HUMAN:NB5R3

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	CYB5R3 (synonyms: DIA1)
Protein Name(s)	NADH-cytochrome b5 reductase 3 B5R Cytochrome b5 reductase Diaphorase-1 NADH-cytochrome b5 reductase 3 membrane-bound form NADH-cytochrome b5 reductase 3 soluble form
External Links
UniProt	P00387
EMBL	M28713 M28705 M28706 M28707 M28708 M28709 M28710 M28711 Y09501 AF361370 AJ010116 AJ010117 AJ010118 AY341030 BT009821 CR456435 AF061830 AF061831 AK302204 Z93241 Z93241 BC004821 AJ310899 AJ310900 M16461 M16462
CCDS	CCDS33658.1
PIR	JS0468
RefSeq	NP_000389.1 NP_001123291.1 NP_001165131.1 NP_001165132.1 NP_015565.1
UniGene	Hs.561064
PDB	1M91 1UMK
PDBsum	1M91 1UMK
ProteinModelPortal	P00387
SMR	P00387
BioGrid	108071
DIP	DIP-50463N
IntAct	P00387
MINT	MINT-5003981
ChEMBL	CHEMBL2146
DrugBank	DB03147
PhosphoSite	P00387
DMDM	127846
REPRODUCTION-2DPAGE	IPI00446235
MaxQB	P00387
PaxDb	P00387
PRIDE	P00387
DNASU	1727
Ensembl	ENST00000352397 ENST00000361740 ENST00000402438 ENST00000407332 ENST00000407623
GeneID	1727
KEGG	hsa:1727
UCSC	uc003bcx.3 uc011aps.2
CTD	1727
GeneCards	GC22M043014
HGNC	HGNC:2873
HPA	HPA001566
MIM	250800 613213
neXtProt	NX_P00387
Orphanet	139373 139380
PharmGKB	PA27331
eggNOG	COG0543
GeneTree	ENSGT00390000008881
HOGENOM	HOG000175005
HOVERGEN	HBG052580
InParanoid	P00387
KO	K00326
OrthoDB	EOG7CZK69
PhylomeDB	P00387
TreeFam	TF314333
BioCyc	MetaCyc:HS02015-MONOMER
BRENDA	1.6.2.2
Reactome	REACT_11202
SABIO-RK	P00387
EvolutionaryTrace	P00387
GeneWiki	CYB5R3
GenomeRNAi	1727
NextBio	6983
PRO	PR:P00387
Proteomes	UP000005640
Bgee	P00387
CleanEx	HS_CYB5R3
ExpressionAtlas	P00387
Genevestigator	P00387
GO	GO:0005737 GO:0005783 GO:0005789 GO:0070062 GO:0005833 GO:0005811 GO:0016020 GO:0005743 GO:0005741 GO:0005739 GO:0043531 GO:0016208 GO:0004128 GO:0071949 GO:0050660 GO:0051287 GO:0008015 GO:0006695 GO:0019852 GO:0044281 GO:0006766 GO:0006767
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
part_of	GO:0016020	membrane	PMID:19946888^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:20833797^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001134)	Seeded From UniProt	complete
part_of	GO:0005811	lipid droplet	PMID:14741744^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(UBERON:0002107)	Seeded From UniProt	complete
enables	GO:0071949	FAD binding	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000452227 UniProtKB:P00387	F		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0051287	NAD binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20070 ensembl:ENSRNOP00000061381	F		Seeded From UniProt	complete
enables	GO:0050660	flavin adenine dinucleotide binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20070 ensembl:ENSRNOP00000061381	F		Seeded From UniProt	complete
enables	GO:0043531	ADP binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20070 ensembl:ENSRNOP00000061381	F		Seeded From UniProt	complete
enables	GO:0016208	AMP binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20070 ensembl:ENSRNOP00000061381	F		Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20070 ensembl:ENSRNOP00000061381	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
enables	GO:0071949	FAD binding	PMID:20861021^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:9207238^[6]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0008015	blood circulation	PMID:1400360^[7]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005833	hemoglobin complex	PMID:1400360^[7]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:9207238^[6]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004128	cytochrome-b5 reductase activity, acting on NAD(P)H	PMID:1400360^[7]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0043312	neutrophil degranulation	Reactome:R-HSA-6798695	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0035578	azurophil granule lumen	Reactome:R-HSA-6798751	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0019852	L-ascorbic acid metabolic process	Reactome:R-HSA-196836	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006805	xenobiotic metabolic process	Reactome:R-HSA-211945	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005741	mitochondrial outer membrane	Reactome:R-HSA-8936442 Reactome:R-HSA-198824	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-6798751	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0008203	cholesterol metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0153	P		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
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: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
involved_in	GO:0006694	steroid biosynthetic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0752	P		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
involved_in	GO:0006695	cholesterol biosynthetic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0152	P		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
involved_in	GO:0008202	steroid metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0753	P		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
involved_in	GO:0016126	sterol biosynthetic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0756	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
involved_in	GO:0006629	lipid metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0443	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
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Notes

