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Protein

NADPH--cytochrome P450 reductase

Gene

POR

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

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

Protein has several cofactor binding sites:

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, FMN, NADP

Enzyme and pathway databases

BioCyciMetaCyc:HS05140-MONOMER.
BRENDAi1.6.2.4. 2681.
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 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:9208. POR.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • intracellular membrane-bounded organelle Source: UniProtKB
  • membrane Source: UniProtKB
  • mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Antley-Bixler syndrome, with genital anomalies and disordered steroidogenesis (ABS1)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:201750
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)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:613571
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.

Chemistry

DrugBankiDB00865. Benzphetamine.
DB00694. Daunorubicin.
DB00997. Doxorubicin.
DB01466. Ethylmorphine.
DB03147. Flavin adenine dinucleotide.
DB00166. Lipoic Acid.
DB00305. Mitomycin.
DB00665. Nilutamide.
DB00698. Nitrofurantoin.

Polymorphism and mutation databases

BioMutaiPOR.
DMDMi2851393.

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

BgeeiP16435.
CleanExiHS_POR.
ExpressionAtlasiP16435. baseline and differential.
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. 20 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 – 768Combined sources
Beta strandi79 – 857Combined sources
Beta strandi87 – 893Combined sources
Helixi90 – 10112Combined sources
Helixi102 – 1054Combined sources
Beta strandi109 – 1124Combined sources
Helixi114 – 1163Combined sources
Helixi119 – 1279Combined sources
Beta strandi132 – 1387Combined sources
Helixi141 – 1433Combined sources
Helixi147 – 1493Combined sources
Helixi150 – 1589Combined sources
Beta strandi167 – 1748Combined sources
Beta strandi178 – 1803Combined sources
Helixi183 – 19412Combined sources
Beta strandi198 – 2014Combined sources
Beta strandi204 – 2074Combined sources
Helixi212 – 23120Combined sources
Beta strandi245 – 2495Combined sources
Helixi255 – 2573Combined sources
Beta strandi259 – 2613Combined sources
Beta strandi263 – 2653Combined sources
Turni266 – 2705Combined sources
Beta strandi278 – 2803Combined sources
Beta strandi282 – 29110Combined sources
Beta strandi294 – 2985Combined sources
Beta strandi300 – 3067Combined sources
Beta strandi319 – 3224Combined sources
Helixi328 – 33811Combined sources
Beta strandi345 – 3528Combined sources
Beta strandi360 – 3667Combined sources
Helixi367 – 3737Combined sources
Helixi383 – 3897Combined sources
Helixi390 – 3923Combined sources
Helixi396 – 40611Combined sources
Beta strandi407 – 4093Combined sources
Helixi410 – 41910Combined sources
Turni420 – 4245Combined sources
Helixi427 – 4337Combined sources
Helixi441 – 4477Combined sources
Beta strandi454 – 4574Combined sources
Turni462 – 4643Combined sources
Beta strandi468 – 4747Combined sources
Beta strandi477 – 4793Combined sources
Beta strandi485 – 4873Combined sources
Helixi489 – 4957Combined sources
Beta strandi508 – 5147Combined sources
Beta strandi528 – 5314Combined sources
Helixi534 – 5374Combined sources
Helixi538 – 55316Combined sources
Beta strandi560 – 5678Combined sources
Turni569 – 5713Combined sources
Helixi576 – 5849Combined sources
Beta strandi587 – 5959Combined sources
Beta strandi598 – 6014Combined sources
Helixi605 – 6117Combined sources
Helixi613 – 6219Combined sources
Beta strandi625 – 6317Combined sources
Turni632 – 6343Combined sources
Helixi635 – 65016Combined sources
Helixi655 – 66713Combined sources
Beta strandi670 – 6767Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MGDSHVDTSS TVSEAVAEEV SLFSMTDMIL FSLIVGLLTY WFLFRKKKEE
60 70 80 90 100
VPEFTKIQTL TSSVRESSFV EKMKKTGRNI IVFYGSQTGT AEEFANRLSK
110 120 130 140 150
DAHRYGMRGM SADPEEYDLA DLSSLPEIDN ALVVFCMATY GEGDPTDNAQ
160 170 180 190 200
DFYDWLQETD VDLSGVKFAV FGLGNKTYEH FNAMGKYVDK RLEQLGAQRI
210 220 230 240 250
FELGLGDDDG NLEEDFITWR EQFWPAVCEH FGVEATGEES SIRQYELVVH
260 270 280 290 300
TDIDAAKVYM GEMGRLKSYE NQKPPFDAKN PFLAAVTTNR KLNQGTERHL
310 320 330 340 350
MHLELDISDS KIRYESGDHV AVYPANDSAL VNQLGKILGA DLDVVMSLNN
360 370 380 390 400
LDEESNKKHP FPCPTSYRTA LTYYLDITNP PRTNVLYELA QYASEPSEQE
410 420 430 440 450
LLRKMASSSG EGKELYLSWV VEARRHILAI LQDCPSLRPP IDHLCELLPR
460 470 480 490 500
LQARYYSIAS SSKVHPNSVH ICAVVVEYET KAGRINKGVA TNWLRAKEPA
510 520 530 540 550
GENGGRALVP MFVRKSQFRL PFKATTPVIM VGPGTGVAPF IGFIQERAWL
560 570 580 590 600
RQQGKEVGET LLYYGCRRSD EDYLYREELA QFHRDGALTQ LNVAFSREQS
610 620 630 640 650
HKVYVQHLLK QDREHLWKLI EGGAHIYVCG DARNMARDVQ NTFYDIVAEL
660 670
GAMEHAQAVD YIKKLMTKGR YSLDVWS
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.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti405 – 4051M → L in BAB18572 (Ref. 3) Curated
Sequence conflicti518 – 5181F → L in AAB21814 (PubMed:1550342).Curated
Sequence conflicti518 – 5181F → L in BAB18572 (Ref. 3) Curated
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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi111443. 20 interactions.
DIPiDIP-29682N.
IntActiP16435. 5 interactions.
MINTiMINT-1212161.
STRINGi9606.ENSP00000265302.

