UniProtKB - P16435 (NCPR_HUMAN)

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History
Entry version 209 (18 Jul 2018)
Sequence version 2 (23 Jan 2007)
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Protein

NADPH--cytochrome P450 reductase

Gene

POR

Organism

Homo sapiens (Human)

Status

Reviewed-Annotation score: -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.UniRule annotation

Catalytic activityⁱ

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

Cofactorⁱ

Protein has several cofactor binding sites:

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	208	FMNUniRule annotation2 Publications	1
Binding siteⁱ	298	NADPUniRule annotation1 Publication	1
Binding siteⁱ	424	FADUniRule annotation2 Publications	1
Binding siteⁱ	478	FADUniRule annotation2 Publications	1
Binding siteⁱ	535	NADPUniRule annotation1 Publication	1
Binding siteⁱ	638	NADPUniRule annotation1 Publication	1
Binding siteⁱ	676	FADUniRule annotation2 Publications	1

Regions

Feature key	Position(s)	DescriptionActions	Length
Nucleotide bindingⁱ	86 – 91	FMNUniRule annotation2 Publications	6
Nucleotide bindingⁱ	138 – 141	FMNUniRule annotation2 Publications	4
Nucleotide bindingⁱ	173 – 182	FMNUniRule annotation2 Publications	10
Nucleotide bindingⁱ	454 – 457	FADUniRule annotation2 Publications	4
Nucleotide bindingⁱ	472 – 474	FADUniRule annotation2 Publications	3
Nucleotide bindingⁱ	488 – 491	FADUniRule annotation2 Publications	4
Nucleotide bindingⁱ	596 – 597	NADPUniRule annotation1 Publication	2
Nucleotide bindingⁱ	602 – 606	NADPUniRule annotation1 Publication	5

GO - Molecular functionⁱ

cytochrome-b5 reductase activity, acting on NAD(P)H Source: Ensembl
electron transfer activity Source: Ensembl
enzyme binding Source: Ensembl
flavin adenine dinucleotide binding Source: Ensembl
FMN binding Source: Ensembl
hydrolase activity Source: Ensembl
iron-cytochrome-c reductase activity Source: Ensembl
NADP binding Source: Ensembl
NADPH-hemoprotein reductase activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 19448135
nitric oxide dioxygenase activity Source: Ensembl

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

carnitine metabolic process Source: Ensembl
cellular organofluorine metabolic process
Source: BHF-UCL
Inferred from direct assayⁱ
- 19448135
cellular response to follicle-stimulating hormone stimulus Source: Ensembl
cellular response to peptide hormone stimulus Source: Ensembl
demethylation Source: Ensembl
fatty acid oxidation Source: Ensembl
flavonoid metabolic process Source: Ensembl
internal peptidyl-lysine acetylation Source: Ensembl
negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
negative regulation of lipase activity Source: Ensembl
nitrate catabolic process Source: Ensembl
nitric oxide catabolic process Source: Ensembl
oxidation-reduction process
Source: BHF-UCL
Inferred from direct assayⁱ
- 19448135
positive regulation of cholesterol biosynthetic process Source: Ensembl
positive regulation of chondrocyte differentiation Source: Ensembl
positive regulation of monooxygenase activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 19448135
positive regulation of smoothened signaling pathway Source: Ensembl
positive regulation of steroid hormone biosynthetic process Source: Ensembl
regulation of growth plate cartilage chondrocyte proliferation Source: Ensembl
response to drug Source: Ensembl
response to nutrient Source: Ensembl
xenobiotic metabolic process Source: Reactome

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Ligand	FAD, Flavoprotein, FMN, NADP

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS05140-MONOMER
BRENDAⁱ	1.6.2.4 2681
Reactomeⁱ	R-HSA-211897 Cytochrome P450 - arranged by substrate type
SABIO-RKⁱ	P16435
SIGNORⁱ	P16435

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: NADPH--cytochrome P450 reductaseUniRule annotation (EC:1.6.2.4UniRule annotation) Short name: CPRUniRule annotation Short name: P450RUniRule annotation
Gene namesⁱ	Name:PORUniRule annotation Synonyms:CYPOR
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 7

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000127948.13
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:9208 POR
MIMⁱ	124015 gene
neXtProtⁱ	NX_P16435

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	2 – 21	LumenalUniRule annotationAdd BLAST	20
Transmembraneⁱ	22 – 42	HelicalUniRule annotationAdd BLAST	21
Topological domainⁱ	43 – 677	CytoplasmicUniRule annotationAdd BLAST	635

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.

