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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.UniRule annotation

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei208FMNUniRule annotation2 Publications1
Binding sitei298NADPUniRule annotation1 Publication1
Binding sitei424FADUniRule annotation2 Publications1
Binding sitei478FADUniRule annotation2 Publications1
Binding sitei535NADPUniRule annotation1 Publication1
Binding sitei638NADPUniRule annotation1 Publication1
Binding sitei676FADUniRule annotation2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi86 – 91FMNUniRule annotation2 Publications6
Nucleotide bindingi138 – 141FMNUniRule annotation2 Publications4
Nucleotide bindingi173 – 182FMNUniRule annotation2 Publications10
Nucleotide bindingi454 – 457FADUniRule annotation2 Publications4
Nucleotide bindingi472 – 474FADUniRule annotation2 Publications3
Nucleotide bindingi488 – 491FADUniRule annotation2 Publications4
Nucleotide bindingi596 – 597NADPUniRule annotation1 Publication2
Nucleotide bindingi602 – 606NADPUniRule annotation1 Publication5

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.
ZFISH:HS05140-MONOMER.
BRENDAi1.6.2.4. 2681.
ReactomeiR-HSA-211897. Cytochrome P450 - arranged by substrate type.
SABIO-RKP16435.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:9208. POR.

Subcellular locationi

  • Endoplasmic reticulum membrane UniRule annotation; Single-pass membrane protein UniRule annotation; Cytoplasmic side UniRule annotation

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 21LumenalUniRule annotationAdd BLAST20
Transmembranei22 – 42HelicalUniRule annotationAdd BLAST21
Topological domaini43 – 677CytoplasmicUniRule annotationAdd BLAST635

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: Reactome
  • integral component of membrane Source: UniProtKB-KW
  • 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)DescriptionActionsGraphical viewLength
Natural variantiVAR_021155284A → P in ABS1 and DISPORD; significant reduction of activity. 2 Publications1
Natural variantiVAR_021156454R → H in ABS1 and DISPORD; significant reduction of activity. 4 Publications1
Natural variantiVAR_021157489V → E in ABS1; significant reduction of activity. 1 Publication1
Natural variantiVAR_021159575Y → C in ABS1. 1 Publication1
Natural variantiVAR_021161609 – 617LKQDREHLW → 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.
See also OMIM:613571
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_021154178Y → D in DISPORD; complete loss of activity. 1 Publication1
Natural variantiVAR_021155284A → P in ABS1 and DISPORD; significant reduction of activity. 2 Publications1
Natural variantiVAR_021156454R → H in ABS1 and DISPORD; significant reduction of activity. 4 Publications1
Natural variantiVAR_021158566C → Y in DISPORD; significant reduction of activity. 2 Publications1
Natural variantiVAR_021160605V → F in DISPORD; significant reduction of activity. 1 Publication1

Keywords - Diseasei

Congenital adrenal hyperplasia, Craniosynostosis, Disease mutation

Organism-specific databases

DisGeNETi5447.
MalaCardsiPOR.
MIMi201750. phenotype.
613571. phenotype.
Orphaneti95699. Congenital adrenal hyperplasia due to cytochrome P450 oxidoreductase deficiency.
PharmGKBiPA33532.

Chemistry databases

ChEMBLiCHEMBL2169731.
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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001675962 – 677NADPH--cytochrome P450 reductaseAdd BLAST676

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylglycine1 Publication1
Modified residuei63PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP16435.
MaxQBiP16435.
PaxDbiP16435.
PeptideAtlasiP16435.
PRIDEiP16435.

PTM databases

iPTMnetiP16435.
PhosphoSitePlusiP16435.
SwissPalmiP16435.

Expressioni

Gene expression databases

BgeeiENSG00000127948.
CleanExiHS_POR.
ExpressionAtlasiP16435. baseline and differential.
GenevisibleiP16435. HS.

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. 34 interactors.
DIPiDIP-29682N.
IntActiP16435. 10 interactors.
MINTiMINT-1212161.
STRINGi9606.ENSP00000419970.

