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CYB5R3 Gene

protein-coding GIFtS: 57

GC22M041340

cytochrome b5 reductase 3
(Previous name: diaphorase (NADH) (cytochrome b-5 reductase) )
Symbol approved by the HUGO Gene Nomenclature Committee (HGNC) database
(Previous symbol: DIA1)

(According to ¹HGNC, ²Entrez Gene,
³UniProtKB/Swiss-Prot, ⁴UniProtKB/TrEMBL, ⁵OMIM, ⁶GeneLoc , and/or ⁷Ensembl, ⁸miRBase)
About This Section

Aliases
B5R ^², ³, ⁵
DIA1 ^², ³, ⁵
Diaphorase-1 ^³
EC 1.6.2.2 ^³
OTTHUMP00000028761 ^²

Descriptions
Cytochrome b5 reductase ^³
NADH-cytochrome b5 reductase ^²
cytochrome b5 reductase 3 ^²
diaphorase (NADH) (cytochrome b-5 reductase) ^¹, ²

External Ids
HGNC: 2873¹
Entrez Gene: 1727²
UniProtKB: P00387³
Ensembl: ENSG00000100243⁷

Search outside databases for aliases for CYB5R3 gene

(According to Entrez Gene, Wikipedia's Gene Wiki,
UniProtKB/Swiss-Prot, and/or UniProtKB/TrEMBL)
About This Section

EntrezGene summary for CYB5R3:

This gene encodes cytochrome b5 reductase, which includes a membrane-bound form in somatic cells

(anchored in the endoplasmic reticulum, mitochondrial and other membranes) and a soluble form in

erythrocytes. The membrane-bound form exists mainly on the cytoplasmic side of the endoplasmic

reticulum and functions in desaturation and elongation of fatty acids, in cholesterol

biosynthesis, and in drug metabolism. The erythrocyte form is located in a soluble fraction of

circulating erythrocytes and is involved in methemoglobin reduction. The membrane-bound form has

both membrane-binding and catalytic domains, while the soluble form has only the catalytic domain.

These two forms are resulted from alternative splicing of the gene. Mutations in this gene cause

methemoglobinemias. [provided by RefSeq]

UniProtKB/Swiss-Prot: NB5R3_HUMAN, P00387

Function: Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism,

and, in erythrocyte, methemoglobin reduction

Gene Wiki entry for CYB5R3

(According to GeneLoc and/or HGNC, and/or
Entrez Gene (NCBI build 36),
and/or miRBase,
Genomic Views according to UCSC and Ensembl, Transcription factor binding sites according to SABiosciences)
About This Section

Genomic View:

UCSC Golden Path with GeneCards custom track

Transcription factor binding sites upstream to the CYB5R3 gene

Entrez Gene cytogenetic band: 22q13.31-qter|22q13.2-q13.31 Ensembl cytogenetic band: 22q13.2 HGNC cytogenetic band: 22q13.31-qter

CYB5R3 Gene in genomic location: bands according to Ensembl, locations according to (and/or Entrez Gene and/or Ensembl if different)

GeneLoc gene densities for chromosome 22 GeneLoc Exon Structure

GeneLoc location for GC22M041340: (about GC identifiers)

Start:	41,344,763 bp from pter
End:	41,375,349 bp from pter
Size:	30,587 bases
Orientation:	minus strand

RefSeq DNA sequence:

NC_000022.9 NT_011520.11

(According to ¹UniProtKB, and/or Ensembl, Phosphorylation sites according to ²Phosphosite, RefSeq according to NCBI, PDB rendering according to OCA and/or Proteopedia, Recombinant Proteins from Invitrogen, Millipore, Sigma-Aldrich, R&D Systems, Enzo Life Sciences, Abnova, OriGene and/or, Abcam,
Biochemical Assays by Invitrogen, Millipore, R&D Systems, Cell Signaling Technology, and/or Enzo Life Sciences, Ontologies according to Gene Ontology Consortium 01 Apr 2009 and Entrez Gene, Antibodies by Invitrogen, Millipore, Sigma-Aldrich, R&D Systems, Cell Signaling Technology, Abcam, Abnova, and/or Novus Biologicals)
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UniProtKB/Swiss-Prot: NB5R3_HUMAN, P00387 (See protein sequence)

Recommended Name: NADH-cytochrome b5 reductase 3

Size: 301 amino acids; 34235 Da

Cofactor: FAD

Subunit: Component of a complex composed of cytochrome b5, NADH-cytochrome b5 reductase (CYB5R3)

and MOSC2 (By similarity)

Subcellular location: Isoform 1: Endoplasmic reticulum membrane; Lipid-anchor; Cytoplasmic side.

Mitochondrion outer membrane; Lipid-anchor; Cytoplasmic side

Subcellular location: Isoform 2: Cytoplasm. Note=Produces the soluble form found in erythrocytes

PDB structure from and Proteopedia :

1M91 (3D)

1UMK (3D)

Secondary accessions: B1AHF2 O75675 Q8TDL8 Q8WTS8 Q9UEN4 Q9UEN5 Q9UL55 Q9UL56

Alternative promoter usage: 2 isoforms: P00387-1 P00387-2

Post-translational modifications:

View phosphorylation sites using PhosphoSite²

REFSEQ proteins (3 alternative transcripts):

NP_000389.1 NP_001123291.1 NP_015565.1

ENSEMBL proteins:

ENSP00000384834 ENSP00000384457 ENSP00000385679 ENSP00000379597 ENSP00000354468 ENSP00000379603

ENSP00000338461

Human Recombinant Proteins

	Browse Drug Discovery Central at Invitrogen for human recombinant proteins
	Browse Purified and Recombinant Proteins at Millipore
	Browse Human Recombinant Proteins at Sigma-Aldrich
	Browse R&D Systems for human recombinant proteins
	Browse recombinant and purified proteins available from Enzo Life Sciences
	Recombinant Proteins from Abcam (CYB5R3)
	Human Recombinant Proteins from Abnova (CYB5R3)

