CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001758
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glutathione reductase, mitochondrial 
Protein Synonyms/Alias
 GR; GRase 
Gene Name
 GSR 
Gene Synonyms/Alias
 GLUR; GRD1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
97AAVVESHKLGGTCVNubiquitination[1]
111NVGCVPKKVMWNTAVubiquitination[1]
164IYQNNLTKSHIEIIRubiquitination[1]
181AAFTSDPKPTIEVSGubiquitination[2, 3]
189PTIEVSGKKYTAPHIubiquitination[4]
300SQVKEVKKTLSGLEVubiquitination[2, 3, 5]
340IGRVPNTKDLSLNKLubiquitination[1, 4]
346TKDLSLNKLGIQTDDubiquitination[1, 4, 6]
379AVGDVCGKALLTPVAubiquitination[1, 7]
401AHRLFEYKEDSKLDYacetylation[8]
405FEYKEDSKLDYNNIPubiquitination[4]
441KYGIENVKTYSTSFTubiquitination[1, 4, 6]
456PMYHAVTKRKTKCVMubiquitination[2, 3]
501AVKMGATKADFDNTVubiquitination[4, 6]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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] 
Functional Description
 Maintains high levels of reduced glutathione in the cytosol. 
Sequence Annotation
 NP_BIND 94 102 FAD.
 ACT_SITE 511 511 Proton acceptor.
 DISULFID 102 107 Redox-active.
 DISULFID 134 134 Interchain.  
Keyword
 3D-structure; Alternative initiation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; FAD; Flavoprotein; Mitochondrion; NADP; Oxidoreductase; Polymorphism; Redox-active center; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 522 AA 
Protein Sequence
MALLPRALSA GAGPSWRRAA RAFRGFLLLL PEPAALTRAL SRAMACRQEP QPQGPPPAAG 60
AVASYDYLVI GGGSGGLASA RRAAELGARA AVVESHKLGG TCVNVGCVPK KVMWNTAVHS 120
EFMHDHADYG FPSCEGKFNW RVIKEKRDAY VSRLNAIYQN NLTKSHIEII RGHAAFTSDP 180
KPTIEVSGKK YTAPHILIAT GGMPSTPHES QIPGASLGIT SDGFFQLEEL PGRSVIVGAG 240
YIAVEMAGIL SALGSKTSLM IRHDKVLRSF DSMISTNCTE ELENAGVEVL KFSQVKEVKK 300
TLSGLEVSMV TAVPGRLPVM TMIPDVDCLL WAIGRVPNTK DLSLNKLGIQ TDDKGHIIVD 360
EFQNTNVKGI YAVGDVCGKA LLTPVAIAAG RKLAHRLFEY KEDSKLDYNN IPTVVFSHPP 420
IGTVGLTEDE AIHKYGIENV KTYSTSFTPM YHAVTKRKTK CVMKMVCANK EEKVVGIHMQ 480
GLGCDEMLQG FAVAVKMGAT KADFDNTVAI HPTSSEELVT LR 522 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0009055; F:electron carrier activity; TAS:UniProtKB.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0004362; F:glutathione-disulfide reductase activity; TAS:Reactome.
 GO:0050661; F:NADP binding; IEA:InterPro.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro.
 GO:0006749; P:glutathione metabolic process; IEA:InterPro.
 GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome. 
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.