References

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

↑ Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
↑ Zhao, X et al. (2011) Phosphoproteome analysis of functional mitochondria isolated from resting human muscle reveals extensive phosphorylation of inner membrane protein complexes and enzymes. Mol. Cell Proteomics 10 M110.000299 PubMed GONUTS page
↑ Fujimoto, Y et al. (2004) Identification of major proteins in the lipid droplet-enriched fraction isolated from the human hepatocyte cell line HuH7. Biochim. Biophys. Acta 1644 47-59 PubMed GONUTS page
↑ Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Wahl, B et al. (2010) Biochemical and spectroscopic characterization of the human mitochondrial amidoxime reducing components hmARC-1 and hmARC-2 suggests the existence of a new molybdenum enzyme family in eukaryotes. J. Biol. Chem. 285 37847-59 PubMed GONUTS page
↑ ^6.0 ^6.1 Du, M et al. (1997) Identification of alternative first exons of NADH-cytochrome b5 reductase gene expressed ubiquitously in human cells. Biochem. Biophys. Res. Commun. 235 779-83 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Shirabe, K et al. (1992) Enzymatic instability of NADH-cytochrome b5 reductase as a cause of hereditary methemoglobinemia type I (red cell type). J. Biol. Chem. 267 20416-21 PubMed GONUTS page

[PMID:19946888-1] Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page

[PMID:20833797-2] Zhao, X et al. (2011) Phosphoproteome analysis of functional mitochondria isolated from resting human muscle reveals extensive phosphorylation of inner membrane protein complexes and enzymes. Mol. Cell Proteomics 10 M110.000299 PubMed GONUTS page

[PMID:14741744-3] Fujimoto, Y et al. (2004) Identification of major proteins in the lipid droplet-enriched fraction isolated from the human hepatocyte cell line HuH7. Biochim. Biophys. Acta 1644 47-59 PubMed GONUTS page

[PMID:21873635-4] Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:20861021-5] Wahl, B et al. (2010) Biochemical and spectroscopic characterization of the human mitochondrial amidoxime reducing components hmARC-1 and hmARC-2 suggests the existence of a new molybdenum enzyme family in eukaryotes. J. Biol. Chem. 285 37847-59 PubMed GONUTS page

[PMID:9207238-6] 6.0 ^6.1 Du, M et al. (1997) Identification of alternative first exons of NADH-cytochrome b5 reductase gene expressed ubiquitously in human cells. Biochem. Biophys. Res. Commun. 235 779-83 PubMed GONUTS page

[PMID:1400360-7] 7.0 ^7.1 ^7.2 Shirabe, K et al. (1992) Enzymatic instability of NADH-cytochrome b5 reductase as a cause of hereditary methemoglobinemia type I (red cell type). J. Biol. Chem. 267 20416-21 PubMed GONUTS page

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HUMAN:NB5R3

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