OriGene Purified Recombinant Human Proteins (see all 2): CYB5R3

5/8 Gene Ontology (GO) cellular component terms (links to tree view) (see all 8 ):

GO ID	Qualified GO term	Evidence	PubMed IDs
GO:0005737	cytoplasm	TAS	9207238
GO:0005739	mitochondrion	IEA	--
GO:0005741	mitochondrial outer membrane	IEA	--
GO:0005743	mitochondrial inner membrane	IEA	--
GO:0005783	endoplasmic reticulum	IEA	--

About this table

Antibodies for CYB5R3:

	Browse Antibodies Central at Invitrogen
	Browse Millipore's Extensive Line of Mono- and Polyclonal Antibodies
	Sigma-Aldrich Antibodies for CYB5R3
	Browse R&D Systems for Antibodies
	Antibodies from Abcam (CYB5R3), each with their Abpromise^SM
	Monoclonal and Polyclonal Antibodies from Abnova (CYB5R3)
	Novus Biologicals Antibodies for CYB5R3

Assays for CYB5R3:

	Browse Invitrogen for biochemical assays
	Browse Kits and Assays available from Millipore
	Browse R&D Systems for biochemical assays
	Browse biochemical assays available from Enzo Life Sciences

(According to InterPro, ProtoNet, UniProtKB, and/or BLOCKS, Sets of similar genes according to GeneDecks)
About This Section

Graphical View of Domain Structure for InterPro Entry P00387

ProtoNet protein and cluster: P00387

4 Blocks protein families:

IPB001433 Oxidoreductase FAD/NAD(P)-binding

IPB001709 Flavoprotein pyridine nucleotide cytochrome reductase signature

IPB001834 Cytochrome B5 reductase signature

IPB008333 Oxidoreductase FAD-binding region

UniProtKB/Swiss-Prot: NB5R3_HUMAN, P00387

Similarity: Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family

Similarity: Contains 1 FAD-binding FR-type domain

(According to MGI Jun 06 2009, UniProtKB, IUBMB,and/or Genatlas,
shRNA from OriGene, Sigma-Aldrich, RNAi from Sigma-Aldrich,
RNAi Products, Clones, and Q-PCR Products from Invitrogen, Millipore, OriGene, and/or Abnova, siRNAs from Applied Biosystems, SYBR primers from OriGene, Cell-based Assays from Millipore, Ontologies according to Gene Ontology Consortium 01 Apr 2009 via Entrez Gene.)
About This Section

Inhib. RNA:		Invitrogen RNAi Products for gene knock-down (CYB5R3)
		Browse for Gene Knock-down Tools from Millipore
		Abnova Chimera RNAi Products for Gene knock-down (CYB5R3)

OriGene 29mer shRNA kit in GFP-retroviral vectors (see all 3): NM_000398

Applied Biosystems Silencer® siRNAs for CYB5R3

Sigma-Aldrich siRNA and siRNA Panels for CYB5R3

Sigma-Aldrich shRNA for CYB5R3

Explore Sigma-Aldrich super-pooled esiRNAs

Clones:		Invitrogen Clones for CYB5R3
		Browse Clones for the Expression of Recombinant Proteins Available from Millipore

OriGene GFP tagged cDNA clones in CMV expression vector (see all 3): NM_000398
Myc/DDK tagged cDNA clones in CMV expression vector (see all 3): NM_000398
untagged cDNA clones in CMV expression vector (see all 3): NM_000398

Primers:

Browse Quantitative PCR Central at Invitrogen for Q-PCR LUX™ Primers

OriGene genome-wide validated SYBR primer pairs: NM_000398

UniProtKB/Swiss-Prot: NB5R3_HUMAN, P00387

Function: Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism,

and, in erythrocyte, methemoglobin reduction

Catalytic activity: NADH + 2 ferricytochrome b5 = NAD(+) + H(+) + 2 ferrocytochrome b5

Enzyme Number (IUBMB): EC 1.6.2.2

3 Gene Ontology (GO) molecular function terms (links to tree view):

GO ID	Qualified GO term	Evidence	PubMed IDs
GO:0004128	cytochrome-b5 reductase activity	TAS	1400360
GO:0009055	electron carrier activity	IEA	--
GO:0016491	oxidoreductase activity	IEA	--

About this table

(Pathways according to Invitrogen (maps by GeneGo), Millipore, Cell Signaling Technology, Sigma-Aldrich, KEGG and/or UniProtKB,
Sets of similar genes according to GeneDecks, Proteins Network according to SABiosciences, Interactions according to ¹UniProtKB, ²MINT, and/or ³STRING, with links to IntAct and Ensembl, Ontologies according to Gene Ontology Consortium 01 Apr 2009 via Entrez Gene.)
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2 Sigma-Aldrich "Your Favorite Gene" Pathways for CYB5R3 (Your Favorite Gene powered by Ingenuity)

Aminosugars Metabolism
Mitochondrial Dysfunction

GeneDecks CYB5R3 for the pathways selected above

About GeneDecksing

Gene Network Central^TM Interacting Genes and Proteins Network for CYB5R3

5/21 Interacting proteins for CYB5R3 (ENSP00000338461³) via UniProtKB, MINT, and/or STRING (see all 21 )

Interactant		Interaction Details
GeneCard	External ID(s)	Interaction Details
CYB5A	ENSP00000341625³	STRING (score=.971)
HBG1	ENSP00000369606³	STRING (score=.961)
DLD	ENSP00000205402³	STRING (score=.936)
DIAPH2	ENSP00000321348³	STRING (score=.906)
HBQ1	ENSP00000199708³	STRING (score=.901)

About this table

3 Gene Ontology (GO) biological process terms (links to tree view):

GO ID	Qualified GO term	Evidence	PubMed IDs
GO:0006695	cholesterol biosynthetic process	IEA	--
GO:0008015	blood circulation	TAS	1400360
GO:0055114	oxidation reduction	IEA	--

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(Chemical Compounds according to UniProtKB, Enzo Life Sciences, Sigma-Aldrich, Tocris Bioscience, and/or Novoseek and Drugs according to Enzo Life Sciences and/or PharmGKB)
About This Section

