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O75828

- CBR3_HUMAN

UniProt

O75828 - CBR3_HUMAN

Protein

Carbonyl reductase [NADPH] 3

Gene

CBR3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Has low NADPH-dependent oxidoreductase activity towards 4-benzoylpyridine and menadione (in vitro).1 Publication

    Catalytic activityi

    R-CHOH-R' + NADP+ = R-CO-R' + NADPH.

    Kineticsi

    1. KM=25 µM for menadione2 Publications
    2. KM=43 µM for menadione2 Publications
    3. KM=90 µM for NADPH2 Publications
    4. KM=38 µM for NADPH2 Publications

    pH dependencei

    Optimum pH is 5.5-7.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei90 – 901NADP; via carbonyl oxygen1 Publication
    Binding sitei140 – 1401SubstrateBy similarity
    Active sitei194 – 1941Proton acceptorPROSITE-ProRule annotation
    Binding sitei239 – 2391NADP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 3425NADP1 PublicationAdd
    BLAST
    Nucleotide bindingi38 – 425NADP1 Publication
    Nucleotide bindingi63 – 642NADP1 Publication
    Nucleotide bindingi194 – 1985NADP1 Publication

    GO - Molecular functioni

    1. 3-keto sterol reductase activity Source: Ensembl
    2. carbonyl reductase (NADPH) activity Source: UniProtKB
    3. NADPH binding Source: UniProtKB

    GO - Biological processi

    1. cognition Source: UniProt
    2. phylloquinone catabolic process Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    SABIO-RKO75828.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbonyl reductase [NADPH] 3 (EC:1.1.1.184)
    Alternative name(s):
    NADPH-dependent carbonyl reductase 3
    Gene namesi
    Name:CBR3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:1549. CBR3.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: UniProtKB
    3. extracellular space Source: UniProt
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26122.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 277277Carbonyl reductase [NADPH] 3PRO_0000054608Add
    BLAST

    Proteomic databases

    MaxQBiO75828.
    PaxDbiO75828.
    PeptideAtlasiO75828.
    PRIDEiO75828.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00290462.

    PTM databases

    PhosphoSiteiO75828.

    Expressioni

    Tissue specificityi

    Detected in ovary, pancreas, intestine, colon, kidney, brain, thymus, lung, heart, liver, spleen, leukocyte, prostate and testis.1 Publication

    Gene expression databases

    BgeeiO75828.
    CleanExiHS_CBR3.
    GenevestigatoriO75828.

    Organism-specific databases

    HPAiHPA018434.

    Interactioni

    Protein-protein interaction databases

    BioGridi107320. 5 interactions.
    IntActiO75828. 5 interactions.
    MINTiMINT-1412792.
    STRINGi9606.ENSP00000290354.

    Structurei

    Secondary structure

    1
    277
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 126
    Helixi16 – 2813
    Beta strandi30 – 3910
    Helixi40 – 5213
    Beta strandi58 – 614
    Helixi67 – 8115
    Beta strandi82 – 898
    Helixi103 – 11412
    Helixi116 – 12510
    Helixi126 – 1283
    Beta strandi129 – 13810
    Helixi142 – 1498
    Helixi152 – 1598
    Helixi165 – 18016
    Turni184 – 1885
    Helixi193 – 21523
    Helixi217 – 2193
    Beta strandi222 – 2276
    Beta strandi237 – 2393
    Helixi241 – 2477
    Helixi249 – 2557
    Beta strandi268 – 2703
    Beta strandi273 – 2753

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HRBX-ray1.90A6-277[»]
    ProteinModelPortaliO75828.
    SMRiO75828. Positions 5-277.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75828.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1028.
    HOVERGENiHBG001909.
    InParanoidiO75828.
    KOiK00084.
    OMAiHGQLVHD.
    OrthoDBiEOG7PGDR4.
    PhylomeDBiO75828.
    TreeFamiTF329359.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002198. DH_sc/Rdtase_SDR.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view]
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.
    PR00080. SDRFAMILY.
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O75828-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSCSRVALV TGANRGIGLA IARELCRQFS GDVVLTARDV ARGQAAVQQL    50
    QAEGLSPRFH QLDIDDLQSI RALRDFLRKE YGGLNVLVNN AAVAFKSDDP 100
    MPFDIKAEMT LKTNFFATRN MCNELLPIMK PHGRVVNISS LQCLRAFENC 150
    SEDLQERFHS ETLTEGDLVD LMKKFVEDTK NEVHEREGWP NSPYGVSKLG 200
    VTVLSRILAR RLDEKRKADR ILVNACCPGP VKTDMDGKDS IRTVEEGAET 250
    PVYLALLPPD ATEPQGQLVH DKVVQNW 277
    Length:277
    Mass (Da):30,850
    Last modified:January 23, 2007 - v3
    Checksum:i8D39D6B99CFE5389
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti4 – 41C → Y.1 Publication
    Corresponds to variant rs8133052 [ dbSNP | Ensembl ].
    VAR_033868
    Natural varianti84 – 841L → V.1 Publication
    Corresponds to variant rs9282628 [ dbSNP | Ensembl ].
    VAR_033869
    Natural varianti93 – 931V → I.
    Corresponds to variant rs2835285 [ dbSNP | Ensembl ].
    VAR_033870
    Natural varianti131 – 1311P → S.1 Publication
    Corresponds to variant rs16993929 [ dbSNP | Ensembl ].
    VAR_033871
    Natural varianti235 – 2351M → L.1 Publication
    Corresponds to variant rs4987121 [ dbSNP | Ensembl ].
    VAR_033872
    Natural varianti244 – 2441V → M Increased catalytic activity. 1 Publication
    Corresponds to variant rs1056892 [ dbSNP | Ensembl ].
    VAR_033873

