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Protein

Carbonyl reductase [NADPH] 1

Gene

CBR1

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

Functioni

NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E2 to prostaglandin F2-alpha. Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione.4 Publications

Catalytic activityi

R-CHOH-R' + NADP+ = R-CO-R' + NADPH.
(5Z,13E)-(15S)-9-alpha,11-alpha,15-trihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate + NADPH.
(13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprost-13-enoate + NADP+ = (13E)-11-alpha-hydroxy-9,15-dioxoprost-13-enoate + NADPH.

Enzyme regulationi

Inhibited by quercetin, rutenin and its derivatives.2 Publications

Kineticsi

  1. KM=30 µM for S-nitrosoglutathione2 Publications
  2. KM=22 µM for menadione2 Publications
  3. KM=309 µM for prostaglandin E22 Publications
  4. KM=173 µM for daunorubicin2 Publications
  5. KM=247 µM for NADPH2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei90 – 901NADP; via carbonyl oxygen3 Publications
    Binding sitei106 – 1061Glutathione
    Binding sitei140 – 1401Substrate
    Active sitei194 – 1941Proton acceptor

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 3425NADP3 PublicationsAdd
    BLAST
    Nucleotide bindingi63 – 642NADP3 Publications
    Nucleotide bindingi194 – 1985NADP3 Publications
    Nucleotide bindingi231 – 2333NADP3 Publications

    GO - Molecular functioni

    GO - Biological processi

    • cyclooxygenase pathway Source: Reactome
    • drug metabolic process Source: UniProtKB
    • epithelial cell differentiation Source: UniProtKB
    • oxidation-reduction process Source: UniProtKB
    • vitamin K metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BRENDAi1.1.1.184. 2681.
    ReactomeiR-HSA-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
    SABIO-RKP16152.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbonyl reductase [NADPH] 1 (EC:1.1.1.184)
    Alternative name(s):
    15-hydroxyprostaglandin dehydrogenase [NADP(+)] (EC:1.1.1.197)
    NADPH-dependent carbonyl reductase 1
    Prostaglandin 9-ketoreductase
    Prostaglandin-E(2) 9-reductase (EC:1.1.1.189)
    Short chain dehydrogenase/reductase family 21C member 1
    Gene namesi
    Name:CBR1
    Synonyms:CBR, CRN, SDR21C1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:1548. CBR1.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: Reactome
    • extracellular exosome Source: UniProtKB
    • extracellular vesicle Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26121.

    Chemistry

    ChEMBLiCHEMBL5586.
    DrugBankiDB00997. Doxorubicin.
    DB00502. Haloperidol.
    DB01046. Lubiprostone.
    DB04844. Tetrabenazine.
    GuidetoPHARMACOLOGYi1383.

    Polymorphism and mutation databases

    BioMutaiCBR1.
    DMDMi118519.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemovedCombined sources
    Chaini2 – 277276Carbonyl reductase [NADPH] 1PRO_0000054602Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineCombined sources
    Modified residuei2 – 21PhosphoserineBy similarity
    Modified residuei30 – 301PhosphoserineBy similarity
    Modified residuei162 – 1621PhosphothreonineBy similarity
    Modified residuei239 – 2391N6-1-carboxyethyl lysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    EPDiP16152.
    MaxQBiP16152.
    PaxDbiP16152.
    PeptideAtlasiP16152.
    PRIDEiP16152.
    TopDownProteomicsiP16152-1. [P16152-1]

    2D gel databases

    REPRODUCTION-2DPAGEIPI00295386.
    UCD-2DPAGEP16152.

    PTM databases

    iPTMnetiP16152.
    PhosphoSiteiP16152.
    SwissPalmiP16152.

    Expressioni

    Gene expression databases

    BgeeiP16152.
    CleanExiHS_CBR1.
    ExpressionAtlasiP16152. baseline and differential.
    GenevisibleiP16152. HS.

    Organism-specific databases

    HPAiHPA018433.

    Interactioni

    Subunit structurei

    Monomer.3 Publications

    Protein-protein interaction databases

    BioGridi107319. 37 interactions.
    DIPiDIP-33136N.
    IntActiP16152. 26 interactions.
    MINTiMINT-1418935.
    STRINGi9606.ENSP00000290349.

    Chemistry

    BindingDBiP16152.