Browse drugs & compounds from Enzo Life Sciences

Browse Small Molecules at Sigma-Aldrich

Browse Tocris compounds for CYB5R3
10/29 Novoseek chemical compound relationships for CYB5R3 gene (see all 29 )

Compound	Score	Articles	PubMed IDs for Articles with Shared Sentences (# sentences)
benzamidoxime	88.35	4	9351903 (1), 15862605 (1), 15302896 (1), 16973608 (1)
nadh	84.42	126	8883403 (6), 15302896 (6), 8402680 (5), 2162152 (4) (see all 54)
sulfamethoxazole hydroxylamine	77.24	3	15302896 (2), 15862605 (1)
flavin-adenine dinucleotide	65.55	1	11159544 (1)
phmb	57.74	2	8883403 (1)
ferricyanide	54.99	1	2189408 (1)
nadph	54.62	12	10611283 (2), 8005794 (2), 11263680 (1), 2161167 (1) (see all 9)
phip	47.85	3	17040106 (2), 18636192 (1)
p-chloromercuribenzoate	46.26	2	12195287 (1)
nad+	45.26	6	8874222 (1), 10807796 (1), 11159544 (1), 12756024 (1)

About this table

(GenBank/EMBL/DDBJ Accessions according to
Unigene (Build 219 Homo sapiens; Jun 2 2009) or GenBank,
RefSeq according to Entrez Gene,
DOTS (version 10), and/or AceView,
non coding RNAs according to RNAdb,
ESTs according to GeneTide,
exon structure from GeneLoc, alternative splicing isoforms according to ASD and/or ECgene,
RNAi Products from Invitrogen, Millipore, and/or Abnova,
siRNAs from Applied Biosystems, Sigma-Aldrich,
shRNA from Sigma-Aldrich, OriGene,
Tagged/untagged cDNA clones from OriGene,
Expression Assays from Applied Biosystems)
About This Section

Inhib. RNA:		Invitrogen RNAi Products for gene knock-down (CYB5R3)
		Browse for Gene Knock-down Tools from Millipore
		Abnova Chimera RNAi Products for Gene knock-down (CYB5R3)

OriGene 29mer shRNA kit in GFP-retroviral vectors (see all 3): NM_000398

Sigma-Aldrich siRNA and siRNA Panels for CYB5R3

Sigma-Aldrich shRNA for CYB5R3

Explore Sigma-Aldrich super-pooled esiRNAs

Applied Biosystems Silencer® siRNAs:

NM_000398 NM_001129819 NM_007326

REFSEQ mRNAs for CYB5R3 gene (3 alternative transcripts):

NM_000398.5 NM_001129819.1 NM_007326.3

Applied Biosystems TaqMan ® Gene Expression Assays:

NM_000398 NM_001129819 NM_007326

               OriGene GFP tagged cDNA clones in CMV expression vector (see all 3): NM_000398
                                 Myc/DDK tagged cDNA clones in CMV expression vector (see all 3): NM_000398
                                 untagged cDNA clones in CMV expression vector (see all 3): NM_000398

Additional cDNA sequence:

AF361370.1 AJ010116.1 AJ010117.1 AJ010118.1 AJ310899.1 AJ310900.1 AK302204.1 AY421733.1

AY421734.1 BC004821.1 BT009821.1 CR456435.1 CR590472.1 CR591561.1 CR591876.1 CR593330.1

CR594068.1 CR594248.1 CR594565.1 CR596321.1 CR596646.1 CR596939.1 CR597031.1 CR597830.1

CR598100.1 CR600429.1 CR600483.1 CR601021.1 CR601590.1 CR602125.1 CR603135.1 CR604771.1

CR604882.1 CR607358.1 CR607839.1 CR610106.1 CR610296.1 CR610489.1 CR612466.1 CR613363.1

CR613744.1 CR614570.1 CR614892.1 CR615126.1 CR616501.1 CR617674.1 CR617720.1 CR618034.1

CR618233.1 CR620124.1 CR621834.1 CR623803.1 CR626640.1 M16461.1 M16462.1 Y09501.1

24/52 DOTS entries (see all 52 ):

DT.100045068 DT.95069144 DT.95069119 DT.100892769 DT.100045067 DT.100830765 DT.100892785 DT.100892777

DT.100892800 DT.100892754 DT.95069139 DT.100892796 DT.120630305 DT.100892762 DT.100645199 DT.100892757

DT.95069141 DT.100645065 DT.100705538 DT.100892752 DT.100892770 DT.100892794 DT.120630295 DT.120630457

24/712 AceView cDNA sequences (see all 712 ):

CB529568 BX462940 CB106080 BX424703 CR610296 BI258961 AA279986 CB130553

CB154557 CB152270 BG152484 BI768166 BM919654 CR600483 CA390977 BI820716

BX428329 BM826404 BI834357 H55658 AK124528 AA636055 CB106199 CA390521

highest scoring ESTs for CYB5R3:

AF361370 AL709930 AW239223 AW401964 BC004821 BE173865 BE312790 BE783173 BE891559 BE892732

Unigene Cluster for CYB5R3:

Cytochrome b5 reductase 3

Hs.700572 [show with all ESTs]

Unigene Representative Sequence: NM_001129819

GeneLoc Exon Structure

5/7 Alternative Splicing Database (ASD) splice patterns (SP) for CYB5R3 (see all 7 )

ExUns:	1a	·	1b	·	1c	^	2	^	3	^	4	^	5a	·	5b	^	6	^	7a	·	7b	^	8a	·	8b	^	9	^	10a	·	10b	^	11a	·	11b	·	11c	·	11d
SP1:							-		-						-						-								-
SP2:							-		-						-				-		-								-
SP3:							-		-						-				-		-		-		-		-		-
SP4:															-						-
SP5:									-						-