Structurei

Secondary structure

1677
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi69 – 76Combined sources8
Beta strandi79 – 85Combined sources7
Beta strandi87 – 89Combined sources3
Helixi90 – 101Combined sources12
Helixi102 – 105Combined sources4
Beta strandi109 – 112Combined sources4
Helixi114 – 116Combined sources3
Helixi119 – 127Combined sources9
Beta strandi132 – 138Combined sources7
Helixi141 – 143Combined sources3
Helixi147 – 149Combined sources3
Helixi150 – 158Combined sources9
Beta strandi167 – 174Combined sources8
Beta strandi178 – 180Combined sources3
Helixi183 – 194Combined sources12
Beta strandi198 – 201Combined sources4
Beta strandi204 – 207Combined sources4
Turni208 – 210Combined sources3
Helixi212 – 231Combined sources20
Beta strandi245 – 249Combined sources5
Helixi255 – 257Combined sources3
Beta strandi259 – 261Combined sources3
Beta strandi263 – 265Combined sources3
Turni266 – 270Combined sources5
Beta strandi278 – 280Combined sources3
Beta strandi282 – 291Combined sources10
Beta strandi294 – 298Combined sources5
Beta strandi300 – 306Combined sources7
Beta strandi319 – 322Combined sources4
Helixi328 – 338Combined sources11
Beta strandi345 – 352Combined sources8
Beta strandi360 – 366Combined sources7
Helixi367 – 373Combined sources7
Helixi383 – 389Combined sources7
Helixi390 – 392Combined sources3
Helixi396 – 406Combined sources11
Beta strandi407 – 409Combined sources3
Helixi410 – 419Combined sources10
Turni420 – 424Combined sources5
Helixi427 – 433Combined sources7
Helixi441 – 447Combined sources7
Beta strandi454 – 457Combined sources4
Turni462 – 464Combined sources3
Beta strandi468 – 474Combined sources7
Beta strandi477 – 479Combined sources3
Beta strandi485 – 487Combined sources3
Helixi489 – 495Combined sources7
Turni501 – 503Combined sources3
Beta strandi508 – 514Combined sources7
Beta strandi528 – 531Combined sources4
Helixi534 – 537Combined sources4
Helixi538 – 553Combined sources16
Beta strandi560 – 567Combined sources8
Turni569 – 571Combined sources3
Helixi576 – 584Combined sources9
Beta strandi587 – 595Combined sources9
Beta strandi598 – 601Combined sources4
Helixi605 – 611Combined sources7
Helixi613 – 621Combined sources9
Beta strandi625 – 631Combined sources7
Turni632 – 634Combined sources3
Helixi635 – 650Combined sources16
Helixi655 – 667Combined sources13
Beta strandi670 – 676Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5EMNX-ray2.20A/B64-677[»]
5FA6X-ray2.30A/B64-677[»]
ProteinModelPortaliP16435.
SMRiP16435.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16435.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini80 – 224Flavodoxin-likeUniRule annotationAdd BLAST145
Domaini279 – 521FAD-binding FR-typeUniRule annotationAdd BLAST243

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
Contains 1 FAD-binding FR-type domain.UniRule annotation
Contains 1 flavodoxin-like domain.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1158. Eukaryota.
COG0369. LUCA.
HOGENOMiHOG000282027.
HOVERGENiHBG000432.
InParanoidiP16435.
KOiK00327.
PhylomeDBiP16435.
TreeFamiTF105719.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
HAMAPiMF_03212. NCPR. 1 hit.
InterProiIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like_dom.
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti405M → L in BAB18572 (Ref. 3) Curated1
Sequence conflicti518F → L in AAB21814 (PubMed:1550342).Curated1
Sequence conflicti518F → L in BAB18572 (Ref. 3) Curated1
Sequence conflicti537 – 538VA → WH in AAB21814 (PubMed:1550342).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_021154178Y → D in DISPORD; complete loss of activity. 1 Publication1
Natural variantiVAR_047885225P → L.2 Publications1
Natural variantiVAR_047886252D → N.1 Publication1
Natural variantiVAR_021155284A → P in ABS1 and DISPORD; significant reduction of activity. 2 Publications1
Natural variantiVAR_021156454R → H in ABS1 and DISPORD; significant reduction of activity. 4 Publications1
Natural variantiVAR_021157489V → E in ABS1; significant reduction of activity. 1 Publication1
Natural variantiVAR_004617500A → V.4 PublicationsCorresponds to variant rs1057868dbSNPEnsembl.1
Natural variantiVAR_004618551R → Q.1
Natural variantiVAR_021158566C → Y in DISPORD; significant reduction of activity. 2 Publications1
Natural variantiVAR_021159575Y → C in ABS1. 1 Publication1
Natural variantiVAR_021160605V → F in DISPORD; significant reduction of activity. 1 Publication1
Natural variantiVAR_021161609 – 617LKQDREHLW → 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.
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.
UCSCiuc003udy.4. 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
PDB 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[»]
5EMNX-ray2.20A/B64-677[»]
5FA6X-ray2.30A/B64-677[»]
ProteinModelPortaliP16435.
SMRiP16435.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111443. 34 interactors.
DIPiDIP-29682N.
IntActiP16435. 10 interactors.
MINTiMINT-1212161.
STRINGi9606.ENSP00000419970.

Chemistry databases

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

PTM databases

iPTMnetiP16435.
PhosphoSitePlusiP16435.
SwissPalmiP16435.

Polymorphism and mutation databases

BioMutaiPOR.
DMDMi2851393.

Proteomic databases

EPDiP16435.
MaxQBiP16435.
PaxDbiP16435.
PeptideAtlasiP16435.
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.
UCSCiuc003udy.4. human.

Organism-specific databases

CTDi5447.
DisGeNETi5447.
GeneCardsiPOR.
GeneReviewsiPOR.
HGNCiHGNC:9208. POR.
HPAiCAB004372.
HPA010136.
MalaCardsiPOR.
MIMi124015. gene.
201750. phenotype.
613571. phenotype.
neXtProtiNX_P16435.
Orphaneti95699. Congenital adrenal hyperplasia due to cytochrome P450 oxidoreductase deficiency.
PharmGKBiPA33532.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1158. Eukaryota.
COG0369. LUCA.
HOGENOMiHOG000282027.
HOVERGENiHBG000432.
InParanoidiP16435.
KOiK00327.
PhylomeDBiP16435.
TreeFamiTF105719.

Enzyme and pathway databases

BioCyciMetaCyc:HS05140-MONOMER.
ZFISH:HS05140-MONOMER.
BRENDAi1.6.2.4. 2681.
ReactomeiR-HSA-211897. Cytochrome P450 - arranged by substrate type.
SABIO-RKP16435.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000127948.
CleanExiHS_POR.
ExpressionAtlasiP16435. baseline and differential.
GenevisibleiP16435. HS.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
HAMAPiMF_03212. NCPR. 1 hit.
InterProiIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like_dom.
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...

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: November 30, 2016
This is version 194 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

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 one 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.