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P00387

- NB5R3_HUMAN

UniProt

P00387 - NB5R3_HUMAN

Protein

NADH-cytochrome b5 reductase 3

Gene

CYB5R3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 196 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction.

    Catalytic activityi

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

    Cofactori

    FAD.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi132 – 14716FADBy similarityAdd
    BLAST
    Nucleotide bindingi171 – 20636FADBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. ADP binding Source: Ensembl
    2. AMP binding Source: Ensembl
    3. cytochrome-b5 reductase activity, acting on NAD(P)H Source: Reactome
    4. FAD binding Source: UniProtKB
    5. flavin adenine dinucleotide binding Source: Ensembl
    6. NAD binding Source: Ensembl

    GO - Biological processi

    1. blood circulation Source: ProtInc
    2. cholesterol biosynthetic process Source: UniProtKB-KW
    3. L-ascorbic acid metabolic process Source: Reactome
    4. small molecule metabolic process Source: Reactome
    5. vitamin metabolic process Source: Reactome
    6. water-soluble vitamin metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

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

    Keywords - Ligandi

    FAD, Flavoprotein, NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02015-MONOMER.
    BRENDAi1.6.2.2. 2681.
    ReactomeiREACT_11202. Vitamin C (ascorbate) metabolism.
    SABIO-RKP00387.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADH-cytochrome b5 reductase 3 (EC:1.6.2.2)
    Short name:
    B5R
    Short name:
    Cytochrome b5 reductase
    Alternative name(s):
    Diaphorase-1
    Cleaved into the following 2 chains:
    Gene namesi
    Name:CYB5R3
    Synonyms:DIA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:2873. CYB5R3.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. endoplasmic reticulum Source: HPA
    3. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    4. extracellular vesicular exosome Source: UniProt
    5. hemoglobin complex Source: ProtInc
    6. lipid particle Source: UniProtKB
    7. membrane Source: UniProtKB
    8. mitochondrial inner membrane Source: Ensembl
    9. mitochondrial outer membrane Source: Reactome
    10. mitochondrion Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Involvement in diseasei

    Methemoglobinemia CYB5R3-related (METHB-CYB5R3) [MIM:250800]: A form of methemoglobinemia, a hematologic disease characterized by the presence of excessive amounts of methemoglobin in blood cells, resulting in decreased oxygen carrying capacity of the blood, cyanosis and hypoxia. There are two types of methemoglobinemia CYB5R3-related. In type 1, the defect affects the soluble form of the enzyme, is restricted to red blood cells, and causes well-tolerated methemoglobinemia. In type 2, the defect affects both the soluble and microsomal forms of the enzyme and is thus generalized, affecting red cells, leukocytes and all body tissues. Type 2 methemoglobinemia is associated with mental deficiency and other neurologic symptoms.10 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti58 – 581R → Q in METHB-CYB5R3; type 1; 62% of activity. 3 Publications
    VAR_004619
    Natural varianti73 – 731L → P in METHB-CYB5R3; type 1. 2 Publications
    VAR_010750
    Natural varianti106 – 1061V → M in METHB-CYB5R3; type 1; 77% of activity. 1 Publication
    Corresponds to variant rs121965009 [ dbSNP | Ensembl ].
    VAR_004620
    Natural varianti128 – 1281S → P in METHB-CYB5R3; type 2; Hiroshima. 1 Publication
    VAR_004621
    Natural varianti149 – 1491L → P in METHB-CYB5R3. 1 Publication
    VAR_004622
    Natural varianti179 – 1791A → V in METHB-CYB5R3; type 1. 1 Publication
    Corresponds to variant rs201232518 [ dbSNP | Ensembl ].
    VAR_010752
    Natural varianti204 – 2041C → R in METHB-CYB5R3; type 2. 1 Publication
    VAR_010753
    Natural varianti204 – 2041C → Y in METHB-CYB5R3; type 1. 2 Publications
    VAR_010754
    Natural varianti256 – 2561Missing in METHB-CYB5R3; type 1; retains approximately 38% of residual diaphorase activity. 1 Publication
    VAR_037315
    Natural varianti273 – 2731Missing in METHB-CYB5R3; type 2. 1 Publication
    VAR_010755
    Natural varianti292 – 2921G → D in METHB-CYB5R3; type 1; retains approximately 58% of residual diaphorase activity. 1 Publication
    VAR_037316
    Natural varianti299 – 2991Missing in METHB-CYB5R3; type2; almost complete loss of activity. 1 Publication
    VAR_004623

