P16435 (NCPR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
NADPH--cytochrome P450 reductase
Short name=CPR
Short name=P450R
EC=1.6.2.4

Gene names

Name:	POR
Synonyms:	CYPOR

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	677 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein.
Cofactor	FAD. FMN.
Subcellular location	Endoplasmic reticulum membrane; Peripheral membrane protein. Note: Anchored to the ER membrane by its N-terminal hydrophobic region.
Involvement in disease	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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.11 Ref.13 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.13
Sequence similarities	In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. Contains 1 FAD-binding FR-type domain. Contains 1 flavodoxin-like domain.
Sequence caution	The sequence AAH34277.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Disease	Congenital adrenal hyperplasia Craniosynostosis Disease mutation
Ligand	FAD FMN Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	carnitine metabolic process Inferred from electronic annotation. Source: Compara cellular organofluorine metabolic process Inferred from direct assay PubMed 19448135. Source: BHF-UCL cellular response to follicle-stimulating hormone stimulus Inferred from electronic annotation. Source: Compara cellular response to peptide hormone stimulus Inferred from electronic annotation. Source: Compara demethylation Inferred from electronic annotation. Source: Compara fatty acid oxidation Inferred from electronic annotation. Source: Compara flavonoid metabolic process Inferred from electronic annotation. Source: Compara internal peptidyl-lysine acetylation Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of lipase activity Inferred from electronic annotation. Source: Compara nitrate catabolic process Inferred from electronic annotation. Source: Compara nitric oxide catabolic process Inferred from electronic annotation. Source: Compara positive regulation of cholesterol biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of chondrocyte differentiation Inferred from electronic annotation. Source: Compara positive regulation of monooxygenase activity Inferred from direct assay PubMed 19448135. Source: BHF-UCL positive regulation of smoothened signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of steroid hormone biosynthetic process Inferred from electronic annotation. Source: Compara regulation of growth plate cartilage chondrocyte proliferation Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to nutrient Inferred from electronic annotation. Source: Compara
Cellular_component	endoplasmic reticulum Traceable author statement. Source: UniProtKB endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	FMN binding Inferred from electronic annotation. Source: Compara NADP binding Inferred from electronic annotation. Source: Compara NADPH-hemoprotein reductase activity Traceable author statement Ref.9Ref.7. Source: UniProtKB cytochrome-b5 reductase activity, acting on NAD(P)H Inferred from electronic annotation. Source: Compara electron carrier activity Inferred from electronic annotation. Source: Compara flavin adenine dinucleotide binding Inferred from electronic annotation. Source: Compara hydrolase activity Inferred from electronic annotation. Source: Compara iron ion binding Inferred from electronic annotation. Source: InterPro iron-cytochrome-c reductase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 677

676

NADPH--cytochrome P450 reductase

PRO_0000167596

Regions

Domain

80 – 224

145

Flavodoxin-like

Domain

279 – 521

243

FAD-binding FR-type

Nucleotide binding

170 – 201

32

FMN By similarity

Nucleotide binding

314 – 325

12

FAD By similarity

Nucleotide binding

451 – 461

11

FAD By similarity

Nucleotide binding

529 – 547

19

NADP By similarity

Nucleotide binding

623 – 639

17

NADP By similarity

Amino acid modifications

Modified residue

2

1

N-acetylglycine

Modified residue

575

1

Phosphotyrosine By similarity

Natural variations

Natural variant

178

1

Y → D in DISPORD; complete loss of activity. Ref.12

VAR_021154

Natural variant

225

1

P → L. Ref.4 Ref.6

VAR_047885

Natural variant

252

1

D → N. Ref.4

VAR_047886

Natural variant

284

1

A → P in ABS1 and DISPORD; significant reduction of activity. Ref.12 Ref.13

VAR_021155

Natural variant

454

1

R → H in ABS1 and DISPORD; significant reduction of activity. Ref.10 Ref.11 Ref.12 Ref.13

VAR_021156

Natural variant

489

1

V → E in ABS1; significant reduction of activity. Ref.13

VAR_021157

Natural variant

500

1

A → V. Ref.1 Ref.4 Ref.6 Ref.11
Corresponds to variant rs1057868 [ dbSNP | Ensembl ].

VAR_004617

Natural variant

551

1

R → Q.

VAR_004618

Natural variant

566

1

C → Y in DISPORD; significant reduction of activity. Ref.12 Ref.13

VAR_021158

Natural variant

575

1

Y → C in ABS1. Ref.11

VAR_021159

Natural variant

605

1

V → F in DISPORD; significant reduction of activity. Ref.13

VAR_021160

Natural variant

609 – 617

9

LKQDREHLW → R in ABS1.

VAR_021161

Experimental info

Sequence conflict

405

1

M → L in BAB18572. Ref.3

Sequence conflict

518

1

F → L in AAB21814. Ref.1

Sequence conflict

518

1

F → L in BAB18572. Ref.3

Sequence conflict

537 – 538

2

VA → WH in AAB21814. Ref.1

Secondary structure

1

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677

Helix Strand Turn

Details...