About this scheme

ECgene alternative splicing isoforms for CYB5R3

7 Ensembl transcripts including schematic representations:

ENST00000407623 ENST00000407332 ENST00000402438 ENST00000396303 ENST00000361740 ENST00000396309

ENST00000352397

(Experimental results according to ¹GeneNote and GNF BioGPS,
probe sets-to-genes annotations according to ²GeneAnnot , ³GeneTide , Sets of similar genes according to GeneDecks, Electronic Northern calculations according to data from UniGene (Build 219 Homo sapiens), SAGE tags according to CGAP, plus additional links to SOURCE, and/or GNF BioGPS, and/or EXPOLDB, and/or UniProtKB,
Expression Assays from Applied Biosystems )
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CYB5R3 expression in normal and diseased human tissues

Applied Biosystems TaqMan ® Gene Expression Assays for CYB5R3

¹ / ² / ³

5 probe-sets matching CYB5R3 gene

Affymetrix probe-set	Array	# genes	Sensitivity	Specificity	Correlation	Length	Gb_Accession	Consensus	Uniqueness	Score	Rank
Affymetrix probe-set	Array	GeneAnnot data			GeneNote data		GeneTide data
36668_at²^{, 3}	U95-A	1	1.00	1.00	0.91	0.96	M28713	0.20	1.00	0.72	1
55326_f_at²^{, 3}	U95-C	2478	0.56	0.01	0.20	1.04	AA595780	0.20	0.06	0.15	1
201885_s_at²^{, 3}	U133-A	1	1.00	1.00	--	--	NM_000398	0.60	1.00	0.82	1
1554574_a_at²	U133Plus2	1	1.00	1.00	--	--	--	--	--	--	--
201885_s_at²	U133Plus2	1	1.00	1.00	--	--	--	--	--	--	--

About this table

Data from

(Publications) and GNF BioGPS
About these images
About these images

CGAP SAGE TAG: --

SOURCE GeneReport for Unigene cluster: Hs.700572
UniProtKB/Swiss-Prot: NB5R3_HUMAN, P00387
Tissue specificity: Isoform 2 (soluble form) is expressed at late stages of erythroid maturation

(Orthologs according to ^1,2HomoloGene (²older version, for species not in ¹newer version), ³euGenes, ⁴SGD and/or ⁵MGI Jun 06 2009, with possible further links to Flybase and/or WormBase, Gene Trees according to Ensembl)
About This Section

Orthologs for CYB5R3 gene from 5/13 species (see all 13 )

Organism	Gene	Locus	Description	Human Similarity	NCBI accessions
dog (Canis familiaris)	CYB5R3¹	--	cytochrome b5 reductase 3	89.8(n) 92.52(a)	474479 XM_531708.2 XP_531708.2
chimpanzee (Pan troglodytes)	CYB5R3¹	--	cytochrome b5 reductase 3	98.45(n) 97.01(a)	458883 XM_001171082.1 XP_001171082.1
cow (Bos taurus)	CYB5R3¹	--	cytochrome b5 reductase 3	92.03(n) 93.23(a)	515773 XM_593854.3 XP_593854.3
rat (Rattus norvegicus)	Cyb5r3¹	--	cytochrome b5 reductase 3	86.16(n) 87.04(a)	25035 NM_138877.1 NP_620232.1
mouse (Mus musculus)	Cyb5r3⁵ Cyb5r3¹	15 (45.20 cM)⁵	cytochrome b5 reductase 3^{1, 5}	86.93(n)¹ 87.38(a)¹	109754¹ NM_029787.2¹ NP_084063.1¹ AF332059⁵ AF332060⁵ (see all 34)

About this table Species with no ortholog for CYB5R3

ENSEMBL Gene Tree for CYB5R3

(Paralogs according to ¹HomoloGene
and ²Ensembl, Pseudogenes according to ³Pseudogene.org)
About This Section

Paralogs for CYB5R3 gene

CYB5R2² CYB5R1² CYB5R4²

(According to the ¹NCBI SNP Database, ²Ensembl, ³PupaSUITE, and UniProtKB, Linkage Disequilibrium by HapMap, Genotyping Reagents from Applied Biosystems)
About This Section

UniProtKB/Swiss-Prot: NB5R3_HUMAN, P00387

Polymorphism: Ser-117 seems to only be found in persons of African origin. The allele frequency is

0.23 in African Americans. It was not found in Caucasians, Asians, Indo-Aryans, or Arabs. There

seems to be no effect on the enzyme activity

10/400 NCBI SNPs in CYB5R3 are shown (see all 400 )
(Click for Applied Biosystems TaqMan ® Genotyping Assay) (see all 135)

AB	SNP ID	Valid	Chr 22 pos	Sequence	Recs	AA Chg	Type	More	Recs	Pop	Total sample	More
AB	Genomic Data				Transcription Data				Allele Frequencies
				--	--	--		--	--			--
	rs1800457^1,2	C,F,H,O	41354215(-)	`GGACAC/GCCATC`	3	T/S	mis¹ ese³		14	NS NA EU EA WA	1396
	rs137124^1,2	A,C,F,H	41345660(+)	`GTGACT/CGGGTG`	3	--	ut3¹ ese³		12	MN EU EA WA NS NA	1346
	rs8190371^1,2	C,F,H	41374709(-)	`GGTTTT/CGCACG`	2	--	int¹ ng3¹		9	NS EU EA WA	1008
	rs137123^1,2	A,C,F	41345436(+)	`GTGTGG/TGGGGT`	3	--	ut3¹ ese³		5	EA NA NS MN	344
	rs2267459^1,2	A,C,F	41373898(+)	`AGGTAT/AGGAAC`	2	--	ng3¹ int¹		7	NS	706
--	rs6002817^1,2	A,C,F	41344411(+)	`gaaccC/Tgggag`	2	--	ng5¹		1	NS	158
	rs3761461^1,2	C,F,H	41377229(+)	`AAGAAC/G/TTGGAA`	1	--	ng3¹		5	EU EA WA	592
	rs2284090^1,2	C,F	41373031(+)	`ACCTAG/AAGCAC`	2	--	ng3¹ int¹		7	NS	808
--	rs8190475^1,2	C,F	41344295(-)	`ttagcC/Tgggat`	2	--	ng5¹		1	NS	160
	rs5996205^1,2	C,F	41375651(+)	`CCTGTT/GCCTGC`	1	--	ng3¹		2	MN EA	1252