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi250800. phenotype.
    Orphaneti139373. Recessive hereditary methemoglobinemia type 1.
    139380. Recessive hereditary methemoglobinemia type 2.
    PharmGKBiPA27331.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 301300NADH-cytochrome b5 reductase 3 membrane-bound formPRO_0000019392Add
    BLAST
    Chaini27 – 301275NADH-cytochrome b5 reductase 3 soluble formPRO_0000019394Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine1 Publication
    Modified residuei42 – 421N6-acetyllysine1 Publication
    Modified residuei43 – 431Phosphotyrosine1 Publication
    Modified residuei120 – 1201N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Lipoprotein, Myristate, Phosphoprotein

    Proteomic databases

    MaxQBiP00387.
    PaxDbiP00387.
    PRIDEiP00387.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00446235.

    PTM databases

    PhosphoSiteiP00387.

    Expressioni

    Tissue specificityi

    Isoform 2 is expressed at late stages of erythroid maturation.

    Gene expression databases

    ArrayExpressiP00387.
    BgeeiP00387.
    CleanExiHS_CYB5R3.
    GenevestigatoriP00387.

    Organism-specific databases

    HPAiHPA001566.

    Interactioni

    Subunit structurei

    Component of a complex composed of cytochrome b5, NADH-cytochrome b5 reductase (CYB5R3) and MOSC2.By similarity

    Protein-protein interaction databases

    BioGridi108071. 8 interactions.
    DIPiDIP-50463N.
    IntActiP00387. 2 interactions.
    MINTiMINT-5003981.

    Structurei

    Secondary structure

    1
    301
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi43 – 5210
    Beta strandi54 – 6310
    Beta strandi78 – 858
    Beta strandi88 – 947
    Beta strandi104 – 1118
    Beta strandi115 – 1184
    Helixi126 – 1338
    Beta strandi139 – 1468
    Beta strandi148 – 1536
    Beta strandi156 – 1594
    Beta strandi168 – 1714
    Beta strandi173 – 1808
    Helixi181 – 1833
    Helixi184 – 19512
    Beta strandi203 – 21210
    Helixi213 – 2153
    Helixi219 – 22810
    Turni230 – 2323
    Beta strandi233 – 2419
    Beta strandi247 – 2526
    Helixi255 – 2617
    Helixi265 – 2673
    Beta strandi270 – 2756
    Helixi277 – 2826
    Helixi285 – 2917
    Helixi295 – 2973
    Beta strandi298 – 3003

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M91model-A1-301[»]
    1UMKX-ray1.75A27-301[»]
    ProteinModelPortaliP00387.
    SMRiP00387. Positions 31-301.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00387.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini40 – 152113FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0543.
    HOGENOMiHOG000175005.
    HOVERGENiHBG052580.
    InParanoidiP00387.
    KOiK00326.
    OMAiVFQEFPL.
    OrthoDBiEOG7CZK69.
    PhylomeDBiP00387.
    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 (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative promoter usage and alternative splicing. Align

    Isoform 1 (identifier: P00387-1) [UniParc]FASTAAdd to Basket

    Also known as: M

    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

    MGAQLSTLGH MVLFPVWFLY SLLMKLFQRS TPAITLESPD IKYPLRLIDR    50
    EIISHDTRRF RFALPSPQHI LGLPVGQHIY LSARIDGNLV VRPYTPISSD 100
    DDKGFVDLVI KVYFKDTHPK FPAGGKMSQY LESMQIGDTI EFRGPSGLLV 150
    YQGKGKFAIR PDKKSNPIIR TVKSVGMIAG GTGITPMLQV IRAIMKDPDD 200
    HTVCHLLFAN QTEKDILLRP ELEELRNKHS ARFKLWYTLD RAPEAWDYGQ 250
    GFVNEEMIRD HLPPPEEEPL VLMCGPPPMI QYACLPNLDH VGHPTERCFV 300
    F 301
    Length:301
    Mass (Da):34,235
    Last modified:January 23, 2007 - v3
    Checksum:iFDCDCDC4EC3570B4
    GO
    Isoform 2 (identifier: P00387-2) [UniParc]FASTAAdd to Basket

    Also known as: S

    The sequence of this isoform differs from the canonical sequence as follows:
         2-23: Missing.

