CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007949
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glutathione reductase, mitochondrial 
Protein Synonyms/Alias
 GR; GRase 
Gene Name
 Gsr 
Gene Synonyms/Alias
 Gr1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
75AAVVESHKLGGTCVNacetylation[1, 2, 3]
88VNVGCVPKKVMWNTAacetylation[2, 3, 4]
274VLKFTQVKEVKKTSSacetylation[1, 2, 4]
Reference
 [1] 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]
 [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] 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]
 [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
 Maintains high levels of reduced glutathione in the cytosol. 
Sequence Annotation
 NP_BIND 72 80 FAD (By similarity).
 ACT_SITE 489 489 Proton acceptor (By similarity).
 DISULFID 80 85 Redox-active (By similarity).
 DISULFID 112 112 Interchain (By similarity).  
Keyword
 Acetylation; Alternative initiation; Complete proteome; Cytoplasm; Disulfide bond; FAD; Flavoprotein; Mitochondrion; NADP; Oxidoreductase; Redox-active center; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 500 AA 
Protein Sequence
MALLPRALGV GAAPSLRRAA RALTCAMASP GEPQPPAPDT SSFDYLVIGG GSGGLASARR 60
AAELGARAAV VESHKLGGTC VNVGCVPKKV MWNTAVHSEF MHDHVDYGFQ SCEGKFSWHV 120
IKQKRDAYVS RLNTIYQNNL TKSHIEIIHG YATFADGPRP TVEVNGKKFT APHILIATGG 180
VPTVPHESQI PGASLGITSD GFFQLEDLPS RSVIVGAGYI AVEIAGILSA LGSKTSLMIR 240
HDKVLRNFDS LISSNCTEEL ENAGVEVLKF TQVKEVKKTS SGLELQVVTS VPGRKPTTTM 300
IPDVDCLLWA IGRDPNSKGL NLNKVGIQTD EKGHILVDEF QNTNVKGVYA VGDVCGKALL 360
TPVAIAAGRK LAHRLFECKQ DSKLDYDNIP TVVFSHPPIG TVGLTEDEAV HKYGKDNVKI 420
YSTAFTPMYH AVTTRKTKCV MKMVCANKEE KVVGIHMQGI GCDEMLQGFA VAVKMGATKA 480
DFDNTVAIHP TSSEELVTLR 500 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0004362; F:glutathione-disulfide reductase activity; IDA:MGI.
 GO:0050661; F:NADP binding; IEA:InterPro.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro.
 GO:0006749; P:glutathione metabolic process; IC:MGI. 
Interpro
 IPR016156; FAD/NAD-linked_Rdtase_dimer.
 IPR013027; FAD_pyr_nucl-diS_OxRdtase.
 IPR006322; Glutathione_Rdtase_euk/bac.
 IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
 IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD.
 IPR012999; Pyr_OxRdtase_I_AS.
 IPR001327; Pyr_OxRdtase_NAD-bd_dom. 
Pfam
 PF00070; Pyr_redox
 PF07992; Pyr_redox_2
 PF02852; Pyr_redox_dim 
SMART
  
PROSITE
 PS00076; PYRIDINE_REDOX_1 
PRINTS
 PR00368; FADPNR.