    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 strandi29 – 3911Combined 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
    Helixi141 – 1488Combined sources
    Helixi152 – 1598Combined sources
    Helixi165 – 18016Combined sources
    Turni184 – 1885Combined sources
    Helixi193 – 21523Combined sources
    Beta strandi222 – 2276Combined sources
    Turni234 – 2363Combined sources
    Helixi244 – 2474Combined 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
    1WMAX-ray1.24A2-277[»]
    2PFGX-ray1.54A2-277[»]
    3BHIX-ray2.27A2-277[»]
    3BHJX-ray1.77A2-277[»]
    3BHMX-ray1.80A2-277[»]
    4Z3DX-ray1.80A/B/C/D2-277[»]
    ProteinModelPortaliP16152.
    SMRiP16152. Positions 3-277.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16152.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni95 – 973Glutathione binding
    Regioni193 – 1942Glutathione binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG1208. Eukaryota.
    COG1028. LUCA.
    GeneTreeiENSGT00510000046499.
    HOVERGENiHBG001909.
    InParanoidiP16152.
    KOiK00079.
    OMAiFRSEIIT.
    OrthoDBiEOG7PGDR4.
    PhylomeDBiP16152.
    TreeFamiTF329359.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    IPR002347. SDR_fam.
    [Graphical view]
    PANTHERiPTHR24322. PTHR24322. 2 hits.
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.
    PR00080. SDRFAMILY.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: P16152-1) [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

            10         20         30         40         50
    MSSGIHVALV TGGNKGIGLA IVRDLCRLFS GDVVLTARDV TRGQAAVQQL
    60 70 80 90 100
    QAEGLSPRFH QLDIDDLQSI RALRDFLRKE YGGLDVLVNN AGIAFKVADP
    110 120 130 140 150
    TPFHIQAEVT MKTNFFGTRD VCTELLPLIK PQGRVVNVSS IMSVRALKSC
    160 170 180 190 200
    SPELQQKFRS ETITEEELVG LMNKFVEDTK KGVHQKEGWP SSAYGVTKIG
    210 220 230 240 250
    VTVLSRIHAR KLSEQRKGDK ILLNACCPGW VRTDMAGPKA TKSPEEGAET
    260 270
    PVYLALLPPD AEGPHGQFVS EKRVEQW
    Length:277
    Mass (Da):30,375
    Last modified:January 23, 2007 - v3
    Checksum:i51A5A495EB4F4EC3
    GO
    Isoform 2 (identifier: P16152-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         133-173: GRVVNVSSIM...TEEELVGLMN → ASCVLSAWSC...ICRCLTLGPF
         174-277: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:173
    Mass (Da):18,762
    Checksum:i0D3547831C072133
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti88 – 881V → I Reduced affinity for NADPH and reduced activity towards daunorubicin and prostaglandin E2. 1 Publication
    Corresponds to variant rs1143663 [ dbSNP | Ensembl ].
    VAR_059053
    Natural varianti131 – 1311P → S.1 Publication
    Corresponds to variant rs41557318 [ dbSNP | Ensembl ].
    VAR_031706

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei133 – 17341GRVVN…VGLMN → ASCVLSAWSCLSQNPSGGKS KPLAWFTEMSIICRCLTLGP F in isoform 2. 1 PublicationVSP_054796Add
    BLAST
    Alternative sequencei174 – 277104Missing in isoform 2. 1 PublicationVSP_054797Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J04056 mRNA. Translation: AAA52070.1.
    M62420 Genomic DNA. Translation: AAA17881.1.
    AB003151 Genomic DNA. Translation: BAA33498.1.
    AP000688 Genomic DNA. Translation: BAA89424.1.
    AB124848 mRNA. Translation: BAE45940.1.
    BT019843 mRNA. Translation: AAV38646.1.
    CR541708 mRNA. Translation: CAG46509.1.
    AK294142 mRNA. Translation: BAG57468.1.
    AK314879 mRNA. Translation: BAG37394.1.
    EF141836 Genomic DNA. Translation: ABK97430.1.
    AP001724 Genomic DNA. Translation: BAA95508.1.
    CH471079 Genomic DNA. Translation: EAX09754.1.
    CH471079 Genomic DNA. Translation: EAX09755.1.
    BC002511 mRNA. Translation: AAH02511.1.
    BC015640 mRNA. Translation: AAH15640.1.
    CCDSiCCDS13641.1. [P16152-1]
    CCDS68202.1. [P16152-2]
    PIRiA61271. RDHUCB.
    RefSeqiNP_001273718.1. NM_001286789.1. [P16152-2]
    NP_001748.1. NM_001757.3. [P16152-1]
    UniGeneiHs.88778.