    Show »
    Length:279
    Mass (Da):31,760
    Checksum:i033CBEBCDB564606
    GO
    Isoform 3 (identifier: P00387-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-7: GAQLST → MNRSLLVGCMQSKDIWGREESICERLKQDGLDVERAESWE

    Note: No experimental confirmation available.

    Show »
    Length:335
    Mass (Da):38,358
    Checksum:i34EB129AA0EC65DB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti28 – 325QRSTP → RWPRA in AAA52307. (PubMed:3035541)Curated
    Sequence conflicti29 – 291R → G in AAA59900. (PubMed:2479590)Curated
    Sequence conflicti31 – 311T → K in CAA09006. 1 PublicationCurated
    Sequence conflicti31 – 311T → K in CAA09007. 1 PublicationCurated
    Sequence conflicti31 – 311T → K in CAA09008. 1 PublicationCurated
    Sequence conflicti34 – 352IT → LA in AAA52307. (PubMed:3035541)Curated
    Sequence conflicti187 – 1882ML → IV in CAA09006. 1 PublicationCurated
    Sequence conflicti187 – 1882ML → IV in CAA09007. 1 PublicationCurated
    Sequence conflicti191 – 1922IR → MS in CAA09006. 1 PublicationCurated
    Sequence conflicti191 – 1922IR → MS in CAA09007. 1 PublicationCurated
    Sequence conflicti192 – 1921R → G in AAA52306. (PubMed:3035541)Curated
    Sequence conflicti233 – 2342FK → CN in CAA09006. 1 PublicationCurated
    Sequence conflicti233 – 2342FK → CN in CAA09007. 1 PublicationCurated
    Sequence conflicti280 – 2801I → N in AAL87744. 1 PublicationCurated

    Polymorphismi

    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.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti58 – 581R → Q in METHB-CYB5R3; type 1; 62% of activity. 3 Publications
    VAR_004619
    Natural varianti66 – 661S → P.3 Publications
    Corresponds to variant rs1130706 [ dbSNP | Ensembl ].
    VAR_018419
    Natural varianti73 – 731L → P in METHB-CYB5R3; type 1. 2 Publications
    VAR_010750
    Natural varianti106 – 1061V → M in METHB-CYB5R3; type 1; 77% of activity. 1 Publication
    Corresponds to variant rs121965009 [ dbSNP | Ensembl ].
    VAR_004620
    Natural varianti117 – 1171T → S.2 Publications
    Corresponds to variant rs1800457 [ dbSNP | Ensembl ].
    VAR_010751
    Natural varianti128 – 1281S → P in METHB-CYB5R3; type 2; Hiroshima. 1 Publication
    VAR_004621
    Natural varianti149 – 1491L → P in METHB-CYB5R3. 1 Publication
    VAR_004622
    Natural varianti179 – 1791A → V in METHB-CYB5R3; type 1. 1 Publication
    Corresponds to variant rs201232518 [ dbSNP | Ensembl ].
    VAR_010752
    Natural varianti204 – 2041C → R in METHB-CYB5R3; type 2. 1 Publication
    VAR_010753
    Natural varianti204 – 2041C → Y in METHB-CYB5R3; type 1. 2 Publications
    VAR_010754
    Natural varianti256 – 2561Missing in METHB-CYB5R3; type 1; retains approximately 38% of residual diaphorase activity. 1 Publication
    VAR_037315
    Natural varianti273 – 2731Missing in METHB-CYB5R3; type 2. 1 Publication
    VAR_010755
    Natural varianti292 – 2921G → D in METHB-CYB5R3; type 1; retains approximately 58% of residual diaphorase activity. 1 Publication
    VAR_037316
    Natural varianti299 – 2991Missing in METHB-CYB5R3; type2; almost complete loss of activity. 1 Publication
    VAR_004623

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 2322Missing in isoform 2. CuratedVSP_010200Add
    BLAST
    Alternative sequencei2 – 76GAQLST → MNRSLLVGCMQSKDIWGREE SICERLKQDGLDVERAESWE in isoform 3. 1 PublicationVSP_042827

