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YEAST:NCB5R

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) CBR1 (synonyms: CBR, CBR5)
Protein Name(s) NADH-cytochrome b5 reductase 1

Microsomal cytochrome b reductase P35

External Links
UniProt P38626
EMBL Z28365
Z46861
BK006942
PIR S49935
RefSeq NP_012221.2
ProteinModelPortal P38626
SMR P38626
BioGrid 34947
IntAct P38626
MINT MINT-1324688
MaxQB P38626
PeptideAtlas P38626
EnsemblFungi YIL043C
GeneID 854768
KEGG sce:YIL043C
EuPathDB FungiDB:YIL043C
SGD S000001305
GeneTree ENSGT00390000008881
HOGENOM HOG000175005
InParanoid P38626
KO K00326
OMA CSAVQDA
OrthoDB EOG7N63XM
BioCyc YEAST:YIL043C-MONOMER
Reactome [www.reactome.org/content/detail/R-SCE-114608 R-SCE-114608]
[www.reactome.org/content/detail/R-SCE-1237044 R-SCE-1237044]
[www.reactome.org/content/detail/R-SCE-196836 R-SCE-196836]
PRO PR:P38626
Proteomes UP000002311
GO GO:0005789
GO:0016021
GO:0005741
GO:0004128
InterPro IPR017927
IPR001709
IPR001834
IPR008333
IPR001433
IPR017938
Pfam PF00970
PF00175
PRINTS PR00406
PR00371
SUPFAM SSF63380
PROSITE PS51384

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0003954

NADH dehydrogenase activity

PMID:27694803[1]

ECO:0000314

F

The author expressed Cbr1 and monitored the reduction of Dph3 through Dph3's absorption at 488nm. The author then added NADH to the reaction tube and noticed that Cbr1 rapidly reduced Dph3 (this is shown is figure 1b). However, the author also found that Cbr1 did not reduce Dph3 upon addition of NADPH (supplemental figure 3).

complete
CACAO 12135

part_of

GO:0005739

mitochondrion

PMID:16823961[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005741

mitochondrial outer membrane

PMID:16407407[3]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:26928762[4]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:24769239[5]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:14576278[6]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0008150

biological_process

GO_REF:0000015

ECO:0000307

no biological data found used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004128

cytochrome-b5 reductase activity, acting on NAD(P)H

PMID:14930[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000182794
PANTHER:PTN001064671
SGD:S000004594

C

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001433
InterPro:IPR001709
InterPro:IPR001834
InterPro:IPR017927

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001433
InterPro:IPR001709
InterPro:IPR001834
InterPro:IPR017927

P

Seeded From UniProt

complete

enables

GO:0004128

cytochrome-b5 reductase activity, acting on NAD(P)H

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.6.2.2

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0496

C

Seeded From UniProt

complete

part_of

GO:0005783

endoplasmic reticulum

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0256

C

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

part_of

GO:0005741

mitochondrial outer membrane

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1000
UniProtKB-SubCell:SL-0172

C

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

part_of

GO:0005789

endoplasmic reticulum membrane

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0097

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Lin, Z et al. (2016) Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification. Nat. Chem. Biol. PubMed GONUTS page
  2. Reinders, J et al. (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J. Proteome Res. 5 1543-54 PubMed GONUTS page
  3. Zahedi, RP et al. (2006) Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins. Mol. Biol. Cell 17 1436-50 PubMed GONUTS page
  4. Yofe, I et al. (2016) One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy. Nat. Methods 13 371-378 PubMed GONUTS page
  5. Renvoisé, M et al. (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. J Proteomics 106 140-50 PubMed GONUTS page
  6. Sickmann, A et al. (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc. Natl. Acad. Sci. U.S.A. 100 13207-12 PubMed GONUTS page
  7. Kubota, S et al. (1977) Studies on the microsomal electron-transport system of anaerobically grown yeast. IV. Purification and characterization of NADH-cytochrome b5 reductase. J. Biochem. 81 187-95 PubMed GONUTS page
  8. Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page