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Protein

NADH-cytochrome b5 reductase 2

Gene

CYB5R2

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

Functioni

NADH-cytochrome b5 reductases are involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction (By similarity). Responsible for NADH-dependent lucigenin chemiluminescence in spermatozoa by reducing both lucigenin and 2-[4-iodophenyl]-3-[4-nitrophenyl]-5-[2,4-disulfophenyl]-2H tetrazolium monosodium salt (WST-1).By similarity1 Publication

Catalytic activityi

NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5.

Cofactori

FADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi107 – 13731FADBy similarityAdd
BLAST
Nucleotide bindingi146 – 18136FADBy similarityAdd
BLAST

GO - Molecular functioni

  • cytochrome-b5 reductase activity, acting on NAD(P)H Source: UniProtKB

GO - Biological processi

  • oxidation-reduction process Source: UniProtKB
  • sterol biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

BRENDAi1.6.2.2. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
NADH-cytochrome b5 reductase 2 (EC:1.6.2.2)
Short name:
b5R.2
Gene namesi
Name:CYB5R2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:24376. CYB5R2.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: UniProtKB
  • mitochondrion Source: Ensembl
  • nucleus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142672060.

Polymorphism and mutation databases

BioMutaiCYB5R2.
DMDMi74709211.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 276276NADH-cytochrome b5 reductase 2PRO_0000287548Add
BLAST

Proteomic databases

MaxQBiQ6BCY4.
PaxDbiQ6BCY4.
PRIDEiQ6BCY4.

2D gel databases

REPRODUCTION-2DPAGEIPI00332396.

PTM databases

PhosphoSiteiQ6BCY4.

Expressioni

Tissue specificityi

Restricted expression.1 Publication

Gene expression databases

BgeeiQ6BCY4.
CleanExiHS_CYB5R2.
ExpressionAtlasiQ6BCY4. baseline and differential.
GenevisibleiQ6BCY4. HS.

Organism-specific databases

HPAiHPA038962.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC23Q9UJX23EBI-744761,EBI-396137
GOLGA2Q083793EBI-744761,EBI-618309
PSMC6P623333EBI-744761,EBI-357669
TRAF1Q130773EBI-744761,EBI-359224
TRAF2Q129333EBI-744761,EBI-355744
TRIP13Q156454EBI-744761,EBI-358993

Protein-protein interaction databases

BioGridi119684. 8 interactions.
IntActiQ6BCY4. 8 interactions.
MINTiMINT-1447606.
STRINGi9606.ENSP00000299498.

Structurei

3D structure databases

ProteinModelPortaliQ6BCY4.
SMRiQ6BCY4. Positions 9-276.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 127113FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0543.
GeneTreeiENSGT00390000008881.
HOGENOMiHOG000175005.
HOVERGENiHBG052580.
InParanoidiQ6BCY4.
KOiK00326.
OMAiYAPEMQF.
OrthoDBiEOG7CZK69.
PhylomeDBiQ6BCY4.
TreeFamiTF314333.

Family and domain databases

InterProiIPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR001834. NADH-Cyt_B5_reductase.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00406. CYTB5RDTASE.
PR00371. FPNCR.
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6BCY4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNSRRREPIT LQDPEAKYPL PLIEKEKISH NTRRFRFGLP SPDHVLGLPV
60 70 80 90 100
GNYVQLLAKI DNELVVRAYT PVSSDDDRGF VDLIIKIYFK NVHPQYPEGG
110 120 130 140 150
KMTQYLENMK IGETIFFRGP RGRLFYHGPG NLGIRPDQTS EPKKTLADHL
160 170 180 190 200
GMIAGGTGIT PMLQLIRHIT KDPSDRTRMS LIFANQTEED ILVRKELEEI
210 220 230 240 250
ARTHPDQFNL WYTLDRPPIG WKYSSGFVTA DMIKEHLPPP AKSTLILVCG
260 270
PPPLIQTAAH PNLEKLGYTQ DMIFTY
Length:276
Mass (Da):31,458
Last modified:September 13, 2004 - v1
Checksum:iA475039D1E56ABDA
GO
Isoform 2 (identifier: Q6BCY4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     221-276: WKYSSGFVTADMIKEHLPPPAKSTLILVCGPPPLIQTAAHPNLEKLGYTQDMIFTY → PWSAEGATLLSNSAQFH

Note: No experimental confirmation available.
Show »
Length:237
Mass (Da):27,043
Checksum:i54044C015E5D4CA0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti130 – 1301G → R in AAF04811 (PubMed:10611283).Curated
Sequence conflicti253 – 2531P → T in AAF04811 (PubMed:10611283).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151E → A.
Corresponds to variant rs11041525 [ dbSNP | Ensembl ].
VAR_032321
Natural varianti209 – 2091N → D.3 Publications
Corresponds to variant rs12801394 [ dbSNP | Ensembl ].
VAR_032322

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei221 – 27656WKYSS…MIFTY → PWSAEGATLLSNSAQFH in isoform 2. 1 PublicationVSP_025559Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF169802 mRNA. Translation: AAF04811.1.
AY665398 mRNA. Translation: AAT75296.1.
BC001346 mRNA. Translation: AAH01346.1.
AL133582 mRNA. Translation: CAB63726.1.
CCDSiCCDS7780.1. [Q6BCY4-1]
PIRiT43491.
RefSeqiNP_001289755.1. NM_001302826.1. [Q6BCY4-1]
NP_057313.2. NM_016229.4. [Q6BCY4-1]
XP_005253032.1. XM_005252975.3. [Q6BCY4-1]
XP_006718314.1. XM_006718251.2. [Q6BCY4-1]
XP_006718315.1. XM_006718252.2. [Q6BCY4-1]
UniGeneiHs.414362.

