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O75828 (CBR3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carbonyl reductase [NADPH] 3

EC=1.1.1.184
Alternative name(s):
NADPH-dependent carbonyl reductase 3
Gene names
Name:CBR3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length277 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has low NADPH-dependent oxidoreductase activity towards 4-benzoylpyridine and menadione (in vitro). Ref.9

Catalytic activity

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

Subcellular location

Cytoplasm Ref.9.

Tissue specificity

Detected in ovary, pancreas, intestine, colon, kidney, brain, thymus, lung, heart, liver, spleen, leukocyte, prostate and testis. Ref.9

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Biophysicochemical properties

Kinetic parameters:

KM=25 µM for menadione (Ref.12) Ref.9 Ref.12

KM=43 µM for menadione (Ref.9)

KM=90 µM for NADPH (Ref.12)

KM=38 µM for NADPH (Ref.9)

pH dependence:

Optimum pH is 5.5-7.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandNADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processphylloquinone catabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from direct assay Ref.9. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 22664934. Source: UniProt

nucleus

Inferred from direct assay. Source: HPA

   Molecular_function3-keto sterol reductase activity

Inferred from electronic annotation. Source: Ensembl

NADPH binding

Inferred from direct assay Ref.9. Source: UniProtKB

carbonyl reductase (NADPH) activity

Inferred from direct assay Ref.9. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 277277Carbonyl reductase [NADPH] 3
PRO_0000054608

Regions

Nucleotide binding10 – 3425NADP
Nucleotide binding38 – 425NADP
Nucleotide binding63 – 642NADP
Nucleotide binding194 – 1985NADP

Sites

Active site1941Proton acceptor By similarity
Binding site901NADP; via carbonyl oxygen
Binding site1401Substrate By similarity
Binding site2391NADP

Natural variations

Natural variant41C → Y. Ref.5
Corresponds to variant rs8133052 [ dbSNP | Ensembl ].
VAR_033868
Natural variant841L → V. Ref.5
Corresponds to variant rs9282628 [ dbSNP | Ensembl ].
VAR_033869
Natural variant931V → I.
Corresponds to variant rs2835285 [ dbSNP | Ensembl ].
VAR_033870
Natural variant1311P → S. Ref.5
Corresponds to variant rs16993929 [ dbSNP | Ensembl ].
VAR_033871
Natural variant2351M → L. Ref.5
Corresponds to variant rs4987121 [ dbSNP | Ensembl ].
VAR_033872
Natural variant2441V → M Increased catalytic activity. Ref.5 Ref.12
Corresponds to variant rs1056892 [ dbSNP | Ensembl ].
VAR_033873

Secondary structure

........................................... 277
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O75828 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8D39D6B99CFE5389

FASTA27730,850
        10         20         30         40         50         60 
MSSCSRVALV TGANRGIGLA IARELCRQFS GDVVLTARDV ARGQAAVQQL QAEGLSPRFH 

        70         80         90        100        110        120 
QLDIDDLQSI RALRDFLRKE YGGLNVLVNN AAVAFKSDDP MPFDIKAEMT LKTNFFATRN 

       130        140        150        160        170        180 
MCNELLPIMK PHGRVVNISS LQCLRAFENC SEDLQERFHS ETLTEGDLVD LMKKFVEDTK 

       190        200        210        220        230        240 
NEVHEREGWP NSPYGVSKLG VTVLSRILAR RLDEKRKADR ILVNACCPGP VKTDMDGKDS 

       250        260        270 
IRTVEEGAET PVYLALLPPD ATEPQGQLVH DKVVQNW 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001227.1. NM_001236.3.
UniGeneHs.154510.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HRBX-ray1.90A6-276[»]
ProteinModelPortalO75828.
SMRO75828. Positions 5-277.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107320. 5 interactions.
IntActO75828. 5 interactions.
MINTMINT-1412792.
STRING9606.ENSP00000290354.

Chemistry

ChEMBLCHEMBL6008.

PTM databases

PhosphoSiteO75828.

2D gel databases

REPRODUCTION-2DPAGEIPI00290462.

Proteomic databases

PaxDbO75828.
PeptideAtlasO75828.
PRIDEO75828.

Protocols and materials databases

DNASU874.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000290354; ENSP00000290354; ENSG00000159231.
GeneID874.
KEGGhsa:874.
UCSCuc002yve.3. human.

Organism-specific databases

CTD874.
GeneCardsGC21P037507.
HGNCHGNC:1549. CBR3.
HPAHPA018434.
MIM603608. gene.
neXtProtNX_O75828.
PharmGKBPA26122.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1028.
HOVERGENHBG001909.
InParanoidO75828.
KOK00084.
OMATEPHGQL.
OrthoDBEOG7PGDR4.
PhylomeDBO75828.
TreeFamTF329359.

Enzyme and pathway databases

SABIO-RKO75828.

Gene expression databases

BgeeO75828.
CleanExHS_CBR3.
GenevestigatorO75828.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO75828.
GeneWikiCBR3.
GenomeRNAi874.
NextBio3638.
PROO75828.
SOURCESearch...

Entry information

Entry nameCBR3_HUMAN
AccessionPrimary (citable) accession number: O75828
Secondary accession number(s): Q6FHP2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM