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Q3TDX8

- NB5R4_MOUSE

UniProt

Q3TDX8 - NB5R4_MOUSE

Protein

Cytochrome b5 reductase 4

Gene

Cyb5r4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 3 (28 Jun 2011)
      Previous versions | rss
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    Functioni

    NADH-cytochrome b5 reductase involved in endoplasmic reticulum stress response pathway. Plays a critical role in protecting pancreatic beta-cells against oxidant stress, possibly by protecting the cell from excess buildup of reactive oxygen species (ROS).1 Publication

    Catalytic activityi

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

    Cofactori

    FAD.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi89 – 891Iron (heme axial ligand)PROSITE-ProRule annotation
    Metal bindingi112 – 1121Iron (heme axial ligand)PROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi372 – 38716FADBy similarityAdd
    BLAST
    Nucleotide bindingi399 – 43133FADBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. cytochrome-b5 reductase activity, acting on NAD(P)H Source: MGI
    2. flavin adenine dinucleotide binding Source: Ensembl
    3. heme binding Source: MGI
    4. metal ion binding Source: UniProtKB-KW
    5. NAD(P)H oxidase activity Source: Ensembl
    6. NADPH-hemoprotein reductase activity Source: Ensembl
    7. protein binding Source: MGI

    GO - Biological processi

    1. cell development Source: MGI
    2. generation of precursor metabolites and energy Source: Ensembl
    3. glucose homeostasis Source: MGI
    4. heme metabolic process Source: MGI
    5. insulin secretion Source: MGI
    6. NADP metabolic process Source: Ensembl
    7. response to antibiotic Source: MGI
    8. superoxide metabolic process Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, Heme, Iron, Metal-binding, NAD

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytochrome b5 reductase 4 (EC:1.6.2.2)
    Alternative name(s):
    Flavohemoprotein b5/b5R
    Short name:
    b5+b5R
    N-terminal cytochrome b5 and cytochrome b5 oxidoreductase domain-containing protein
    cb5/cb5R
    Gene namesi
    Name:Cyb5r4
    Synonyms:Ncb5or
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:2386848. Cyb5r4.

    Subcellular locationi

    Endoplasmic reticulum
    Note: Soluble protein.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. endoplasmic reticulum Source: MGI
    3. perinuclear region of cytoplasm Source: Ensembl

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Disruption phenotypei

    Mice display insulin-deficient diabetes. Embryos and fetus develop normally. At 4 weeks of age, mice show have normal blood glucose levels but impaired glucose tolerance. Isolated islets have markedly impaired glucose- or arginine-stimulated insulin secretion. By 7 weeks of age, they develop severe hyperglycemia with markedly decreased serum insulin levels and nearly normal insulin tolerance. As the animals age, there is a progressive loss of beta cells in pancreatic islets, but there is no loss of alpha, delta, or PP cells. 4 week-old mice have enhanced sensitivity to the diabetogenic agent streptozotocin.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 528528Cytochrome b5 reductase 4PRO_0000410469Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiQ3TDX8.

    PTM databases

    PhosphoSiteiQ3TDX8.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Isoform 2 is expressed in testis, brain, skeletal muscle and in the male germline.2 Publications

    Gene expression databases

    BgeeiQ3TDX8.
    CleanExiMM_CYB5R4.
    GenevestigatoriQ3TDX8.

    Interactioni

    Protein-protein interaction databases

    IntActiQ3TDX8. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3TDX8.
    SMRiQ3TDX8. Positions 51-137, 282-502.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini54 – 13077Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini172 – 26392CSPROSITE-ProRule annotationAdd
    BLAST
    Domaini280 – 392113FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CS domain.PROSITE-ProRule annotation
    Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation
    Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0543.
    GeneTreeiENSGT00390000008881.
    HOVERGENiHBG108174.
    InParanoidiQ3TDX8.
    OMAiKDYHEEK.
    OrthoDBiEOG718KBZ.
    TreeFamiTF313874.