Helix

69 – 76

8

Beta strand

79 – 85

7

Beta strand

87 – 89

3

Helix

90 – 101

12

Helix

102 – 105

4

Beta strand

109 – 112

4

Helix

114 – 116

3

Helix

119 – 127

9

Beta strand

132 – 138

7

Helix

141 – 143

3

Helix

147 – 149

3

Helix

150 – 158

9

Beta strand

167 – 174

8

Beta strand

178 – 180

3

Helix

183 – 194

12

Beta strand

198 – 201

4

Beta strand

204 – 207

4

Helix

212 – 231

20

Beta strand

245 – 249

5

Helix

255 – 257

3

Beta strand

259 – 261

3

Beta strand

263 – 265

3

Turn

266 – 270

5

Beta strand

278 – 280

3

Beta strand

282 – 291

10

Beta strand

294 – 298

5

Beta strand

300 – 306

7

Beta strand

319 – 322

4

Helix

328 – 338

11

Beta strand

345 – 352

8

Beta strand

360 – 366

7

Helix

367 – 373

7

Helix

383 – 389

7

Helix

390 – 392

3

Helix

396 – 406

11

Beta strand

407 – 409

3

Helix

410 – 419

10

Turn

420 – 424

5

Helix

427 – 433

7

Helix

441 – 447

7

Beta strand

454 – 457

4

Turn

462 – 464

3

Beta strand

468 – 474

7

Beta strand

477 – 479

3

Beta strand

485 – 487

3

Helix

489 – 495

7

Beta strand

508 – 514

7

Beta strand

528 – 531

4

Helix

534 – 537

4

Helix

538 – 553

16

Beta strand

560 – 567

8

Turn

569 – 571

3

Helix

576 – 584

9

Beta strand

587 – 595

9

Beta strand

598 – 601

4

Helix

605 – 611

7

Helix

613 – 621

9

Beta strand

625 – 631

7

Turn

632 – 634

3

Helix

635 – 650

16

Helix

655 – 667

13

Beta strand

670 – 676

7

Sequences

	Sequence		Length	Mass (Da)
	P16435 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 2F7D4B9CDFDF5A74	FASTA	677	76,690
	10 20 30 40 50 60 MGDSHVDTSS TVSEAVAEEV SLFSMTDMIL FSLIVGLLTY WFLFRKKKEE VPEFTKIQTL 70 80 90 100 110 120 TSSVRESSFV EKMKKTGRNI IVFYGSQTGT AEEFANRLSK DAHRYGMRGM SADPEEYDLA 130 140 150 160 170 180 DLSSLPEIDN ALVVFCMATY GEGDPTDNAQ DFYDWLQETD VDLSGVKFAV FGLGNKTYEH 190 200 210 220 230 240 FNAMGKYVDK RLEQLGAQRI FELGLGDDDG NLEEDFITWR EQFWPAVCEH FGVEATGEES 250 260 270 280 290 300 SIRQYELVVH TDIDAAKVYM GEMGRLKSYE NQKPPFDAKN PFLAAVTTNR KLNQGTERHL 310 320 330 340 350 360 MHLELDISDS KIRYESGDHV AVYPANDSAL VNQLGKILGA DLDVVMSLNN LDEESNKKHP 370 380 390 400 410 420 FPCPTSYRTA LTYYLDITNP PRTNVLYELA QYASEPSEQE LLRKMASSSG EGKELYLSWV 430 440 450 460 470 480 VEARRHILAI LQDCPSLRPP IDHLCELLPR LQARYYSIAS SSKVHPNSVH ICAVVVEYET 490 500 510 520 530 540 KAGRINKGVA TNWLRAKEPA GENGGRALVP MFVRKSQFRL PFKATTPVIM VGPGTGVAPF 550 560 570 580 590 600 IGFIQERAWL RQQGKEVGET LLYYGCRRSD EDYLYREELA QFHRDGALTQ LNVAFSREQS 610 620 630 640 650 660 HKVYVQHLLK QDREHLWKLI EGGAHIYVCG DARNMARDVQ NTFYDIVAEL GAMEHAQAVD 670 YIKKLMTKGR YSLDVWS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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. Tissue: Liver.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Web resources

GeneReviews

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00470467.

PIR

A60557. A33421.

RefSeq

NP_000932.3. NM_000941.2.

UniGene

Hs.354056.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P16435.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29682N.

IntAct

P16435. 4 interactions.

MINT

MINT-1212161.

STRING

9606.ENSP00000265302.

PTM databases

PhosphoSite

P16435.

Polymorphism databases

DMDM

2851393.

Proteomic databases

PaxDb

P16435.

PRIDE

P16435.

Protocols and materials databases

DNASU

5447.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

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.

GeneID

5447.

KEGG

hsa:5447.

UCSC

uc011kge.2. human.

Organism-specific databases

CTD

5447.

GeneCards

GC07P075528.

HGNC

HGNC:9208. POR.

HPA

CAB004372.
HPA010136.

MIM

124015. gene.
201750. phenotype.
613571. phenotype.

neXtProt

NX_P16435.

Orphanet

95699. Congenital adrenal hyperplasia due to cytochrome P450 oxidoreductase deficiency.

PharmGKB

PA33532.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0369.

HOGENOM

HOG000282027.

HOVERGEN

HBG000432.

InParanoid

P16435.

KO

K00327.

OrthoDB

EOG46HG96.

Enzyme and pathway databases

BioCyc

MetaCyc:HS05140-MONOMER.

Gene expression databases

ArrayExpress

P16435.

Bgee

P16435.

CleanEx

HS_POR.

Genevestigator

P16435.

GermOnline

ENSG00000127948. Homo sapiens.

Family and domain databases

Gene3D

1.20.990.10. 1 hit.

InterPro

IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR023208. P450R.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]

Pfam

PF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]

PIRSF

PIRSF000208. P450R. 1 hit.

PRINTS

PR00369. FLAVODOXIN.
PR00371. FPNCR.

SUPFAM

SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.

PROSITE

PS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

POR. human.

DrugBank

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

EvolutionaryTrace

P16435.

GenomeRNAi

5447.

NextBio

21083.

SOURCE

Search...

Entry information

Entry name

NCPR_HUMAN

Accession

Primary (citable) accession number: P16435
Secondary accession number(s): Q16455 , Q197M5, Q8N181, Q9H3M8, Q9UDT3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 160 of the entry and version 2 of the sequence. [Complete history]

Entry status

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.