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Protein

NADH-cytochrome b5 reductase 1

Gene

CYB5R1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 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

Catalytic activityi

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

Cofactori

FADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi136 – 16631FADBy similarityAdd
BLAST
Nucleotide bindingi175 – 21036FADBy similarityAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. 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

Names & Taxonomyi

Protein namesi
Recommended name:
NADH-cytochrome b5 reductase 1 (EC:1.6.2.2)
Short name:
b5R.1
Alternative name(s):
Humb5R2
NAD(P)H:quinone oxidoreductase type 3 polypeptide A2
Gene namesi
Name:CYB5R1
Synonyms:NQO3A2
ORF Names:UNQ3049/PRO9865
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:13397. CYB5R1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei8 – 2821HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: UniProtKB
  4. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134979668.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 305305NADH-cytochrome b5 reductase 1PRO_0000287545Add
BLAST

Proteomic databases

MaxQBiQ9UHQ9.
PaxDbiQ9UHQ9.
PeptideAtlasiQ9UHQ9.
PRIDEiQ9UHQ9.

PTM databases

PhosphoSiteiQ9UHQ9.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ9UHQ9.
CleanExiHS_CYB5R1.
GenevestigatoriQ9UHQ9.

Organism-specific databases

HPAiHPA010641.
HPA014147.

Interactioni

Protein-protein interaction databases

BioGridi119690. 10 interactions.
IntActiQ9UHQ9. 2 interactions.
MINTiMINT-2873535.
STRINGi9606.ENSP00000356218.

Structurei

3D structure databases

ProteinModelPortaliQ9UHQ9.
SMRiQ9UHQ9. Positions 36-305.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 156113FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0543.
GeneTreeiENSGT00390000008881.
HOVERGENiHBG052580.
InParanoidiQ9UHQ9.
KOiK00326.
OMAiVFQEFPL.
OrthoDBiEOG7CZK69.
PhylomeDBiQ9UHQ9.
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]

Sequencei

Sequence statusi: Complete.

Q9UHQ9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGIQTSPVLL ASLGVGLVTL LGLAVGSYLV RRSRRPQVTL LDPNEKYLLR
60 70 80 90 100
LLDKTTVSHN TKRFRFALPT AHHTLGLPVG KHIYLSTRID GSLVIRPYTP
110 120 130 140 150
VTSDEDQGYV DLVIKVYLKG VHPKFPEGGK MSQYLDSLKV GDVVEFRGPS
160 170 180 190 200
GLLTYTGKGH FNIQPNKKSP PEPRVAKKLG MIAGGTGITP MLQLIRAILK
210 220 230 240 250
VPEDPTQCFL LFANQTEKDI ILREDLEELQ ARYPNRFKLW FTLDHPPKDW
260 270 280 290 300
AYSKGFVTAD MIREHLPAPG DDVLVLLCGP PPMVQLACHP NLDKLGYSQK

MRFTY
Length:305
Mass (Da):34,095
Last modified:May 1, 2000 - v1
Checksum:iDC9DAFEC619F9317
GO

Sequence cautioni

The sequence AAC72953.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAI27946.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821H → R in BAD97136. 1 PublicationCurated
Sequence conflicti92 – 921S → N in AAF06147. (PubMed:10611283)Curated
Sequence conflicti142 – 1421D → H in AAF06147. (PubMed:10611283)Curated
Sequence conflicti212 – 2121F → S in BAC11115. (PubMed:16303743)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti44 – 441N → S.
Corresponds to variant rs2232842 [ dbSNP | Ensembl ].
VAR_032320

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1431.1.
RefSeqiNP_057327.2. NM_016243.2.
UniGeneiHs.334832.

Genome annotation databases

EnsembliENST00000367249; ENSP00000356218; ENSG00000159348.
GeneIDi51706.
KEGGihsa:51706.
UCSCiuc001gyt.2. human.

Polymorphism databases

DMDMi74761957.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1431.1.
RefSeqiNP_057327.2. NM_016243.2.
UniGeneiHs.334832.

3D structure databases

ProteinModelPortaliQ9UHQ9.
SMRiQ9UHQ9. Positions 36-305.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119690. 10 interactions.
IntActiQ9UHQ9. 2 interactions.
MINTiMINT-2873535.
STRINGi9606.ENSP00000356218.

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM databases

PhosphoSiteiQ9UHQ9.

Polymorphism databases

DMDMi74761957.

Proteomic databases

MaxQBiQ9UHQ9.
PaxDbiQ9UHQ9.
PeptideAtlasiQ9UHQ9.
PRIDEiQ9UHQ9.

Protocols and materials databases

DNASUi51706.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367249; ENSP00000356218; ENSG00000159348.
GeneIDi51706.
KEGGihsa:51706.
UCSCiuc001gyt.2. human.

Organism-specific databases

CTDi51706.
GeneCardsiGC01M202930.
HGNCiHGNC:13397. CYB5R1.
HPAiHPA010641.
HPA014147.
MIMi608341. gene.
neXtProtiNX_Q9UHQ9.
PharmGKBiPA134979668.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0543.
GeneTreeiENSGT00390000008881.
HOVERGENiHBG052580.
InParanoidiQ9UHQ9.
KOiK00326.
OMAiVFQEFPL.
OrthoDBiEOG7CZK69.
PhylomeDBiQ9UHQ9.
TreeFamiTF314333.

Miscellaneous databases

ChiTaRSiCYB5R1. human.
GeneWikiiCYB5R1.
GenomeRNAii51706.
NextBioi55748.
PROiQ9UHQ9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UHQ9.
CleanExiHS_CYB5R1.
GenevestigatoriQ9UHQ9.

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], 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. 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.
    , 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] [Europe PMC] [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.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [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. 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] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Platelet.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNB5R1_HUMAN
AccessioniPrimary (citable) accession number: Q9UHQ9
Secondary accession number(s): A0PK21
, B2R8E0, O95329, Q53F73, Q8NCL5, Q9UHJ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 1, 2000
Last modified: February 4, 2015
This is version 116 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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.