About this table

HapMap Linkage Disequilibrium images for CYB5R3 (up to first 250kb)

(in which this Gene is Involved, According to OMIM, UniProtKB, Novoseek, PharmGKB, Genatlas, GeneTests, Blood group antigen gene mutations by BGMUT, HGMD, GAD, HuGE Navigator, BCGD, and/or TGDB.)
About This Section

OMIM: 250800

UniProtKB/Swiss-Prot: NB5R3_HUMAN, P00387

Defects in CYB5R3 are the cause of hereditary methemoglobinemia (HM) [MIM:250800]. There

are three forms of this disease: type 1 (HM1) in which the enzyme is only deficient in

erythrocytes with a mild cyanosis; type 2 (HM2), in which the enzyme is completely deficient; type

3 (HM3) where the deficiency is seen in all blood cells. Type 2 is a severe form accompanied with

mental retardation and neurological impairment

10 Novoseek disease relationships for CYB5R3 gene

Disease	Score	Articles	PubMed IDs for Articles with Shared Sentences (# sentences)
methemoglobinemia hereditary	97.96	42	1400360 (3), 11243135 (3), 2107882 (3), 10979206 (3) (see all 18)
methemoglobinemia	92.30	58	10807796 (3), 10874300 (3), 10534899 (3), 7860238 (3) (see all 31)
methemoglobinemia acquired	71.35	2	15921385 (1), 10870338 (1)
enzyme deficiency	67.78	6	1400360 (1), 2323714 (1), 1707593 (1), 2107882 (1) (see all 5)
rare disease	17.62	3	18202104 (1), 7668255 (1)
genetic disorder	10.63	2	2323714 (1)
mental retardation	7.16	4	8352247 (1), 8427971 (1), 8143727 (1)
tumors	4.43	4	18794327 (2), 8005794 (1), 7987842 (1)
congenital malformation	0.00	2	7668255 (1)
cancer	0.00	9	17040106 (1), 8883403 (1), 19082487 (1)

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Human Gene Mutation Database: CYB5R3

(Possibly Related Articles in Doctor's Guide)
About This Section

(in PubMed. Associations of this gene to articles via ¹Novoseek, ²HGNC, ³Entrez Gene, ⁴UniProtKB/Swiss-Prot, ⁵UniProtKB/TrEMBL, ⁶GAD, and/or ⁷PharmGKB)
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100/178 PubMed articles for CYB5R3 gene (see all 178 ):