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M28713
    , M28705, M28706, M28707, M28708, M28709, M28710, M28711 Genomic DNA. Translation: AAA59900.1.
    Y09501 mRNA. Translation: CAA70696.1.
    AF361370 mRNA. Translation: AAL87744.1.
    AJ010116 mRNA. Translation: CAA09006.1.
    AJ010117 mRNA. Translation: CAA09007.1.
    AJ010118 mRNA. Translation: CAA09008.1.
    AY341030 Genomic DNA. Translation: AAP88936.1.
    BT009821 mRNA. Translation: AAP88823.1.
    CR456435 mRNA. Translation: CAG30321.1.
    AF061830 Genomic DNA. Translation: AAF06818.1.
    AF061831 Genomic DNA. Translation: AAF06819.1.
    AK302204 mRNA. Translation: BAH13649.1.
    Z93241 Genomic DNA. Translation: CAB42843.1.
    Z93241 Genomic DNA. Translation: CAQ08414.1.
    BC004821 mRNA. Translation: AAH04821.1.
    AJ310899 mRNA. Translation: CAC84523.1.
    AJ310900 mRNA. Translation: CAC84524.1.
    M16461 mRNA. Translation: AAA52306.1.
    M16462 mRNA. Translation: AAA52307.1.
    CCDSiCCDS33658.1. [P00387-1]
    PIRiJS0468. RDHUB5.
    RefSeqiNP_000389.1. NM_000398.6. [P00387-1]
    NP_001123291.1. NM_001129819.2.
    NP_001165131.1. NM_001171660.1.
    NP_015565.1. NM_007326.4.
    UniGeneiHs.561064.

    Genome annotation databases

    EnsembliENST00000352397; ENSP00000338461; ENSG00000100243. [P00387-1]
    ENST00000361740; ENSP00000354468; ENSG00000100243. [P00387-3]
    GeneIDi1727.
    KEGGihsa:1727.
    UCSCiuc003bcx.3. human. [P00387-1]
    uc011aps.2. human. [P00387-3]

    Polymorphism databases

    DMDMi127846.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M28713
    , M28705 , M28706 , M28707 , M28708 , M28709 , M28710 , M28711 Genomic DNA. Translation: AAA59900.1 .
    Y09501 mRNA. Translation: CAA70696.1 .
    AF361370 mRNA. Translation: AAL87744.1 .
    AJ010116 mRNA. Translation: CAA09006.1 .
    AJ010117 mRNA. Translation: CAA09007.1 .
    AJ010118 mRNA. Translation: CAA09008.1 .
    AY341030 Genomic DNA. Translation: AAP88936.1 .
    BT009821 mRNA. Translation: AAP88823.1 .
    CR456435 mRNA. Translation: CAG30321.1 .
    AF061830 Genomic DNA. Translation: AAF06818.1 .
    AF061831 Genomic DNA. Translation: AAF06819.1 .
    AK302204 mRNA. Translation: BAH13649.1 .
    Z93241 Genomic DNA. Translation: CAB42843.1 .
    Z93241 Genomic DNA. Translation: CAQ08414.1 .
    BC004821 mRNA. Translation: AAH04821.1 .
    AJ310899 mRNA. Translation: CAC84523.1 .
    AJ310900 mRNA. Translation: CAC84524.1 .
    M16461 mRNA. Translation: AAA52306.1 .
    M16462 mRNA. Translation: AAA52307.1 .
    CCDSi CCDS33658.1. [P00387-1 ]
    PIRi JS0468. RDHUB5.
    RefSeqi NP_000389.1. NM_000398.6. [P00387-1 ]
    NP_001123291.1. NM_001129819.2.
    NP_001165131.1. NM_001171660.1.
    NP_015565.1. NM_007326.4.
    UniGenei Hs.561064.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1M91 model - A 1-301 [» ]
    1UMK X-ray 1.75 A 27-301 [» ]
    ProteinModelPortali P00387.
    SMRi P00387. Positions 31-301.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108071. 8 interactions.
    DIPi DIP-50463N.
    IntActi P00387. 2 interactions.
    MINTi MINT-5003981.

    Chemistry

    ChEMBLi CHEMBL2146.
    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei P00387.

    Polymorphism databases

    DMDMi 127846.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00446235.

    Proteomic databases

    MaxQBi P00387.
    PaxDbi P00387.
    PRIDEi P00387.

