CPLM-001754

Genbank Nucleotide ID

NADH-cytochrome b5 reductase 3

Protein Synonyms/Alias

B5R; Cytochrome b5 reductase; Diaphorase-1; NADH-cytochrome b5 reductase 3 membrane-bound form; NADH-cytochrome b5 reductase 3 soluble form

Homo sapiens (Human)

Position	Peptide	Type	References
42	TLESPDIKYPLRLID	acetylation	[1, 2]
42	TLESPDIKYPLRLID	ubiquitination	[3, 4, 5, 6, 7]
120	YFKDTHPKFPAGGKM	ubiquitination	[4, 5, 6]
126	PKFPAGGKMSQYLES	ubiquitination	[4, 5]
173	NPIIRTVKSVGMIAG	ubiquitination	[4, 6, 8, 9]
196	QVIRAIMKDPDDHTV	ubiquitination	[4, 5]
214	LFANQTEKDILLRPE	ubiquitination	[4]
234	NKHSARFKLWYTLDR	ubiquitination	[4, 8, 10]

[1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[2] Regulation of cellular metabolism by protein lysine acetylation.
Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
[3] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
[4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[8] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[9] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[10] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]

Functional Description

Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction.

DOMAIN 40 152 FAD-binding FR-type.
NP_BIND 132 147 FAD (By similarity).
NP_BIND 171 206 FAD (By similarity).
MOD_RES 42 42 N6-acetyllysine.
MOD_RES 43 43 Phosphotyrosine.
MOD_RES 120 120 N6-acetyllysine (By similarity).
MOD_RES 130 130 Phosphotyrosine (By similarity).
LIPID 2 2 N-myristoyl glycine.

3D-structure; Acetylation; Alternative promoter usage; Alternative splicing; Cholesterol biosynthesis; Cholesterol metabolism; Complete proteome; Cytoplasm; Direct protein sequencing; Disease mutation; Endoplasmic reticulum; FAD; Flavoprotein; Lipid biosynthesis; Lipid metabolism; Lipoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane; Myristate; NAD; Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome; Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis; Sterol metabolism.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO:0005833; C:hemoglobin complex; TAS:ProtInc.
GO:0005811; C:lipid particle; IDA:UniProtKB.
GO:0005743; C:mitochondrial inner membrane; IEA:Compara.
GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
GO:0043531; F:ADP binding; IEA:Compara.
GO:0016208; F:AMP binding; IEA:Compara.
GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; TAS:Reactome.
GO:0071949; F:FAD binding; IDA:UniProtKB.
GO:0050660; F:flavin adenine dinucleotide binding; IEA:Compara.
GO:0051287; F:NAD binding; IEA:Compara.
GO:0008015; P:blood circulation; TAS:ProtInc.
GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
GO:0019852; P:L-ascorbic acid metabolic process; TAS:Reactome.

IPR017927; Fd_Rdtase_FAD-bd.
IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR001834; NADH-Cyt_B5_reductase.
IPR008333; OxRdtase_FAD-bd_dom.
IPR001433; OxRdtase_FAD/NAD-bd.
IPR017938; Riboflavin_synthase-like_b-brl.

PF00970; FAD_binding_6
PF00175; NAD_binding_1

PR00406; CYTB5RDTASE.
PR00371; FPNCR.