The organization and the complete nucleotide sequence of the human NADH-cytochrome b5 reductase gene. (PubMed id 2479590)^{2, 3, 4} Tomatsu S.... Sakaki Y. (1989)
An erythroid-specific transcript generates the soluble form of NADH- cytochrome b5 reductase in humans. (PubMed id 9639531)^{1, 3, 4} Bulbarelli A....Borgese N. (1998)
A novel mutation in the NADH-cytochrome b5 reductase gene of a Chinese patient with recessive congenital methemoglobinemia. (PubMed id 10807796)^{1, 3, 4} Wang Y.... Zhu Z.-Y. (2000)
Molecular basis of hereditary methaemoglobinaemia, types I and II: two novel mutations in the NADH-cytochrome b5 reductase gene. (PubMed id 9886302)^{1, 3, 4} Higasa K.... Fukumaki Y. (1998)
A high-frequency polymorphism of NADH-cytochrome b5 reductase in African-Americans. (PubMed id 9048929)^{1, 3, 4} Jenkins M.M. and Prchal J.T. (1997)
Identification of a novel point mutation (Leu72-to-Pro) in the NADH- cytochrome b5 reductase gene of a patient with hereditary methaemoglobinaemia type I. (PubMed id 9695975)^{1, 3, 4} Wu Y.-S.... Zhu Z.-Y. (1998)
Role of cysteine residues in human NADH-cytochrome b5 reductase studied by site-directed mutagenesis. Cys-273 and Cys-283 are located close to the NADH-binding site but are not catalytically essential. (PubMed id 2019583)^{1, 3, 4} Shirabe K.... Takeshita M. (1991)
Enzymatic instability of NADH-cytochrome b5 reductase as a cause of hereditary methemoglobinemia type I (red cell type). (PubMed id 1400360)^{1, 3, 4} Shirabe K....Takeshita M. (1992)
Exonic point mutations in NADH-cytochrome B5 reductase genes of homozygotes for hereditary methemoglobinemia, types I and III: putative mechanisms of tissue-dependent enzyme deficiency. (PubMed id 1707593)^{1, 3, 4} Katsube T.... Fukumaki Y. (1991)
Arginine-glutamine replacement at residue 57 of NADH-cytochrome b5 reductase in Chinese hereditary methemoglobinemia. (PubMed id 15622768)^{1, 3, 4} Huang C.-H.... Wu Y.-S. (1997)
Four new mutations in the NADH-cytochrome b5 reductase gene from patients with recessive congenital methemoglobinemia type II. (PubMed id 7718898)^{1, 3, 4} Vieira L.M.... Leroux A. (1995)
An in-frame deletion of codon 298 of the NADH-cytochrome b5 reductase gene results in hereditary methemoglobinemia type II (generalized type). A functional implication for the role of the COOH-terminal region of the enzyme. (PubMed id 8119939)^{1, 3, 4} Shirabe K.... Takeshita M. (1994)
Structural role of serine 127 in the NADH-binding site of human NADH- cytochrome b5 reductase. (PubMed id 1898726)^{1, 3, 4} Yubisui T.... Takano T. (1991)
Structure of human erythrocyte NADH-cytochrome b5 reductase. (PubMed id 15502298)^{1, 3, 4} Bando S....Nakagawa A. (2004)
Familial idiopathic methemoglobinemia revisited: original cases reveal 2 novel mutations in NADH-cytochrome b5 reductase. (PubMed id 12393396)^{3, 4} Percy M.J....Lappin T.R.J. (2002)
The NH2-terminal structures of human and rat liver microsomal NADH- cytochrome b5 reductases. (PubMed id 2498303)^{3, 4} Murakami K.... Miyata T. (1989)
Cloning and chromosomal mapping of human cytochrome b5 reductase (DIA1). (PubMed id 3268037)^{2, 3} Bull P.C....Phillips I.R. (1988)
Molecular cloning of cDNAs of human liver and placenta NADH- cytochrome b5 reductase. (PubMed id 3035541)^{3, 4} Yubisui T.... Sakaki Y. (1987)
Complete amino acid sequence of NADH-cytochrome b5 reductase purified from human erythrocytes. (PubMed id 3700359)^{3, 4} Yubisui T.... Takeshita M. (1986)
Amino acid sequence of NADH-cytochrome b5 reductase of human erythrocytes. (PubMed id 6389526)^{3, 4} Yubisui T.... Nakajima H. (1984)
Identification of alternative first exons of NADH-cytochrome b5 reductase gene expressed ubiquitously in human cells. (PubMed id 9207238)^{1, 3} Du M....Takeshita M. (1997)
Serine-proline replacement at residue 127 of NADH-cytochrome b5 reductase causes hereditary methemoglobinemia, generalized type. (PubMed id 2107882)^{1, 3} Kobayashi Y....Sakaki Y. (1990)
A case of methemoglobinemia type II due to NADH-cytochrome b5 reductase deficiency: determination of the molecular basis. (PubMed id 10874300)^{1, 3} Aalfs C.M....Wijburg F.A. (2000)
A novel point mutation in a 3' splice site of the NADH-cytochrome b5 reductase gene results in immunologically undetectable enzyme and impaired NADH-dependent ascorbate regeneration in cultured fibroblasts of a patient with type II hereditary methemoglobinemia. (PubMed id 7668255)^{1, 3} Shirabe K....Borgese N. (1995)
Recessive hereditary methemoglobinemia: two novel mutations in the NADH-cytochrome b5 reductase gene. (PubMed id 18343696)^{1, 3} Fermo E....Zanella A. (2008)
Analysis of mutant NADH-cytochrome b5 reductase: apparent "type III" methemoglobinemia can be explained as type I with an unstable reductase. (PubMed id 8427971)^{1, 3} Nagai T....Takeshita M. (1993)
Prenatal diagnosis of recessive congenital methaemoglobinaemia type II: novel mutation in the NADH-cytochrome b5 reductase gene leading to stop codon read-through. (PubMed id 15813912)^{1, 3} Leroux A....Szajnert M.F. (2005)
Congenital methaemoglobinaemia Type I in a Turkish infant due to a novel mutation, Pro144Ser, in NADH-cytochrome b5 reductase. (PubMed id 15297856)^{1, 3} Percy M.J....Irken G. (2004)
Characterization of the covalent cross-links of the active sites of amidinated cytochrome b5 and NADH:cytochrome b5 reductase. (PubMed id 2123873)^{1, 3} Strittmatter P....Ozols J. (1990)
Recessive congenital methaemoglobinaemia: functional characterization of the novel D239G mutation in the NADH-binding lobe of cytochrome b5 reductase. (PubMed id 15953014)^{1, 4} Percy M.J....Lappin T.R.J. (2005)
Recessive congenital methaemoglobinaemia type II a new mutation which causes incorrect splicing in the NADH-cytochrome b5 reductase gene. (PubMed id 9266404)^{1, 3} Owen E.P....Harley E.H. (1997)
A role for N-myristoylation in protein targeting: NADH-cytochrome b5 reductase requires myristic acid for association with outer mitochondrial but not ER membranes. (PubMed id 8978818)^{1, 3} Borgese N....Bassetti M. (1996)