Genome annotation databases

EnsembliENST00000299498; ENSP00000299498; ENSG00000166394.
ENST00000524790; ENSP00000435916; ENSG00000166394. [Q6BCY4-2]
ENST00000533558; ENSP00000437041; ENSG00000166394.
GeneIDi51700.
KEGGihsa:51700.
UCSCiuc001mfm.3. human. [Q6BCY4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF169802 mRNA. Translation: AAF04811.1.
AY665398 mRNA. Translation: AAT75296.1.
BC001346 mRNA. Translation: AAH01346.1.
AL133582 mRNA. Translation: CAB63726.1.
CCDSiCCDS7780.1. [Q6BCY4-1]
PIRiT43491.
RefSeqiNP_001289755.1. NM_001302826.1. [Q6BCY4-1]
NP_057313.2. NM_016229.4. [Q6BCY4-1]
XP_005253032.1. XM_005252975.3. [Q6BCY4-1]
XP_006718314.1. XM_006718251.2. [Q6BCY4-1]
XP_006718315.1. XM_006718252.2. [Q6BCY4-1]
UniGeneiHs.414362.

3D structure databases

ProteinModelPortaliQ6BCY4.
SMRiQ6BCY4. Positions 9-276.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119684. 8 interactions.
IntActiQ6BCY4. 8 interactions.
MINTiMINT-1447606.
STRINGi9606.ENSP00000299498.

PTM databases

PhosphoSiteiQ6BCY4.

Polymorphism and mutation databases

BioMutaiCYB5R2.
DMDMi74709211.

2D gel databases

REPRODUCTION-2DPAGEIPI00332396.

Proteomic databases

MaxQBiQ6BCY4.
PaxDbiQ6BCY4.
PRIDEiQ6BCY4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000299498; ENSP00000299498; ENSG00000166394.
ENST00000524790; ENSP00000435916; ENSG00000166394. [Q6BCY4-2]
ENST00000533558; ENSP00000437041; ENSG00000166394.
GeneIDi51700.
KEGGihsa:51700.
UCSCiuc001mfm.3. human. [Q6BCY4-1]

Organism-specific databases

CTDi51700.
GeneCardsiGC11M007642.
HGNCiHGNC:24376. CYB5R2.
HPAiHPA038962.
MIMi608342. gene.
neXtProtiNX_Q6BCY4.
PharmGKBiPA142672060.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0543.
GeneTreeiENSGT00390000008881.
HOGENOMiHOG000175005.
HOVERGENiHBG052580.
InParanoidiQ6BCY4.
KOiK00326.
OMAiYAPEMQF.
OrthoDBiEOG7CZK69.
PhylomeDBiQ6BCY4.
TreeFamiTF314333.

Enzyme and pathway databases

BRENDAi1.6.2.2. 2681.

Miscellaneous databases

GeneWikiiCYB5R2.
GenomeRNAii51700.
NextBioi55720.
PROiQ6BCY4.
SOURCEiSearch...

Gene expression databases

BgeeiQ6BCY4.
CleanExiHS_CYB5R2.
ExpressionAtlasiQ6BCY4. baseline and differential.
GenevisibleiQ6BCY4. HS.

Family and domain databases

InterProiIPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR001834. NADH-Cyt_B5_reductase.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00406. CYTB5RDTASE.
PR00371. FPNCR.
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a cytochrome b-type NAD(P)H oxidoreductase ubiquitously expressed in human cells."
    Zhu H., Qiu H., Yoon H.-W., Huang S., Bunn H.F.
    Proc. Natl. Acad. Sci. U.S.A. 96:14742-14747(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT ASP-209.
  2. "Identification of cytochrome-b5 reductase as the enzyme responsible for NADH-dependent lucigenin chemiluminescence in human spermatozoa."
    Baker M.A., Krutskikh A., Curry B.J., Hetherington L., Aitken R.J.
    Biol. Reprod. 73:334-342(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
  3. "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] (ISOFORM 2), VARIANT ASP-209.
    Tissue: Placenta.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-276 (ISOFORM 1), VARIANT ASP-209.
    Tissue: Testis.

Entry informationi

Entry nameiNB5R2_HUMAN
AccessioniPrimary (citable) accession number: Q6BCY4
Secondary accession number(s): Q9BVA3, Q9UF68, Q9UHJ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: September 13, 2004
Last modified: July 22, 2015
This is version 94 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

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