CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021003
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 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 
Gene Name
 Cyb5r3 
Gene Synonyms/Alias
 Dia1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
42TLENPDIKYPLRLIDacetylation[1, 2]
42TLENPDIKYPLRLIDubiquitination[3]
50YPLRLIDKEVISPDTacetylation[2]
50YPLRLIDKEVISPDTubiquitination[3]
115LVVKVYFKDTHPKFPacetylation[2]
115LVVKVYFKDTHPKFPubiquitination[3]
120YFKDTHPKFPAGGKMacetylation[1, 2]
120YFKDTHPKFPAGGKMubiquitination[3]
126PKFPAGGKMSQYLENubiquitination[3]
135SQYLENMKIGDTIEFubiquitination[3]
154GLLVYQGKGKFAIRAubiquitination[3]
173NPVVRTVKSVGMIAGubiquitination[3]
196QVIRAVLKDPNDHTVacetylation[2]
234NEHSARFKLWYTVDKubiquitination[3]
241KLWYTVDKAPDAWDYubiquitination[3]
295LERVGHPKERCFTF*acetylation[4]
Reference
 [1] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] 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]
 [4] 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
Functional Description
 Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction (By similarity). 
Sequence Annotation
 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 (By similarity).
 MOD_RES 120 120 N6-acetyllysine.
 MOD_RES 130 130 Phosphotyrosine.
 LIPID 2 2 N-myristoyl glycine (By similarity).  
Keyword
 Acetylation; Alternative promoter usage; Cholesterol biosynthesis; Cholesterol metabolism; Complete proteome; Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; FAD; Flavoprotein; Lipid biosynthesis; Lipid metabolism; Lipoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane; Myristate; NAD; Oxidoreductase; Phosphoprotein; Reference proteome; Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis; Sterol metabolism. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 301 AA 
Protein Sequence
MGAQLSTLSH VVLSPVWFIY SLFMKLFQRS TPAITLENPD IKYPLRLIDK EVISPDTRRF 60
RFALPSPQHI LGLPIGQHIY LSTRIDGNLV IRPYTPVSSD DDKGFVDLVV KVYFKDTHPK 120
FPAGGKMSQY LENMKIGDTI EFRGPNGLLV YQGKGKFAIR ADKKSNPVVR TVKSVGMIAG 180
GTGITPMLQV IRAVLKDPND HTVCYLLFAN QSEKDILLRP ELEELRNEHS ARFKLWYTVD 240
KAPDAWDYSQ GFVNEEMIRD HLPTPGEEPL ILMCGPPPMI QFACLPNLER VGHPKERCFT 300
F 301 
Gene Ontology
 GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0005811; C:lipid particle; IEA:Compara.
 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
 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; IEA:EC.
 GO:0071949; F:FAD binding; IEA:Compara.
 GO:0051287; F:NAD binding; IEA:Compara.
 GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW. 
Interpro
 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. 
Pfam
 PF00970; FAD_binding_6
 PF00175; NAD_binding_1 
SMART
  
PROSITE
 PS51384; FAD_FR 
PRINTS
 PR00406; CYTB5RDTASE.
 PR00371; FPNCR.