    Genome annotation databases

    EnsembliENST00000290349; ENSP00000290349; ENSG00000159228. [P16152-1]
    ENST00000530908; ENSP00000434613; ENSG00000159228. [P16152-2]
    GeneIDi873.
    KEGGihsa:873.
    UCSCiuc002yvb.3. human. [P16152-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J04056 mRNA. Translation: AAA52070.1.
    M62420 Genomic DNA. Translation: AAA17881.1.
    AB003151 Genomic DNA. Translation: BAA33498.1.
    AP000688 Genomic DNA. Translation: BAA89424.1.
    AB124848 mRNA. Translation: BAE45940.1.
    BT019843 mRNA. Translation: AAV38646.1.
    CR541708 mRNA. Translation: CAG46509.1.
    AK294142 mRNA. Translation: BAG57468.1.
    AK314879 mRNA. Translation: BAG37394.1.
    EF141836 Genomic DNA. Translation: ABK97430.1.
    AP001724 Genomic DNA. Translation: BAA95508.1.
    CH471079 Genomic DNA. Translation: EAX09754.1.
    CH471079 Genomic DNA. Translation: EAX09755.1.
    BC002511 mRNA. Translation: AAH02511.1.
    BC015640 mRNA. Translation: AAH15640.1.
    CCDSiCCDS13641.1. [P16152-1]
    CCDS68202.1. [P16152-2]
    PIRiA61271. RDHUCB.
    RefSeqiNP_001273718.1. NM_001286789.1. [P16152-2]
    NP_001748.1. NM_001757.3. [P16152-1]
    UniGeneiHs.88778.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WMAX-ray1.24A2-277[»]
    2PFGX-ray1.54A2-277[»]
    3BHIX-ray2.27A2-277[»]
    3BHJX-ray1.77A2-277[»]
    3BHMX-ray1.80A2-277[»]
    4Z3DX-ray1.80A/B/C/D2-277[»]
    ProteinModelPortaliP16152.
    SMRiP16152. Positions 3-277.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi107319. 37 interactions.
    DIPiDIP-33136N.
    IntActiP16152. 26 interactions.
    MINTiMINT-1418935.
    STRINGi9606.ENSP00000290349.

    Chemistry

    BindingDBiP16152.
    ChEMBLiCHEMBL5586.
    DrugBankiDB00997. Doxorubicin.
    DB00502. Haloperidol.
    DB01046. Lubiprostone.
    DB04844. Tetrabenazine.
    GuidetoPHARMACOLOGYi1383.

    PTM databases

    iPTMnetiP16152.
    PhosphoSiteiP16152.
    SwissPalmiP16152.

    Polymorphism and mutation databases

    BioMutaiCBR1.
    DMDMi118519.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00295386.
    UCD-2DPAGEP16152.

    Proteomic databases

    EPDiP16152.
    MaxQBiP16152.
    PaxDbiP16152.
    PeptideAtlasiP16152.
    PRIDEiP16152.
    TopDownProteomicsiP16152-1. [P16152-1]

    Protocols and materials databases

    DNASUi873.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000290349; ENSP00000290349; ENSG00000159228. [P16152-1]
    ENST00000530908; ENSP00000434613; ENSG00000159228. [P16152-2]
    GeneIDi873.
    KEGGihsa:873.
    UCSCiuc002yvb.3. human. [P16152-1]

    Organism-specific databases

    CTDi873.
    GeneCardsiCBR1.
    HGNCiHGNC:1548. CBR1.
    HPAiHPA018433.
    MIMi114830. gene.
    neXtProtiNX_P16152.
    PharmGKBiPA26121.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG1208. Eukaryota.
    COG1028. LUCA.
    GeneTreeiENSGT00510000046499.
    HOVERGENiHBG001909.
    InParanoidiP16152.
    KOiK00079.
    OMAiFRSEIIT.
    OrthoDBiEOG7PGDR4.
    PhylomeDBiP16152.
    TreeFamiTF329359.