Chemistry

ChEMBLiCHEMBL2169731.
DrugBankiDB00865. Benzphetamine.
DB00694. Daunorubicin.
DB00997. Doxorubicin.
DB01466. Ethylmorphine.
DB03147. Flavin adenine dinucleotide.
DB00166. Lipoic Acid.
DB00305. Mitomycin.
DB00665. Nilutamide.
DB00698. Nitrofurantoin.

PTM databases

PhosphoSiteiP16435.

Polymorphism and mutation databases

BioMutaiPOR.
DMDMi2851393.

Proteomic databases

MaxQBiP16435.
PaxDbiP16435.
PRIDEiP16435.

Protocols and materials databases

DNASUi5447.
Structural Biology KnowledgebaseSearch...

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.

Organism-specific databases

CTDi5447.
GeneCardsiGC07P075528.
GeneReviewsiPOR.
HGNCiHGNC:9208. POR.
HPAiCAB004372.
HPA010136.
MIMi124015. gene.
201750. phenotype.
613571. phenotype.
neXtProtiNX_P16435.
Orphaneti95699. Congenital adrenal hyperplasia due to cytochrome P450 oxidoreductase deficiency.
PharmGKBiPA33532.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciMetaCyc:HS05140-MONOMER.
BRENDAi1.6.2.4. 2681.
SABIO-RKP16435.

Miscellaneous databases

ChiTaRSiPOR. human.
EvolutionaryTraceiP16435.
GeneWikiiCytochrome_P450_reductase.
GenomeRNAii5447.
NextBioi21083.
PROiP16435.
SOURCEiSearch...

Gene expression databases

BgeeiP16435.
CleanExiHS_POR.
ExpressionAtlasiP16435. baseline and differential.
GenevestigatoriP16435.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. "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: April 29, 2015
This is version 178 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.