    Family and domain databases

    Gene3Di2.60.40.790. 1 hit.
    3.10.120.10. 1 hit.
    InterProiIPR007052. CS_dom.
    IPR001199. Cyt_B5-like_heme/steroid-bd.
    IPR018506. Cyt_B5_heme-BS.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR008978. HSP20-like_chaperone.
    IPR001834. NADH-Cyt_B5_reductase.
    IPR008333. OxRdtase_FAD-bd_dom.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view]
    PfamiPF04969. CS. 1 hit.
    PF00173. Cyt-b5. 1 hit.
    PF00970. FAD_binding_6. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    [Graphical view]
    PRINTSiPR00406. CYTB5RDTASE.
    PR00363. CYTOCHROMEB5.
    SUPFAMiSSF49764. SSF49764. 1 hit.
    SSF55856. SSF55856. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEiPS51203. CS. 1 hit.
    PS00191. CYTOCHROME_B5_1. 1 hit.
    PS50255. CYTOCHROME_B5_2. 1 hit.
    PS51384. FAD_FR. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q3TDX8-4) [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

    MLNVPSQAFP APGSQQRVSS QGRSKVPLKQ GRSLMDWIRL TKSGKDLTGL    50
    KGGLIEVTEE ELKKHNKKED CWICIRGFVY NVSPYMEYHP GGEDELMRAA 100
    GADGTDLFNE VHRWVNYESM LKECLVGRMA VKPAVPKDCH EGKRVLNGML 150
    PKSQMSDTLP RDVTDTLPRE DLSSPSYDWF QTESSVTIVV YTKQKNISLD 200
    SVIVDLQDDS LRAEAVIKDH SYLVHVGLSH EVQENFSVRV IENVGKIEIV 250
    LQKKESVSWQ CLGDHLEKHD SFIPKKDTGL YYRRCQLISK EDVTHDTRLF 300
    CLMLPPSTHL QVPVGQHVYL KLSVTGAEIV KPYTPVSDSL LSDFKEPVLS 350
    PNKYICFLIK IYPAGLFTPE LDRLQIGDFI SVSGPEGDFK VSKLQEVEDL 400
    FLLAAGTGFT PMVTVLNYAL SHMSSLRKVK LMFFNKTEDD IIWRCQLEKL 450
    ALREKRFDVE FVLSAPSPEW NGKQGHISRA LLSEFLQRSS ENSRAFLCIC 500
    GPTPFTDEGI RLLHDLNFSD DEIHGFTA 528
    Length:528
    Mass (Da):59,716
    Last modified:June 28, 2011 - v3
    Checksum:i8CF34CE865980A66
    GO
    Isoform 2 (identifier: Q3TDX8-5) [UniParc]FASTAAdd to Basket

    Also known as: cb5/cb5rDelta12

    The sequence of this isoform differs from the canonical sequence as follows:
         326-376: Missing.