    Protocols and materials databases

    DNASUi 1727.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000352397 ; ENSP00000338461 ; ENSG00000100243 . [P00387-1 ]
    ENST00000361740 ; ENSP00000354468 ; ENSG00000100243 . [P00387-3 ]
    GeneIDi 1727.
    KEGGi hsa:1727.
    UCSCi uc003bcx.3. human. [P00387-1 ]
    uc011aps.2. human. [P00387-3 ]

    Organism-specific databases

    CTDi 1727.
    GeneCardsi GC22M043014.
    HGNCi HGNC:2873. CYB5R3.
    HPAi HPA001566.
    MIMi 250800. phenotype.
    613213. gene.
    neXtProti NX_P00387.
    Orphaneti 139373. Recessive hereditary methemoglobinemia type 1.
    139380. Recessive hereditary methemoglobinemia type 2.
    PharmGKBi PA27331.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0543.
    HOGENOMi HOG000175005.
    HOVERGENi HBG052580.
    InParanoidi P00387.
    KOi K00326.
    OMAi VFQEFPL.
    OrthoDBi EOG7CZK69.
    PhylomeDBi P00387.
    TreeFami TF314333.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS02015-MONOMER.
    BRENDAi 1.6.2.2. 2681.
    Reactomei REACT_11202. Vitamin C (ascorbate) metabolism.
    SABIO-RK P00387.

    Miscellaneous databases

    EvolutionaryTracei P00387.
    GeneWikii CYB5R3.
    GenomeRNAii 1727.
    NextBioi 6983.
    PROi P00387.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P00387.
    Bgeei P00387.
    CleanExi HS_CYB5R3.
    Genevestigatori P00387.

