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Q9UHQ9

- NB5R1_HUMAN

UniProt

Q9UHQ9 - NB5R1_HUMAN

Protein

NADH-cytochrome b5 reductase 1

Gene

CYB5R1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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

    FAD.By 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

    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

    GO - Cellular componenti

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

    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. 5 interactions.
    IntActiQ9UHQ9. 2 interactions.
    MINTiMINT-2873535.
    STRINGi9606.ENSP00000356218.

    Structurei

    3D structure databases

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

    Transmembrane

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

    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.
    HOVERGENiHBG052580.
    InParanoidiQ9UHQ9.
    KOiK00326.
    OMAiMKVGDYL.
    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

    MGIQTSPVLL ASLGVGLVTL LGLAVGSYLV RRSRRPQVTL LDPNEKYLLR    50
    LLDKTTVSHN TKRFRFALPT AHHTLGLPVG KHIYLSTRID GSLVIRPYTP 100
    VTSDEDQGYV DLVIKVYLKG VHPKFPEGGK MSQYLDSLKV GDVVEFRGPS 150
    GLLTYTGKGH FNIQPNKKSP PEPRVAKKLG MIAGGTGITP MLQLIRAILK 200
    VPEDPTQCFL LFANQTEKDI ILREDLEELQ ARYPNRFKLW FTLDHPPKDW 250
    AYSKGFVTAD MIREHLPAPG DDVLVLLCGP PPMVQLACHP NLDKLGYSQK 300
    MRFTY 305
    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.
    The sequence AAI27946.1 differs from that shown. Reason: Erroneous initiation.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS1431.1.
    RefSeqi NP_057327.2. NM_016243.2.
    UniGenei Hs.334832.

    3D structure databases

    ProteinModelPortali Q9UHQ9.
    SMRi Q9UHQ9. Positions 36-305.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119690. 5 interactions.
    IntActi Q9UHQ9. 2 interactions.
    MINTi MINT-2873535.
    STRINGi 9606.ENSP00000356218.

    PTM databases

    PhosphoSitei Q9UHQ9.

    Polymorphism databases

    DMDMi 74761957.

    Proteomic databases

    MaxQBi Q9UHQ9.
    PaxDbi Q9UHQ9.
    PeptideAtlasi Q9UHQ9.
    PRIDEi Q9UHQ9.

    Protocols and materials databases

    DNASUi 51706.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367249 ; ENSP00000356218 ; ENSG00000159348 .
    GeneIDi 51706.
    KEGGi hsa:51706.
    UCSCi uc001gyt.2. human.

    Organism-specific databases

    CTDi 51706.
    GeneCardsi GC01M202930.
    HGNCi HGNC:13397. CYB5R1.
    HPAi HPA010641.
    HPA014147.
    MIMi 608341. gene.
    neXtProti NX_Q9UHQ9.
    PharmGKBi PA134979668.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0543.
    HOVERGENi HBG052580.
    InParanoidi Q9UHQ9.
    KOi K00326.
    OMAi MKVGDYL.
    OrthoDBi EOG7CZK69.
    PhylomeDBi Q9UHQ9.
    TreeFami TF314333.

    Miscellaneous databases

    ChiTaRSi CYB5R1. human.
    GeneWikii CYB5R1.
    GenomeRNAii 51706.
    NextBioi 55748.
    PROi Q9UHQ9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9UHQ9.
    CleanExi HS_CYB5R1.
    Genevestigatori Q9UHQ9.

    Family and domain databases

    InterProi IPR017927. 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 ]
    Pfami PF00970. FAD_binding_6. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00406. CYTB5RDTASE.
    PR00371. FPNCR.
    SUPFAMi SSF63380. SSF63380. 1 hit.
    PROSITEi PS51384. FAD_FR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 112 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