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Reviewed, UniProtKB/Swiss-Prot Q9UHQ9 (NB5R1_HUMAN)

Last modified November 3, 2009. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    NADH-cytochrome b5 reductase 1
      Short name=b5R.1
    EC=1.6.2.2
Alternative name(s):
    NAD(P)H:quinone oxidoreductase type 3 polypeptide A2
    Humb5R2
Gene names
Name: CYB5R1
Synonyms: NQO3A2
ORF Names: UNQ3049/PRO9865
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length305 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

NADH-cytochrome b5 reductases are involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction By similarity.

Catalytic activity

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

Cofactor

FAD By similarity.

Subcellular location

Membrane; Single-pass membrane protein Potential.

Tissue specificity

Widely expressed. Ref.1

Sequence similarities

Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.

Contains 1 FAD-binding FR-type domain.

Ontologies

Keywords
   Biological processLipid synthesis
Steroid biosynthesis
Sterol biosynthesis
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

sterol biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncytochrome-b5 reductase activity

Inferred from electronic annotation. Source: EC

electron carrier activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 305305NADH-cytochrome b5 reductase 1
PRO_0000287545

Regions

Transmembrane8 – 2821 Potential
Domain44 – 156113FAD-binding FR-type
Nucleotide binding136 – 16631FAD By similarity
Nucleotide binding175 – 21036FAD By similarity

Natural variations

Natural variant441N → S: dbSNP rs2232842.
VAR_032320

Experimental info

Sequence conflict821H → R in BAD97136. Ref.7
Sequence conflict921S → N in AAF06147. Ref.1
Sequence conflict1421D → H in AAF06147. Ref.1
Sequence conflict2121F → S in BAC11115. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9UHQ9-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: DC9DAFEC619F9317

FASTA30534,095
        10         20         30         40         50         60 
MGIQTSPVLL ASLGVGLVTL LGLAVGSYLV RRSRRPQVTL LDPNEKYLLR LLDKTTVSHN 

        70         80         90        100        110        120 
TKRFRFALPT AHHTLGLPVG KHIYLSTRID GSLVIRPYTP VTSDEDQGYV DLVIKVYLKG 

       130        140        150        160        170        180 
VHPKFPEGGK MSQYLDSLKV GDVVEFRGPS GLLTYTGKGH FNIQPNKKSP PEPRVAKKLG 

       190        200        210        220        230        240 
MIAGGTGITP MLQLIRAILK VPEDPTQCFL LFANQTEKDI ILREDLEELQ ARYPNRFKLW 

       250        260        270        280        290        300 
FTLDHPPKDW AYSKGFVTAD MIREHLPAPG DDVLVLLCGP PPMVQLACHP NLDKLGYSQK 


MRFTY 

« Hide

References

« Hide 'large scale' references
[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: 10611283] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"Cloning of a new human cDNA homology to human NADH-cytochrome-b5 reductase mRNA."
Xu Z.G., Yu L., Yue P., Tu Q., Zheng L.H., Zhao S.Y.
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[5]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed: 16303743] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"A novel gene expressed in human adrenal gland."
Peng Y., Gu Y., Li Y., Fu S., Gu J., Zhang L., Jiang C., Yu Y., Fu G., Wang Y., Chen Z., Han Z.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Adrenal gland.
[7]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon.
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[10]"Full-insert sequence of mapped XREF EST."
Barrow I.K.-P., Boguski M.S., Touchman J., Spencer F.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 172-305.
[11]Bienvenut W.V., Claeys D.
Submitted (NOV-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 66-81 AND 140-158, MASS SPECTROMETRY.
Tissue: Platelet.
[12]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases

AF169481 mRNA. Translation: AAF06147.1.
AF087912 mRNA. Translation: AAP97209.1.
AF093822 mRNA. Translation: AAP97218.1.
AY359026 mRNA. Translation: AAQ89385.1.
AK074654 mRNA. Translation: BAC11115.1.
AF125533 mRNA. Translation: AAF17227.1.
AK223416 mRNA. Translation: BAD97136.1.
AK313333 mRNA. Translation: BAG36137.1.
CH471067 Genomic DNA. Translation: EAW91452.1.
BC018732 mRNA. Translation: AAH18732.1.
BC127945 mRNA. Translation: AAI27946.1. Different initiation.
AF091084 mRNA. Translation: AAC72953.1. Different initiation.
IPIIPI00470674.
RefSeqNP_057327.2.
UniGeneHs.334832

3D structure databases

HSSPHSSP built from PDB template 1I7P based on UniProtKB P20070.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9UHQ9. 1 interaction.
STRINGQ9UHQ9.

PTM databases

PhosphoSiteQ9UHQ9.

Proteomic databases

PeptideAtlasQ9UHQ9.
PRIDEQ9UHQ9.

Genome annotation databases

EnsemblENST00000367249; ENSP00000356218; ENSG00000159348; Homo sapiens. [Genome view]
ENST00000446185; ENSP00000396382; ENSG00000159348; Homo sapiens. [Genome view]
GeneID51706.
KEGGhsa:51706.
UCSCuc001gyt.1. human.

Organism-specific databases

CTD51706.
GeneCardsGC01M201197.
H-InvDBHIX0001483.
HGNCHGNC:13397. CYB5R1.
HPAHPA010641.
HPA014147.
MIM608341. gene.
PharmGKBPA134979668.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ9UHQ9.
OMALWFTLDH.

Enzyme and pathway databases

BRENDA1.6.2.2. 247.

Gene expression databases

ArrayExpressQ9UHQ9.
BgeeQ9UHQ9.
CleanExHS_CYB5R1.
GenevestigatorQ9UHQ9.

Family and domain databases

InterProIPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR001834. NADH-Cyt_B5_reductase.
IPR008333. OxRdtase_FAD-bd.
IPR001433. OxRdtase_FAD/NAD_bd.
[Graphical view]
PfamPF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSPR00406. CYTB5RDTASE.
PR00371. FPNCR.
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio55748.
SOURCESearch...

Entry information

Entry nameNB5R1_HUMAN
AccessionPrimary (citable) accession number: Q9UHQ9
Secondary accession number(s): A0PK21 expand/collapse secondary AC list , B2R8E0, O95329, Q53F73, Q8NCL5, Q9UHJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 1, 2000
Last modified: November 3, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents