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Protein

Carbonyl reductase [NADPH] 3

Gene

CBR3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

    • 3-keto sterol reductase activity Source: Ensembl
    • carbonyl reductase (NADPH) activity Source: UniProtKB
    • NADPH binding Source: UniProtKB

    GO - Biological processi

    • cognition Source: UniProtKB
    • phylloquinone catabolic process Source: Ensembl
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BRENDAi1.1.1.184. 2681.
    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
    Short chain dehydrogenase/reductase family 21C member 2
    Gene namesi
    Name:CBR3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:1549. CBR3.

    Subcellular locationi

    • Cytoplasm 1 Publication

    GO - Cellular componenti

    • cytoplasm Source: HPA
    • cytosol Source: UniProtKB
    • extracellular space Source: UniProtKB
    • nucleoplasm Source: HPA
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26122.

    Chemistry

    DrugBankiDB00997. Doxorubicin.

    Polymorphism and mutation databases

    BioMutaiCBR3.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 277276Carbonyl reductase [NADPH] 3PRO_0000054608Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    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.
    ExpressionAtlasiO75828. baseline and differential.
    GenevisibleiO75828. HS.

    Organism-specific databases

    HPAiHPA018434.

    Interactioni

    Protein-protein interaction databases

    BioGridi107320. 9 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 – 126Combined sources
    Helixi16 – 2813Combined sources
    Beta strandi30 – 3910Combined sources
    Helixi40 – 5213Combined sources
    Beta strandi58 – 614Combined sources
    Helixi67 – 8115Combined sources
    Beta strandi82 – 898Combined sources
    Helixi103 – 11412Combined sources
    Helixi116 – 12510Combined sources
    Helixi126 – 1283Combined sources
    Beta strandi129 – 13810Combined sources
    Helixi142 – 1498Combined sources
    Helixi152 – 1598Combined sources
    Helixi165 – 18016Combined sources
    Turni184 – 1885Combined sources
    Helixi193 – 21523Combined sources
    Helixi217 – 2193Combined sources
    Beta strandi222 – 2276Combined sources
    Beta strandi237 – 2393Combined sources
    Helixi241 – 2477Combined sources
    Helixi249 – 2557Combined sources
    Beta strandi268 – 2703Combined sources
    Beta strandi273 – 2753Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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.
    OMAiESICLES.
    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.

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

    O75828-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSSCSRVALV TGANRGIGLA IARELCRQFS GDVVLTARDV ARGQAAVQQL
    60 70 80 90 100
    QAEGLSPRFH QLDIDDLQSI RALRDFLRKE YGGLNVLVNN AAVAFKSDDP
    110 120 130 140 150
    MPFDIKAEMT LKTNFFATRN MCNELLPIMK PHGRVVNISS LQCLRAFENC
    160 170 180 190 200
    SEDLQERFHS ETLTEGDLVD LMKKFVEDTK NEVHEREGWP NSPYGVSKLG
    210 220 230 240 250
    VTVLSRILAR RLDEKRKADR ILVNACCPGP VKTDMDGKDS IRTVEEGAET
    260 270
    PVYLALLPPD ATEPQGQLVH DKVVQNW
    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. 2 Publications
    Corresponds to variant rs1056892 [ dbSNP | Ensembl ].
    VAR_033873

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi107320. 9 interactions.
    IntActiO75828. 5 interactions.
    MINTiMINT-1412792.
    STRINGi9606.ENSP00000290354.

    Chemistry

    ChEMBLiCHEMBL6008.
    DrugBankiDB00997. Doxorubicin.

    PTM databases

    PhosphoSiteiO75828.

    Polymorphism and mutation databases

    BioMutaiCBR3.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00290462.

    Proteomic databases

    PaxDbiO75828.
    PeptideAtlasiO75828.
    PRIDEiO75828.

    Protocols and materials databases

    DNASUi874.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi874.
    GeneCardsiGC21P037507.
    HGNCiHGNC:1549. CBR3.
    HPAiHPA018434.
    MIMi603608. gene.
    neXtProtiNX_O75828.
    PharmGKBiPA26122.
    GenAtlasiSearch...

    Phylogenomic databases

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

    Enzyme and pathway databases

    BRENDAi1.1.1.184. 2681.
    SABIO-RKO75828.

    Miscellaneous databases

    EvolutionaryTraceiO75828.
    GeneWikiiCBR3.
    GenomeRNAii874.
    NextBioi3638.
    PROiO75828.
    SOURCEiSearch...

    Gene expression databases

    BgeeiO75828.
    CleanExiHS_CBR3.
    ExpressionAtlasiO75828. baseline and differential.
    GenevisibleiO75828. HS.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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: June 24, 2015
    This is version 139 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

    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.