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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

  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: UniProtKB
  2. phylloquinone catabolic process Source: Ensembl
Complete GO annotation...

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: UniProtKB
  4. nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26122.

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

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.
ExpressionAtlasiO75828. baseline and differential.
GenevestigatoriO75828.

Organism-specific databases

HPAiHPA018434.

Interactioni

Protein-protein interaction databases

BioGridi107320. 8 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. 8 interactions.
IntActiO75828. 5 interactions.
MINTiMINT-1412792.
STRINGi9606.ENSP00000290354.

Chemistry

ChEMBLiCHEMBL6008.
DrugBankiDB00997. Doxorubicin.

PTM databases

PhosphoSiteiO75828.

2D gel databases

REPRODUCTION-2DPAGEIPI00290462.

Proteomic databases

MaxQBiO75828.
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

SABIO-RKO75828.

Miscellaneous databases

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

Gene expression databases

BgeeiO75828.
CleanExiHS_CBR3.
ExpressionAtlasiO75828. baseline and differential.
GenevestigatoriO75828.

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: March 4, 2015
This is version 135 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.