    Show »
    Length:477
    Mass (Da):53,994
    Checksum:i4F809037109F6B5D
    GO

    Sequence cautioni

    The sequence AAH25438.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAC41118.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAE34044.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAE42908.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti171 – 1711D → G in BAE34044. (PubMed:16141072)Curated
    Sequence conflicti171 – 1711D → G in BAE41470. (PubMed:16141072)Curated
    Sequence conflicti171 – 1711D → G in BAE42908. (PubMed:16141072)Curated
    Sequence conflicti171 – 1711D → G in AAK08116. (PubMed:10611283)Curated
    Sequence conflicti171 – 1711D → G in AAQ83900. (PubMed:14962668)Curated
    Sequence conflicti171 – 1711D → G in AAQ83901. (PubMed:14962668)Curated
    Sequence conflicti216 – 2161V → I in AAH25438. (PubMed:15489334)Curated
    Sequence conflicti300 – 3001F → L in BAE34044. (PubMed:16141072)Curated
    Sequence conflicti300 – 3001F → L in BAE41470. (PubMed:16141072)Curated
    Sequence conflicti300 – 3001F → L in BAE42908. (PubMed:16141072)Curated
    Sequence conflicti300 – 3001F → L in AAH02170. (PubMed:15489334)Curated
    Sequence conflicti300 – 3001F → L in AAK08116. (PubMed:10611283)Curated
    Sequence conflicti300 – 3001F → L in AAQ83900. (PubMed:14962668)Curated
    Sequence conflicti300 – 3001F → L in AAQ83901. (PubMed:14962668)Curated
    Sequence conflicti336 – 3361V → L in BAE34044. (PubMed:16141072)Curated
    Sequence conflicti339 – 3391S → P in BAE41470. (PubMed:16141072)Curated
    Sequence conflicti356 – 3561C → Y in BAE34044. (PubMed:16141072)Curated
    Sequence conflicti356 – 3561C → Y in BAE41470. (PubMed:16141072)Curated
    Sequence conflicti356 – 3561C → Y in BAE42908. (PubMed:16141072)Curated
    Sequence conflicti356 – 3561C → Y in AAH02170. (PubMed:15489334)Curated
    Sequence conflicti356 – 3561C → Y in AAH25438. (PubMed:15489334)Curated
    Sequence conflicti356 – 3561C → Y in AAK08116. (PubMed:10611283)Curated
    Sequence conflicti356 – 3561C → Y in AAQ83900. (PubMed:14962668)Curated
    Sequence conflicti388 – 3881D → N in BAE34044. (PubMed:16141072)Curated
    Sequence conflicti388 – 3881D → N in BAE41470. (PubMed:16141072)Curated
    Sequence conflicti388 – 3881D → N in BAE42908. (PubMed:16141072)Curated
    Sequence conflicti388 – 3881D → N in AAH02170. (PubMed:15489334)Curated
    Sequence conflicti388 – 3881D → N in AAH25438. (PubMed:15489334)Curated
    Sequence conflicti388 – 3881D → N in AAK08116. (PubMed:10611283)Curated
    Sequence conflicti388 – 3881D → N in AAQ83900. (PubMed:14962668)Curated
    Sequence conflicti388 – 3881D → N in AAQ83901. (PubMed:14962668)Curated
    Sequence conflicti393 – 3931K → T in AAH25438. (PubMed:15489334)Curated
    Sequence conflicti438 – 4381E → D in BAC37357. (PubMed:16141072)Curated
    Sequence conflicti504 – 5041P → Q in BAE39522. (PubMed:16141072)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti156 – 1561S → SDTLPRDVT.4 Publications

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei326 – 37651Missing in isoform 2. 1 PublicationVSP_041453Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK078682 mRNA. Translation: BAC37357.1.
    AK090159 mRNA. Translation: BAC41118.1. Different initiation.
    AK157312 mRNA. Translation: BAE34044.1. Different initiation.
    AK167436 mRNA. Translation: BAE39522.1.
    AK169937 mRNA. Translation: BAE41470.1.
    AK172252 mRNA. Translation: BAE42908.1. Different initiation.
    AC156793 Genomic DNA. No translation available.
    BC025438 mRNA. Translation: AAH25438.1. Different initiation.
    BC002170 mRNA. Translation: AAH02170.1.
    AF338818 mRNA. Translation: AAK08116.1.
    AY321368 mRNA. Translation: AAQ83900.1.
    AY321369 mRNA. Translation: AAQ83901.1.
    CCDSiCCDS40716.2. [Q3TDX8-4]
    RefSeqiNP_077157.2. NM_024195.2. [Q3TDX8-4]
    XP_006511262.1. XM_006511199.1. [Q3TDX8-5]
    UniGeneiMm.30166.

    Genome annotation databases

    EnsembliENSMUST00000168529; ENSMUSP00000126119; ENSMUSG00000032872. [Q3TDX8-4]
    ENSMUST00000173126; ENSMUSP00000134460; ENSMUSG00000032872. [Q3TDX8-5]
    GeneIDi266690.
    KEGGimmu:266690.
    UCSCiuc009qyc.2. mouse. [Q3TDX8-4]
    uc009qyf.2. mouse. [Q3TDX8-5]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK078682 mRNA. Translation: BAC37357.1 .
    AK090159 mRNA. Translation: BAC41118.1 . Different initiation.
    AK157312 mRNA. Translation: BAE34044.1 . Different initiation.
    AK167436 mRNA. Translation: BAE39522.1 .
    AK169937 mRNA. Translation: BAE41470.1 .
    AK172252 mRNA. Translation: BAE42908.1 . Different initiation.
    AC156793 Genomic DNA. No translation available.
    BC025438 mRNA. Translation: AAH25438.1 . Different initiation.
    BC002170 mRNA. Translation: AAH02170.1 .
    AF338818 mRNA. Translation: AAK08116.1 .
    AY321368 mRNA. Translation: AAQ83900.1 .
    AY321369 mRNA. Translation: AAQ83901.1 .
    CCDSi CCDS40716.2. [Q3TDX8-4 ]
    RefSeqi NP_077157.2. NM_024195.2. [Q3TDX8-4 ]
    XP_006511262.1. XM_006511199.1. [Q3TDX8-5 ]
    UniGenei Mm.30166.