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB004854 mRNA. Translation: BAA33500.1.
    AB003151 Genomic DNA. Translation: BAA34207.1.
    AB041012 mRNA. Translation: BAD74062.1.
    AB124847 mRNA. Translation: BAE45939.1.
    CR541709 mRNA. Translation: CAG46510.1.
    EF462915 Genomic DNA. Translation: ABO43035.1.
    AP000689 Genomic DNA. Translation: BAA89425.1.
    AP001725 Genomic DNA. Translation: BAA95547.1.
    CH471079 Genomic DNA. Translation: EAX09747.1.
    BC002812 mRNA. Translation: AAH02812.1.
    CCDSiCCDS13642.1.
    RefSeqiNP_001227.1. NM_001236.3.
    UniGeneiHs.154510.

    Genome annotation databases

    EnsembliENST00000290354; ENSP00000290354; ENSG00000159231.
    GeneIDi874.
    KEGGihsa:874.
    UCSCiuc002yve.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB004854 mRNA. Translation: BAA33500.1 .
    AB003151 Genomic DNA. Translation: BAA34207.1 .
    AB041012 mRNA. Translation: BAD74062.1 .
    AB124847 mRNA. Translation: BAE45939.1 .
    CR541709 mRNA. Translation: CAG46510.1 .
    EF462915 Genomic DNA. Translation: ABO43035.1 .
    AP000689 Genomic DNA. Translation: BAA89425.1 .
    AP001725 Genomic DNA. Translation: BAA95547.1 .
    CH471079 Genomic DNA. Translation: EAX09747.1 .
    BC002812 mRNA. Translation: AAH02812.1 .
    CCDSi CCDS13642.1.
    RefSeqi NP_001227.1. NM_001236.3.
    UniGenei Hs.154510.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HRB X-ray 1.90 A 6-277 [» ]
    ProteinModelPortali O75828.
    SMRi O75828. Positions 5-277.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107320. 5 interactions.
    IntActi O75828. 5 interactions.
    MINTi MINT-1412792.
    STRINGi 9606.ENSP00000290354.

    Chemistry

    ChEMBLi CHEMBL6008.

    PTM databases

    PhosphoSitei O75828.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00290462.

    Proteomic databases

    MaxQBi O75828.
    PaxDbi O75828.
    PeptideAtlasi O75828.
    PRIDEi O75828.

    Protocols and materials databases

    DNASUi 874.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000290354 ; ENSP00000290354 ; ENSG00000159231 .
    GeneIDi 874.
    KEGGi hsa:874.
    UCSCi uc002yve.3. human.

    Organism-specific databases

    CTDi 874.
    GeneCardsi GC21P037507.
    HGNCi HGNC:1549. CBR3.
    HPAi HPA018434.
    MIMi 603608. gene.
    neXtProti NX_O75828.
    PharmGKBi PA26122.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1028.
    HOVERGENi HBG001909.
    InParanoidi O75828.
    KOi K00084.
    OMAi HGQLVHD.
    OrthoDBi EOG7PGDR4.
    PhylomeDBi O75828.
    TreeFami TF329359.

    Enzyme and pathway databases

    SABIO-RK O75828.

    Miscellaneous databases

    EvolutionaryTracei O75828.
    GeneWikii CBR3.
    GenomeRNAii 874.
    NextBioi 3638.
    PROi O75828.
    SOURCEi Search...

    Gene expression databases

    Bgeei O75828.
    CleanExi HS_CBR3.
    Genevestigatori O75828.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR002198. DH_sc/Rdtase_SDR.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view ]
    Pfami PF00106. adh_short. 1 hit.
    [Graphical view ]
    PRINTSi PR00081. GDHRDH.
    PR00080. SDRFAMILY.
    PROSITEi PS00061. ADH_SHORT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mapping of a novel human carbonyl reductase, CBR3, and ribosomal pseudogenes to human chromosome 21q22.2."
      Watanabe K., Sugawara C., Ono A., Fukuzumi Y., Itakura S., Yamazaki M., Tashiro H., Osoegawa K., Soeda E., Nomura T.
      Genomics 52:95-100(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. "Homo sapiens mRNA for NADPH-dependent carbonyl reductase 3, complete cds."
      Shimizu N., Kudoh J., Shibuya K.
      Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetal kidney.
    3. "Human fetal brain carbonyl reductases."
      Terada T., Mizobuchi H.
      Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetal brain.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. SeattleSNPs variation discovery resource
      Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TYR-4; VAL-84; SER-131; LEU-235 AND MET-244.
    6. "The DNA sequence of human chromosome 21."
      Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
      , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
      Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Placenta.
    9. "Different functions between human monomeric carbonyl reductase 3 and carbonyl reductase 1."
      Miura T., Nishinaka T., Terada T.
      Mol. Cell. Biochem. 315:113-121(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Crystal structure of human carbonyl reductase 3, complexed with NADP+."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 6-276 IN COMPLEX WITH NADP.
    12. "Functional significance of a natural allelic variant of human carbonyl reductase 3 (CBR3)."
      Lakhman S.S., Ghosh D., Blanco J.G.
      Drug Metab. Dispos. 33:254-257(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT MET-244, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiCBR3_HUMAN
    AccessioniPrimary (citable) accession number: O75828
    Secondary accession number(s): Q6FHP2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 130 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, Reference proteome

    Documents

    1. Human chromosome 21
      Human chromosome 21: 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