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_021157	489	V → E in ABS1; significant reduction of activity. 1 Publication	1
Natural variantⁱVAR_021159	575	Y → C in ABS1. 1 Publication	1
Natural variantⁱVAR_021161	609 – 617	LKQDREHLW → R in ABS1.	9

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.

Keywords - Diseaseⁱ

Congenital adrenal hyperplasia, Craniosynostosis, Disease mutation

Organism-specific databases

DisGeNET More...DisGeNETⁱ	5447
GeneReviewsⁱ	POR
MalaCards human disease database More...MalaCardsⁱ	POR
MIMⁱ	201750 phenotype 613571 phenotype
Orphanetⁱ	95699 Congenital adrenal hyperplasia due to cytochrome P450 oxidoreductase deficiency
PharmGKBⁱ	PA33532

Chemistry databases

ChEMBLⁱ	CHEMBL2169731
Drug and drug target database More...DrugBankⁱ	DB03461 2'-Monophosphoadenosine 5'-Diphosphoribose DB00865 Benzphetamine DB00694 Daunorubicin DB00997 Doxorubicin DB01466 Ethylmorphine DB03147 Flavin adenine dinucleotide DB00166 Lipoic Acid DB00305 Mitomycin DB00665 Nilutamide DB00698 Nitrofurantoin DB03247 Riboflavin Monophosphate

Polymorphism and mutation databases

BioMutaⁱ	POR
DMDMⁱ	2851393

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed1 Publication
ChainⁱPRO_0000167596	2 – 677	NADPH--cytochrome P450 reductaseAdd BLAST		676

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	2	N-acetylglycine1 Publication		1
Modified residueⁱ	63	PhosphoserineCombined sources		1

Keywords - PTMⁱ

Acetylation, Phosphoprotein

Proteomic databases

EPDⁱ	P16435
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P16435
PaxDbⁱ	P16435
PeptideAtlas More...PeptideAtlasⁱ	P16435
PRIDEⁱ	P16435
ProteomicsDBⁱ	53360

PTM databases

iPTMnetⁱ	P16435
PhosphoSitePlusⁱ	P16435
SwissPalmⁱ	P16435

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000127948
CleanExⁱ	HS_POR
ExpressionAtlasⁱ	P16435 baseline and differential
Genevisibleⁱ	P16435 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB004372 HPA010136

HPAⁱ

CAB004372
HPA010136

Interactionⁱ

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
CYP2C2	P00181	4	EBI-726554,EBI-4320576	From Oryctolagus cuniculus.
PGRMC1	O00264	5	EBI-726554,EBI-1045534

Show more details

GO - Molecular functionⁱ

enzyme binding Source: Ensembl

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	111443, 37 interactors
Database of interacting proteins More...DIPⁱ	DIP-29682N
IntActⁱ	P16435, 12 interactors
Molecular INTeraction database More...MINTⁱ	P16435
STRINGⁱ	9606.ENSP00000419970