    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. "The organization and the complete nucleotide sequence of the human NADH-cytochrome b5 reductase gene."
      Tomatsu S., Kobayashi Y., Fukumaki Y., Yubisui T., Orii T., Sakaki Y.
      Gene 80:353-361(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PRO-66.
      Tissue: Placenta.
    2. Voice M.W.
      Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    3. Yoon B., Chung H., Ko E., Lee D.
      Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. Lan F.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PRO-66, VARIANTS HM GLN-58; PRO-73 AND TYR-204.
      Tissue: Leukocyte.
    5. NIEHS SNPs program
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-117.
    6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    8. "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] (ISOFORM 3).
      Tissue: Testis.
    9. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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 1).
      Tissue: Placenta.
    11. "Molecular cloning of cDNAs of human liver and placenta NADH-cytochrome b5 reductase."
      Yubisui T., Naitoh Y., Zenno S., Tamura M., Takeshita M., Sakaki Y.
      Proc. Natl. Acad. Sci. U.S.A. 84:3609-3613(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-301 (ISOFORM 1), VARIANT PRO-66.
      Tissue: Liver.
    12. "Upregulation of voltage-gated Na+ channel expression and metastatic potential in human breast cancer: correlative studies on cell lines and biopsy tissues."
      Diss J.K.J., Fraser S.P., Coombes R.C., Djamgoz M.B.A.
      Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 101-250 (ISOFORM 1).
    13. "The NH2-terminal structures of human and rat liver microsomal NADH-cytochrome b5 reductases."
      Murakami K., Yubisui T., Takeshita M., Miyata T.
      J. Biochem. 105:312-317(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-25, MYRISTOYLATION AT GLY-2.
    14. "Complete amino acid sequence of NADH-cytochrome b5 reductase purified from human erythrocytes."
      Yubisui T., Miyata T., Iwanaga S., Tamura M., Takeshita M.
      J. Biochem. 99:407-422(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-301.
      Tissue: Erythrocyte.
    15. "Amino acid sequence of NADH-cytochrome b5 reductase of human erythrocytes."
      Yubisui T., Miyata T., Iwanaga S., Tamura M., Yoshida S., Takeshita M., Nakajima H.
      J. Biochem. 96:579-582(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-301.
      Tissue: Erythrocyte.
    16. "An erythroid-specific transcript generates the soluble form of NADH-cytochrome b5 reductase in humans."
      Bulbarelli A., Valentini A., De Silvestris M., Cappellini M.D., Borgese N.
      Blood 92:310-319(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE PROMOTER USAGE.
    17. "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."
      Shirabe K., Yubisui T., Nishino T., Takeshita M.
      J. Biol. Chem. 266:7531-7536(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYSTEINE RESIDUES.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 31-301.
    22. "Structural role of serine 127 in the NADH-binding site of human NADH-cytochrome b5 reductase."
      Yubisui T., Shirabe K., Takeshita M., Kobayashi Y., Fukumaki Y., Sakaki Y., Takano T.
      J. Biol. Chem. 266:66-70(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT METHB-CYB5R3 PRO-128.
    23. "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."
      Katsube T., Sakamoto N., Kobayashi Y., Seki R., Hirano M., Tanishima K., Tomoda A., Takazakura E., Yubisui T., Takeshita M., Sakaki Y., Fukumaki Y.
      Am. J. Hum. Genet. 48:799-808(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS METHB-CYB5R3 GLN-58 AND PRO-149.
    24. "Enzymatic instability of NADH-cytochrome b5 reductase as a cause of hereditary methemoglobinemia type I (red cell type)."
      Shirabe K., Yubisui T., Borgese N., Tang C.-Y., Hultquist D.E., Takeshita M.
      J. Biol. Chem. 267:20416-20421(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT METHB-CYB5R3 MET-106.
    25. "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."
      Shirabe K., Fujimoto Y., Yubisui T., Takeshita M.
      J. Biol. Chem. 269:5952-5957(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT METHB-CYB5R3 PHE-299 DEL.
    26. "Four new mutations in the NADH-cytochrome b5 reductase gene from patients with recessive congenital methemoglobinemia type II."
      Vieira L.M., Kaplan J.-C., Kahn A., Leroux A.
      Blood 85:2254-2262(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS METHB-CYB5R3 ARG-204 AND MET-273 DEL.
    27. "A high-frequency polymorphism of NADH-cytochrome b5 reductase in African-Americans."
      Jenkins M.M., Prchal J.T.
      Hum. Genet. 99:248-250(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SER-117.
    28. "Identification of a novel point mutation (Leu72-to-Pro) in the NADH-cytochrome b5 reductase gene of a patient with hereditary methaemoglobinaemia type I."
      Wu Y.-S., Huang C.-H., Wan Y., Huang Q.-J., Zhu Z.-Y.
      Br. J. Haematol. 102:575-577(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT METHB-CYB5R3 PRO-73.
    29. "Molecular basis of hereditary methaemoglobinaemia, types I and II: two novel mutations in the NADH-cytochrome b5 reductase gene."
      Higasa K., Manabe J.I., Yubisui T., Sumimoto H., Pung-Amritt P., Tanphaichitr V.S., Fukumaki Y.
      Br. J. Haematol. 103:922-930(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-83 AND 171-187, VARIANT METHB-CYB5R3 VAL-179.
    30. "A novel mutation in the NADH-cytochrome b5 reductase gene of a Chinese patient with recessive congenital methemoglobinemia."
      Wang Y., Wu Y.-S., Zheng P.-Z., Yang W.-X., Fang G.-A., Tang Y.-C., Xie F., Lan F.-H., Zhu Z.-Y.
      Blood 95:3250-3255(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT METHB-CYB5R3 TYR-204.
    31. "Arginine-glutamine replacement at residue 57 of NADH-cytochrome b5 reductase in Chinese hereditary methemoglobinemia."
      Huang C.-H., Xie Y., Wang Y., Wu Y.-S.
      Zhonghua Xue Ye Xue Za Zhi 18:200-203(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT METHB-CYB5R3 GLN-58.
    32. "Familial idiopathic methemoglobinemia revisited: original cases reveal 2 novel mutations in NADH-cytochrome b5 reductase."
      Percy M.J., Gillespie M.J.S., Savage G., Hughes A.E., McMullin M.F., Lappin T.R.J.
      Blood 100:3447-3449(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS METHB-CYB5R3 GLU-256 DEL AND ASP-292.
    33. "Recessive congenital methaemoglobinaemia: functional characterization of the novel D239G mutation in the NADH-binding lobe of cytochrome b5 reductase."
      Percy M.J., Crowley L.J., Davis C.A., McMullin M.F., Savage G., Hughes J., McMahon C., Quinn R.J.M., Smith O., Barber M.J., Lappin T.R.J.
      Br. J. Haematol. 129:847-853(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS METHB-CYB5R3 GLU-256 DEL AND ASP-292.

    Entry informationi

    Entry nameiNB5R3_HUMAN
    AccessioniPrimary (citable) accession number: P00387
    Secondary accession number(s): B1AHF2
    , B7Z7L3, O75675, Q8TDL8, Q8WTS8, Q9UEN4, Q9UEN5, Q9UL55, Q9UL56
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 196 of the entry and version 3 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3