CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-039509
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 NADH-cytochrome b5 reductase 3 
Protein Synonyms/Alias
  
Gene Name
 Cyb5r3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
19TLENPDIKYPLRLIDacetylation[1, 2, 3, 4, 5, 6, 7]
19TLENPDIKYPLRLIDubiquitination[8]
27YPLRLIDKEVISPDTacetylation[3, 6]
27YPLRLIDKEVISPDTsuccinylation[6]
27YPLRLIDKEVISPDTubiquitination[8]
80PVSSDDDKGFVDLVVacetylation[7]
92LVVKVYFKDTHPKFPacetylation[7]
92LVVKVYFKDTHPKFPubiquitination[8]
97YFKDTHPKFPAGGKMacetylation[2, 6, 7]
97YFKDTHPKFPAGGKMubiquitination[8]
103PKFPAGGKMSQYLENacetylation[3, 6]
103PKFPAGGKMSQYLENsuccinylation[6]
103PKFPAGGKMSQYLENubiquitination[8]
112SQYLENMKIGDTIEFubiquitination[8]
131GLLVYQGKGKFAIRAubiquitination[8]
Reference
 [1] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
 Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
 J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
 [2] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [5] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [6] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [7] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [8] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 144 AA 
Protein Sequence
MKLFQRSTPA ITLENPDIKY PLRLIDKEVI SPDTRRFRFA LPSPQHILGL PIGQHIYLST 60
RIDGNLVIRP YTPVSSDDDK GFVDLVVKVY FKDTHPKFPA GGKMSQYLEN MKIGDTIEFR 120
GPNGLLVYQG KGKFAIRADK KSNP 144 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IEA:Compara.
 GO:0005811; C:lipid particle; IEA:Compara.
 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0043531; F:ADP binding; IEA:Compara.
 GO:0016208; F:AMP binding; IEA:Compara.
 GO:0071949; F:FAD binding; IEA:Compara.
 GO:0051287; F:NAD binding; IEA:Compara.
 GO:0016491; F:oxidoreductase activity; IEA:InterPro. 
Interpro
 IPR017927; Fd_Rdtase_FAD-bd.
 IPR001834; NADH-Cyt_B5_reductase.
 IPR008333; OxRdtase_FAD-bd_dom.
 IPR017938; Riboflavin_synthase-like_b-brl. 
Pfam
 PF00970; FAD_binding_6 
SMART
  
PROSITE
 PS51384; FAD_FR 
PRINTS
 PR00406; CYTB5RDTASE.