Activity of membrane-bound NADH-methemoglobin reductase and physical state of lipids in erythrocyte membranes. (PubMed id 15039026)³ Lukyanenko L.M....Slobozhanina E.I. (2004)
Cytochrome b5 reductase: the roles of the recessive congenital methemoglobinemia mutants P144L, L148P, and R159*. (PubMed id 15488472)³ Davis C.A....Barber M.J. (2004)
Modification and identification of cytochrome b5 carboxyl groups involved in protein-protein interaction with cytochrome b5 reductase. (PubMed id 221468)³ Dailey H.A. and Strittmatter P. (1979)
Soluble cytochrome b 5 reductase from human erythrocytes. (PubMed id 4403130)³ Passon P.G. and Hultquist D.E. (1972)
[Establishment of a cellular model with human NADH-cytochrome b5 reductase deficiency via RNA interference] (PubMed id 18683136)¹ Zhuang Y....Lan F. (2008)
Determination of concentration of cytosolic NADH-cytochrome b5 reductase in erythrocytes from normal Chinese adults, neonates and patients with hereditary methemoglobinemia by double-antibody sandwich ELISA. (PubMed id 9691146)¹ Lan F....Zhu Z. (1998)
Development and validation of a spectrophotometric assay for measuring the activity of NADH: cytochrome b5 reductase in human tumour cells. (PubMed id 8883403)¹ Barham H.M....Stratford I.J. (1996)
Hydrogen peroxide- and cell-density-regulated expression of NADH-cytochrome b5 reductase in HeLa cells. (PubMed id 12887015)¹ Bello R.I....Villalba J.M. (2003)
Establishment of monoclonal antibodies against human erythrocyte NADH-cytochrome b5 reductase. (PubMed id 8880217)¹ Lan F....Zhu Z. (1996)
Reductive detoxification of arylhydroxylamine carcinogens by human NADH cytochrome b5 reductase and cytochrome b5. (PubMed id 17040106)¹ Kurian J.R....Trepanier L.A. (2006)
Epidemiological evaluation of recurrent stomatitis, nitrates in drinking water, and cytochrome b5 reductase activity. (PubMed id 10406239)¹ Gupta S.K....Sharma S. (1999)
Antibody-based spot test for NADH-cytochrome b5 reductase activity for the laboratory diagnosis of congenital methemoglobinemia. (PubMed id 9620466)¹ Lan F.H....Zhu Z.Y. (1998)
N-myristoylation determines dual targeting of mammalian NADH-cytochrome b5 reductase to ER and mitochondrial outer membranes by a mechanism of kinetic partitioning. (PubMed id 15738266)¹ Colombo S....Borgese N. (2005)
NADH cytochrome b5 reductase and cytochrome b5 catalyze the microsomal reduction of xenobiotic hydroxylamines and amidoximes in humans. (PubMed id 15302896)¹ Kurian J.R....Trepanier L.A. (2004)
A compound heterozygote in the NADH-cytochrome b5 reductase gene from a Chinese patient with hereditary methemoglobinemia type I. (PubMed id 10979206)¹ Wu Y.S....Zhu Z.Y. (2000)
[Leu 72 Pro mutation in the NADH-cytochrome b5 reductase gene found in a Chinese hereditary methemoglobinemia patient] (PubMed id 11243135)¹ Wu Y....Zhu Z. (1998)
Role of carboxyl residues surrounding heme of human cytochrome b5 in the electrostatic interaction with NADH-cytochrome b5 reductase. (PubMed id 9588172)¹ Kawano M....Takeshita M. (1998)
A novel mutation found in the 3' domain of NADH-cytochrome B5 reductase in an African-American family with type I congenital methemoglobinemia. (PubMed id 8639921)¹ Jenkins M.M. and Prchal J.T. (1996)
Molecular cloning of a cDNA encoding rat NADH-cytochrome b5 reductase and the corresponding gene. (PubMed id 2391344)¹ Zenno S....Sakaki Y. (1990)
Identification of cytochrome-b5 reductase as the enzyme responsible for NADH-dependent lucigenin chemiluminescence in human spermatozoa. (PubMed id 15858218)¹ Baker M.A.... Aitken R.J. (2005)
[Role of NADH-cytochrome b(5) reductase in biosynthesis of thyroid hydrogen peroxide] (PubMed id 12195287)¹ Huang G.L....Zhu J.W. (2002)
Adaptation of cytochrome-b5 reductase activity and methaemoglobinaemia in areas with a high nitrate concentration in drinking-water. (PubMed id 10534899)¹ Gupta S.K....Gupta A. (1999)
Role of cytochrome b5 reductase on the antioxidant function of coenzyme Q in the plasma membrane. (PubMed id 9266501)¹ Villalba J.M....Navas P. (1997)
Electrostatic properties deduced from refined structures of NADH-cytochrome b5 reductase and the other flavin-dependent reductases: pyridine nucleotide-binding and interaction with an electron-transfer partner. (PubMed id 8880927)¹ Nishida H. and Miki K. (1996)
Reductive activation of mitomycin C by NADH:cytochrome b5 reductase. (PubMed id 8402680)¹ Hodnick W.F. and Sartorelli A.C. (1993)
New variant of cytochrome b5 reductase deficiency (b5RKurashiki) in red cells, platelets, lymphocytes, and cultured fibroblasts with congenital methemoglobinemia, mental and neurological retardation, and skeletal anomalies. (PubMed id 1503085)¹ Yawata Y....Tomoda A. (1992)
[Molecular analysis of the structure of the mutant NADH-cytochrome b5 reductase gene causing methemoglobinemia] (PubMed id 2323714)¹ Kobayashi Y. (1990)
Transcriptional and translational mechanisms of cytochrome b5 reductase isoenzyme generation in humans. (PubMed id 11284742)¹ Leroux A.... Kahn A. (2001)
Molecular basis of recessive congenital methemoglobinemia, types I and II: Exon skipping and three novel missense mutations in the NADH-cytochrome b5 reductase (diaphorase 1) gene. (PubMed id 11295830)¹ Kugler W....Lakomek M. (2001)
Superoxide, neuroleptics and the ubiquinone and cytochrome b5 reductases in brain and lymphocytes from normals and schizophrenic patients. (PubMed id 9672898)¹ Whatley S.A....Marchbanks R.M. (1998)
The cytoplasmic and transmembrane domains of the vaccinia virus B5R protein target a chimeric human immunodeficiency virus type 1 glycoprotein to the outer envelope of nascent vaccinia virions. (PubMed id 9060681)¹ Katz E....Moss B. (1997)
Transient kinetics of intracomplex electron transfer in the human cytochrome b5 reductase-cytochrome b5 system: NAD+ modulates protein-protein binding and electron transfer. (PubMed id 7733677)¹ Meyer T.E....Tollin G. (1995)
Effects of domain-specific erythrocyte membrane modulators on acetylcholinesterase and NADH:cytochrome b5 reductase activities. (PubMed id 2162152)¹ Palmieri D.A....Butterfield D.A. (1990)