    Enzyme and pathway databases

    BRENDAi1.1.1.184. 2681.
    ReactomeiR-HSA-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
    SABIO-RKP16152.

    Miscellaneous databases

    EvolutionaryTraceiP16152.
    GeneWikiiCBR1.
    GenomeRNAii873.
    PROiP16152.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP16152.
    CleanExiHS_CBR1.
    ExpressionAtlasiP16152. baseline and differential.
    GenevisibleiP16152. HS.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    IPR002347. SDR_fam.
    [Graphical view]
    PANTHERiPTHR24322. PTHR24322. 2 hits.
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.
    PR00080. SDRFAMILY.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Human carbonyl reductase. Nucleotide sequence analysis of a cDNA and amino acid sequence of the encoded protein."
      Wermuth B., Bohren K.M., Heinemann G., von Wartburg J.-P., Gabbay K.H.
      J. Biol. Chem. 263:16185-16188(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
      Tissue: Placenta.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
      Tissue: Mammary gland.
    3. "Genomic sequence and expression of a cloned human carbonyl reductase gene with daunorubicin reductase activity."
      Forrest G.L., Akman S., Doroshow J., Rivera H., Kaplan W.D.
      Mol. Pharmacol. 40:502-507(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    4. "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] (ISOFORM 1).
    5. "Human fetal brain carbonyl reductases."
      Terada T., Mizobuchi H.
      Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal brain.
    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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. "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] (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] (ISOFORMS 1 AND 2).
      Tissue: Hippocampus.
    9. SeattleSNPs variation discovery resource
      Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT SER-131.
    10. "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].
    11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. "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: Skin.
    13. "Carboxyethyllysine in a protein: native carbonyl reductase/NADP(+)-dependent prostaglandin dehydrogenase."
      Krook M., Ghosh D., Stroemberg R., Carlquist M., Joernvall H.
      Proc. Natl. Acad. Sci. U.S.A. 90:502-506(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, N6-1-CARBOXYETHYLATION AT LYS-239.
    14. "Inhibition of polymorphic human carbonyl reductase 1 (CBR1) by the cardioprotectant flavonoid 7-monohydroxyethyl rutoside (monoHER)."
      Gonzalez-Covarrubias V., Kalabus J.L., Blanco J.G.
      Pharm. Res. 25:1730-1734(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, FUNCTION.
    15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "An unbiased cell morphology-based screen for new, biologically active small molecules."
      Tanaka M., Bateman R., Rauh D., Vaisberg E., Ramachandani S., Zhang C., Hansen K.C., Burlingame A.L., Trautman J.K., Shokat K.M., Adams C.L.
      PLoS Biol. 3:E128-E128(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) OF 2-276 IN COMPLEX WITH THE SYNTHETIC INHIBITOR HYDROXY-PP AND NADP, IDENTIFICATION BY MASS SPECTROMETRY, PARTIAL PROTEIN SEQUENCE, FUNCTION.
    18. "Glutathione traps formaldehyde by formation of a bicyclo[4.4.1]undecane adduct."
      Bateman R., Rauh D., Shokat K.M.
      Org. Biomol. Chem. 5:3363-3367(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 2-277 IN COMPLEX WITH NADP AND FORMALDEHYDE-GLUTATHIONE ADDUCT, FUNCTION.
    19. "Human carbonyl reductase 1 is an S-nitrosoglutathione reductase."
      Bateman R.L., Rauh D., Tavshanjian B., Shokat K.M.
      J. Biol. Chem. 283:35756-35762(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 2-277 IN COMPLEX WITH NADP, SUBSTRATE ANALOGS, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    20. "A functional genetic polymorphism on human carbonyl reductase 1 (CBR1 V88I) impacts on catalytic activity and NADPH binding affinity."
      Gonzalez-Covarrubias V., Ghosh D., Lakhman S.S., Pendyala L., Blanco J.G.
      Drug Metab. Dispos. 35:973-980(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ILE-88, CHARACTERIZATION OF VARIANT ILE-88, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.

    Entry informationi

    Entry nameiCBR1_HUMAN
    AccessioniPrimary (citable) accession number: P16152
    Secondary accession number(s): B2RBZ7, B4DFK7, Q3LHW8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 23, 2007
    Last modified: July 6, 2016
    This is version 184 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 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

    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 one 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.