    3D structure databases

    ProteinModelPortali Q3TDX8.
    SMRi Q3TDX8. Positions 51-137, 282-502.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q3TDX8. 1 interaction.

    PTM databases

    PhosphoSitei Q3TDX8.

    Proteomic databases

    PRIDEi Q3TDX8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000168529 ; ENSMUSP00000126119 ; ENSMUSG00000032872 . [Q3TDX8-4 ]
    ENSMUST00000173126 ; ENSMUSP00000134460 ; ENSMUSG00000032872 . [Q3TDX8-5 ]
    GeneIDi 266690.
    KEGGi mmu:266690.
    UCSCi uc009qyc.2. mouse. [Q3TDX8-4 ]
    uc009qyf.2. mouse. [Q3TDX8-5 ]

    Organism-specific databases

    CTDi 51167.
    MGIi MGI:2386848. Cyb5r4.

    Phylogenomic databases

    eggNOGi COG0543.
    GeneTreei ENSGT00390000008881.
    HOVERGENi HBG108174.
    InParanoidi Q3TDX8.
    OMAi KDYHEEK.
    OrthoDBi EOG718KBZ.
    TreeFami TF313874.

    Miscellaneous databases

    ChiTaRSi CYB5R4. mouse.
    NextBioi 392180.
    PROi Q3TDX8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q3TDX8.
    CleanExi MM_CYB5R4.
    Genevestigatori Q3TDX8.

    Family and domain databases

    Gene3Di 2.60.40.790. 1 hit.
    3.10.120.10. 1 hit.
    InterProi IPR007052. CS_dom.
    IPR001199. Cyt_B5-like_heme/steroid-bd.
    IPR018506. Cyt_B5_heme-BS.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR008978. HSP20-like_chaperone.
    IPR001834. NADH-Cyt_B5_reductase.
    IPR008333. OxRdtase_FAD-bd_dom.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view ]
    Pfami PF04969. CS. 1 hit.
    PF00173. Cyt-b5. 1 hit.
    PF00970. FAD_binding_6. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00406. CYTB5RDTASE.
    PR00363. CYTOCHROMEB5.
    SUPFAMi SSF49764. SSF49764. 1 hit.
    SSF55856. SSF55856. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEi PS51203. CS. 1 hit.
    PS00191. CYTOCHROME_B5_1. 1 hit.
    PS50255. CYTOCHROME_B5_2. 1 hit.
    PS51384. FAD_FR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASP-THR-LEU-PRO-ARG-ASP-VAL-THR-156 INS.
      Strain: C57BL/6J and NOD.
      Tissue: Eye, Liver, Spinal cord and Spleen.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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 1), VARIANT ASP-THR-LEU-PRO-ARG-ASP-VAL-THR-156 INS.
      Strain: Czech II and FVB/N.
      Tissue: Mammary tumor.
    4. "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] OF 35-528 (ISOFORM 1), VARIANT ASP-THR-LEU-PRO-ARG-ASP-VAL-THR-156 INS.
    5. "Identification and characterization of a novel splice variant of mouse and rat cytochrome b5/cytochrome b5 reductase."
      Curry B.J., Roman S.D., Wallace C.A., Scott R., Miriami E., Aitken R.J.
      Genomics 83:425-438(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-528 (ISOFORMS 1 AND 2), VARIANT ASP-THR-LEU-PRO-ARG-ASP-VAL-THR-156 INS, TISSUE SPECIFICITY.
      Strain: Swiss.
      Tissue: Testis.
    6. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    7. "Promoter characterization and transcriptional regulation of Ncb5or, a novel reductase necessary for pancreatic beta-cell maintenance."
      Larade K., Bunn H.F.
      Biochim. Biophys. Acta 1759:257-262(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiNB5R4_MOUSE
    AccessioniPrimary (citable) accession number: Q3TDX8
    Secondary accession number(s): E9Q129
    , Q3TJH3, Q3U012, Q6VXY4, Q6VXY5, Q8BJV8, Q8BTI5, Q8R3H8, Q99LY4, Q99P29
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 15, 2007
    Last sequence update: June 28, 2011
    Last modified: October 1, 2014
    This is version 91 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3