Dissecting the role of multiple reductases in bioactivation and cytotoxicity of the antitumor agent 2,5-diaziridinyl-3-(hydroxymethyl)-6-methyl-1,4-benzoquinone (RH1). (PubMed id 18794327)¹ Yan C....Ross D. (2008)
Molecular dynamics simulation study on stabilities and reactivities of NADH cytochrome B5 reductase. (PubMed id 18412408)¹ Asada T....Koseki S. (2008)
Antibodies against the extracellular enveloped virus B5R protein are mainly responsible for the EEV neutralizing capacity of vaccinia immune globulin. (PubMed id 15246280)¹ Bell E....Isaacs S.N. (2004)
Compound heterozygosity of two missense mutations in the NADH-cytochrome b5 reductase gene of a Polish patient with type I recessive congenital methaemoglobinaemia. (PubMed id 12756024)¹ Grabowska D....Burzynska B. (2003)
Seven new mutations in the nicotinamide adenine dinucleotide reduced-cytochrome b(5) reductase gene leading to methemoglobinemia type I. (PubMed id 11159544)¹ Dekker J....Roos D. (2001)
[A novel point mutation in NADH-cytochrome b5 reductase gene] (PubMed id 11721397)¹ Wang Y....Yang W. (1999)
Electrostatic interaction between NADH-cytochrome b5 reductase and cytochrome b5 studied by site-directed mutagenesis. (PubMed id 9602031)¹ Shirabe K....Takeshita M. (1998)
The pH-dependent reduction of Adriamycin catalysed by NADH:cytochrome b5 reductase. (PubMed id 8076371)¹ Hodnick W.F. and Sartorelli A.C. (1994)
Heterogeneity of the rat NADH-cytochrome-b5-reductase transcripts resulting from multiple alternative first exons. (PubMed id 8143727)¹ Mota Vieira L....Leroux A. (1994)
Purification and characterization of two forms of soluble NADH cytochrome b5 reductases from human erythrocytes. (PubMed id 1499270)¹ Arinc E....Adali O. (1992)
Role of NADPH-cytochrome P450 reductase and cytochrome-b5/NADH-b5 reductase in variability of CYP3A activity in human liver microsomes. (PubMed id 18838505)¹ Gan L....Court M.H. (2009)
Methemoglobinemia in children with acute lymphoblastic leukemia (ALL) receiving dapsone for pneumocystis carinii pneumonia (PCP) prophylaxis: a correlation with cytochrome b5 reductase (Cb5R) enzyme levels. (PubMed id 15390276)¹ Williams S....Athale U.H. (2005)
Evaluation of data in terms of two-dimensional random walk model: interaction between NADH-cytochrome b5 reductase and cytochrome b5. (PubMed id 16295697)¹ Tonegawa Y....Ishibashi T. (2005)
Identification and characterization of a novel splice variant of mouse and rat cytochrome b5/cytochrome b5 reductase. (PubMed id 14962668)¹ Curry B.J....Aitken R.J. (2004)
A novel plasma membrane quinone reductase and NAD(P)H:quinone oxidoreductase 1 are upregulated by serum withdrawal in human promyelocytic HL-60 cells. (PubMed id 12171070)¹ Forthoffer N....Villalba J.M. (2002)
Vaccinia virus F13L protein with a conserved phospholipase catalytic motif induces colocalization of the B5R envelope glycoprotein in post-Golgi vesicles. (PubMed id 11462025)¹ Husain M. and Moss B. (2001)
Free radical generation from heterocyclic amines by cytochrome b5 reductase in the presence of NADH. (PubMed id 10503889)¹ Maeda H....Akaike T. (1999)
NADH-methemoglobin reductase (cytochrome b5 reductase) levels in two groups of American blacks and whites. (PubMed id 9549232)¹ Mansouri A. and Nandy I. (1998)
DT-diaphorase and cytochrome B5 reductase in human lung and breast tumours. (PubMed id 9328153)¹ Marin A....Bello J. (1997)
NADH:Fe(III)-chelate reductase of maize roots is an active cytochrome b5 reductase. (PubMed id 9323038)¹ Sparla F....Trost P. (1997)
Two novel mutations in the reduced nicotinamide adenine dinucleotide (NADH)-cytochrome b5 reductase gene of a patient with generalized type, hereditary methemoglobinemia. (PubMed id 8874222)¹ Manabe J....Fukumaki Y. (1996)
The reducing ability of iron chelates by NADH-cytochrome B5 reductase or cytochrome B5 responsible for NADH-supported lipid peroxidation. (PubMed id 8653076)¹ Miura A....Yonaha M. (1995)
Cytochrome b5 reductase deficiency, an uncommon cause of cyanosis. (PubMed id 8196824)¹ Posthumus M.D. and van Berkel W. (1994)
Interaction of non-myristoylated NADH-cytochrome b5 reductase with cytochrome b5-dimyristoylphosphatidylcholine vesicles. (PubMed id 8226835)¹ Strittmatter P....Ozols J. (1993)
Role of Lys-110 of human NADH-cytochrome b5 reductase in NADH binding as probed by site-directed mutagenesis. (PubMed id 8482363)¹ Fujimoto Y....Takeshita M. (1993)
[Methemoglobinemias. Cytochrome b5-reductase deficiency] (PubMed id 8258315)¹ Thu D.T. and Damianova L. (1993)
A single mRNA, transcribed from an alternative, erythroid-specific, promoter, codes for two non-myristylated forms of NADH-cytochrome b5 reductase. (PubMed id 1577871)¹ Pietrini G....Borgese N. (1992)
Cytochrome b5-mediated redox cycling of estrogen. (PubMed id 1897935)¹ Roy D....Liehr J.G. (1991)
High-level expression in Escherichia coli of the catalytically active flavin domain of corn leaf NADH:nitrate reductase and its comparison to human NADH:cytochrome B5 reductase. (PubMed id 2189408)¹ Hyde G.E. and Campbell W.H. (1990)
NADH-cytochrome b5 reductase in a Turkish family with recessive congenital methaemoglobinaemia type I. (PubMed id 18820099)¹ Percy M.J. and Aslan D. (2008)
A novel G143D mutation in the NADH-cytochrome b5 reductase gene in an Indian patient with type I recessive hereditary methemoglobinemia. (PubMed id 17964195)¹ Kedar P.S....Ghosh K. (2008)
Structure of Physarum polycephalum cytochrome b5 reductase at 1.56 A resolution. (PubMed id 17401193)¹ Kim S....Tsukihara T. (2007)
Structure and properties of the recombinant NADH-cytochrome b5 reductase of Physarum polycephalum. (PubMed id 17341833)¹ Ikegami T....Yubisui T. (2007)
Unusual dehydroxylation of antimicrobial amidoxime prodrugs by cytochrome b5 and NADH cytochrome b5 reductase. (PubMed id 16131524)¹ Saulter J.Y....Hall J.E. (2005)
[Genetics and biochemistry of NADH-cytochrome b5 reductase] (PubMed id 15658445)¹ Shirabe K. (2004)

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Entrez Gene: 1727	HGNC: 2873	AceView: DIA1	Ensembl:ENSG00000100243	euGenes: HUgn1727
ECgene: CYB5R3	H-InvDB: CYB5R3

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