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	69 – 76	Combined sources	8
Beta strandⁱ	79 – 85	Combined sources	7
Beta strandⁱ	87 – 89	Combined sources	3
Helixⁱ	90 – 101	Combined sources	12
Helixⁱ	102 – 105	Combined sources	4
Beta strandⁱ	109 – 112	Combined sources	4
Helixⁱ	114 – 116	Combined sources	3
Helixⁱ	119 – 127	Combined sources	9
Beta strandⁱ	132 – 138	Combined sources	7
Helixⁱ	141 – 143	Combined sources	3
Helixⁱ	147 – 149	Combined sources	3
Helixⁱ	150 – 158	Combined sources	9
Beta strandⁱ	167 – 174	Combined sources	8
Beta strandⁱ	178 – 180	Combined sources	3
Helixⁱ	183 – 194	Combined sources	12
Beta strandⁱ	198 – 201	Combined sources	4
Beta strandⁱ	204 – 207	Combined sources	4
Turnⁱ	208 – 210	Combined sources	3
Helixⁱ	212 – 231	Combined sources	20
Beta strandⁱ	245 – 249	Combined sources	5
Helixⁱ	255 – 257	Combined sources	3
Beta strandⁱ	259 – 261	Combined sources	3
Beta strandⁱ	263 – 265	Combined sources	3
Turnⁱ	266 – 270	Combined sources	5
Beta strandⁱ	278 – 280	Combined sources	3
Beta strandⁱ	282 – 291	Combined sources	10
Beta strandⁱ	294 – 298	Combined sources	5
Beta strandⁱ	300 – 306	Combined sources	7
Beta strandⁱ	319 – 322	Combined sources	4
Helixⁱ	328 – 338	Combined sources	11
Beta strandⁱ	345 – 352	Combined sources	8
Beta strandⁱ	360 – 366	Combined sources	7
Helixⁱ	367 – 373	Combined sources	7
Helixⁱ	383 – 389	Combined sources	7
Helixⁱ	390 – 392	Combined sources	3
Helixⁱ	396 – 406	Combined sources	11
Beta strandⁱ	407 – 409	Combined sources	3
Helixⁱ	410 – 419	Combined sources	10
Turnⁱ	420 – 424	Combined sources	5
Helixⁱ	427 – 433	Combined sources	7
Helixⁱ	441 – 447	Combined sources	7
Beta strandⁱ	454 – 457	Combined sources	4
Turnⁱ	462 – 464	Combined sources	3
Beta strandⁱ	468 – 474	Combined sources	7
Beta strandⁱ	477 – 479	Combined sources	3
Beta strandⁱ	485 – 487	Combined sources	3
Helixⁱ	489 – 495	Combined sources	7
Turnⁱ	501 – 503	Combined sources	3
Beta strandⁱ	508 – 514	Combined sources	7
Beta strandⁱ	528 – 531	Combined sources	4
Helixⁱ	534 – 537	Combined sources	4
Helixⁱ	538 – 553	Combined sources	16
Beta strandⁱ	560 – 567	Combined sources	8
Turnⁱ	569 – 571	Combined sources	3
Helixⁱ	576 – 584	Combined sources	9
Beta strandⁱ	587 – 595	Combined sources	9
Beta strandⁱ	598 – 601	Combined sources	4
Helixⁱ	605 – 611	Combined sources	7
Helixⁱ	613 – 621	Combined sources	9
Beta strandⁱ	625 – 631	Combined sources	7
Turnⁱ	632 – 634	Combined sources	3
Helixⁱ	635 – 650	Combined sources	16
Helixⁱ	655 – 667	Combined sources	13
Beta strandⁱ	670 – 676	Combined sources	7

3D structure databases

ProteinModelPortalⁱ	P16435
SMRⁱ	P16435
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P16435

EvolutionaryTraceⁱ

P16435

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	80 – 224	Flavodoxin-likeUniRule annotationAdd BLAST		145
Domainⁱ	279 – 521	FAD-binding FR-typeUniRule annotationAdd BLAST		243

Sequence similaritiesⁱ

Belongs to the NADPH--cytochrome P450 reductase family.UniRule annotation

In the N-terminal section; belongs to the flavodoxin family.UniRule annotation

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

Keywords - Domainⁱ

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG1158 Eukaryota COG0369 LUCA
HOGENOMⁱ	HOG000282027
HOVERGENⁱ	HBG000432
InParanoidⁱ	P16435
KEGG Orthology (KO) More...KOⁱ	K00327
PhylomeDBⁱ	P16435
TreeFamⁱ	TF105719

Family and domain databases

Gene3Dⁱ	1.20.990.10, 4 hits 3.40.50.360, 1 hit 3.40.50.80, 1 hit
HAMAPⁱ	MF_03212 NCPR, 1 hit
InterProⁱ	View protein in InterPro IPR003097 FAD-binding_1 IPR017927 Fd_Rdtase_FAD-bd IPR001094 Flavdoxin-like IPR008254 Flavodoxin/NO_synth IPR001709 Flavoprot_Pyr_Nucl_cyt_Rdtase IPR029039 Flavoprotein-like_sf IPR039261 FNR_nucleotide_bd IPR023173 NADPH_Cyt_P450_Rdtase_alpha IPR001433 OxRdtase_FAD/NAD-bd IPR023208 P450R IPR017938 Riboflavin_synthase-like_b-brl
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00667 FAD_binding_1, 1 hit PF00258 Flavodoxin_1, 1 hit PF00175 NAD_binding_1, 1 hit
PIRSFⁱ	PIRSF000208 P450R, 1 hit
PRINTSⁱ	PR00369 FLAVODOXIN PR00371 FPNCR
SUPFAMⁱ	SSF52218 SSF52218, 1 hit SSF52343 SSF52343, 1 hit SSF63380 SSF63380, 1 hit
PROSITEⁱ	View protein in PROSITE PS51384 FAD_FR, 1 hit PS50902 FLAVODOXIN_LIKE, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P16435-1 [UniParc]FASTA Add 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

Sequence cautionⁱ

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

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	405	M → L in BAB18572 (Ref. 3) Curated	1
Sequence conflictⁱ	518	F → L in AAB21814 (PubMed:1550342).Curated	1
Sequence conflictⁱ	518	F → L in BAB18572 (Ref. 3) Curated	1
Sequence conflictⁱ	537 – 538	VA → WH in AAB21814 (PubMed:1550342).Curated	2

