene expression in human tissues."
      Shephard E.A., Palmer C.N., Segall H.J., Phillips I.R.
      Arch. Biochem. Biophys. 294:168-172(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-500.
    2. "Polymorphism of human CYPOR: expression of new allele."
      Czerwinski M., Sahni M., Madan A., Parkinson A.
      Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    3. "cDNA cloning and characterization of NADPH-cytochrome P-450 reductase in human HL-60 cell."
      Murakami H.O., Ogawa H., Nisimoto Y.
      Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. NIEHS SNPs program
      Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-225; ASN-252 AND VAL-500.
    5. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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], VARIANTS LEU-225 AND VAL-500.
      Tissue: Lung.
    7. "Structural and functional analysis of NADPH-cytochrome P-450 reductase from human liver: complete sequence of human enzyme and NADPH-binding sites."
      Haniu M., McManus M.E., Birkett D.J., Lee T.D., Shively J.E.
      Biochemistry 28:8639-8645(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-677, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT GLY-2.
      Tissue: Liver.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Crystal structure of the FMN-binding domain of human cytochrome P450 reductase at 1.93 A resolution."
      Zhao Q., Modi S., Smith G., Paine M., McDonagh P.D., Wolf C.R., Tew D., Lian L.Y., Roberts G.C., Driessen H.P.
      Protein Sci. 8:298-306(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 62-242.
    10. "Compound heterozygous mutations of cytochrome P450 oxidoreductase gene (POR) in two patients with Antley-Bixler syndrome."
      Adachi M., Tachibana K., Asakura Y., Yamamoto T., Hanaki K., Oka A.
      Am. J. Med. Genet. A 128:333-339(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ABS1 HIS-454.
    11. "Cytochrome P450 oxidoreductase gene mutations and Antley-Bixler syndrome with abnormal genitalia and/or impaired steroidogenesis: molecular and clinical studies in 10 patients."
      Fukami M., Horikawa R., Nagai T., Tanaka T., Naiki Y., Sato N., Okuyama T., Nakai H., Soneda S., Tachibana K., Matsuo N., Sato S., Homma K., Nishimura G., Hasegawa T., Ogata T.
      J. Clin. Endocrinol. Metab. 90:414-426(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ABS1 HIS-454; CYS-575 AND 608-LEU--TRP-617 DELINS ARG, VARIANT VAL-500.
    12. "Congenital adrenal hyperplasia caused by mutant P450 oxidoreductase and human androgen synthesis: analytical study."
      Arlt W., Walker E.A., Draper N., Ivison H.E., Ride J.P., Hammer F., Chalder S.M., Borucka-Mankiewicz M., Hauffa B.P., Malunowicz E.M., Stewart P.M., Shackleton C.H.L.
      Lancet 363:2128-2135(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS DISPORD ASP-178; PRO-284; HIS-454 AND TYR-566, CHARACTERIZATION OF VARIANTS DISPORD ASP-178; PRO-284; HIS-454 AND TYR-566.
    13. "Mutant P450 oxidoreductase causes disordered steroidogenesis with and without Antley-Bixler syndrome."
      Flueck C.E., Tajima T., Pandey A.V., Arlt W., Okuhara K., Verge C.F., Jabs E.W., Mendonca B.B., Fujieda K., Miller W.L.
      Nat. Genet. 36:228-230(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ABS1 PRO-284; HIS-454 AND GLU-489, VARIANTS DISPORD TYR-566 AND PHE-605, CHARACTERIZATION OF VARIANTS ABS1 PRO-284; HIS-454 AND GLU-489, CHARACTERIZATION OF VARIANTS DISPORD TYR-566 AND PHE-605.

    Entry informationi

    Entry nameiNCPR_HUMAN
    AccessioniPrimary (citable) accession number: P16435
    Secondary accession number(s): Q16455
    , Q197M5, Q8N181, Q9H3M8, Q9UDT3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 172 of the entry and version 2 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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