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_021154	178	Y → D in DISPORD; complete loss of activity. 1 Publication	1
Natural variantⁱVAR_047885	225	P → L2 Publications	1
Natural variantⁱVAR_047886	252	D → N1 Publication	1
Natural variantⁱVAR_021155	284	A → P in ABS1 and DISPORD; significant reduction of activity. 2 Publications	1
Natural variantⁱVAR_021156	454	R → H in ABS1 and DISPORD; significant reduction of activity. 5 Publications	1
Natural variantⁱVAR_021157	489	V → E in ABS1; significant reduction of activity. 1 Publication	1
Natural variantⁱVAR_004617	500	A → V4 PublicationsCorresponds to variant dbSNP:rs1057868Ensembl.	1
Natural variantⁱVAR_004618	551	R → Q.	1
Natural variantⁱVAR_021158	566	C → Y in DISPORD; significant reduction of activity. 2 Publications	1
Natural variantⁱVAR_021159	575	Y → C in ABS1. 1 Publication	1
Natural variantⁱVAR_021160	605	V → F in DISPORD; significant reduction of activity. 1 Publication	1
Natural variantⁱVAR_021161	609 – 617	LKQDREHLW → R in ABS1.	9

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.
PIRⁱ	A33421 A60557
NCBI Reference Sequences More...RefSeqⁱ	NP_000932.3, NM_000941.2
UniGeneⁱ	Hs.354056

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
UCSC genome browser More...UCSCⁱ	uc003udy.4 human

Keywords - Coding sequence diversityⁱ

Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length
P16435	Uncharacterized protein (Fragment)		HUMAN		686
POR isoform 14 (Fragment)		PANTR		188
UPI000013D5F4		HUMAN		680
POR isoform 18 (Fragment)		PANTR		146
POR isoform 16 (Fragment)		PANTR		172
+1

Protein	Similar proteins		Species	Score	Length
P16435	NADPH--cytochrome P450 reductase	)	RAT		678
UPI000766F3A6		MYODS		796
UPI000CCC5A02		MYOLU		744
NADPH--cytochrome P450 reductase		MYOBR		731
UPI0009428D63		Chinese rufous horseshoe bat		713
+159

Protein	Similar proteins		Species	Score	Length
P16435	NADPH--cytochrome P450 reductase	)	RAT		678
UPI000766F3A6		MYODS		796
UPI000CCC5A02		MYOLU		744
NADPH--cytochrome P450 reductase		MYOBR		731
UPI0009428D63		Chinese rufous horseshoe bat		713
+194

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	[»]
5EMN	X-ray	2.20	A/B	64-677	[»]
5FA6	X-ray	2.30	A/B	64-677	[»]
ProteinModelPortalⁱ	P16435
SMRⁱ	P16435
ModBaseⁱ	Search...
MobiDBⁱ	Search...

The DNASU plasmid repository More...DNASUⁱ	5447
Structural Biology Knowledgebase	Search...

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
UCSC genome browser More...UCSCⁱ	uc003udy.4 human

CTDⁱ	5447
DisGeNET More...DisGeNETⁱ	5447
EuPathDBⁱ	HostDB:ENSG00000127948.13
GeneCardsⁱ	POR
GeneReviewsⁱ	POR
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:9208 POR
Human Protein Atlas More...HPAⁱ	CAB004372 HPA010136
MalaCards human disease database More...MalaCardsⁱ	POR
MIMⁱ	124015 gene 201750 phenotype 613571 phenotype
neXtProtⁱ	NX_P16435
Orphanetⁱ	95699 Congenital adrenal hyperplasia due to cytochrome P450 oxidoreductase deficiency
PharmGKBⁱ	PA33532
GenAtlas: human gene database More...GenAtlasⁱ	Search...

ChiTaRSⁱ	POR human
EvolutionaryTraceⁱ	P16435
GeneWikiⁱ	Cytochrome_P450_reductase
GenomeRNAiⁱ	5447
Protein Ontology More...PROⁱ	PR:P16435
SOURCEⁱ	Search...

Entry informationⁱ

Entry nameⁱ	NCPR_HUMAN
Accessionⁱ	P16435Primary (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:	July 18, 2018
	This is version 209 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

Human chromosome 7
Human chromosome 7: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

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Annotation systems

Supporting data

UniProtKB - P16435 (NCPR_HUMAN)

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NADPH--cytochrome P450 reductase

POR

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Endoplasmic reticulum

Endoplasmic reticulum

Mitochondrion

Other locations

Topology

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Natural variant

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

UniProt is an ELIXIR core data resource

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