CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001309
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glutaredoxin-3 
Protein Synonyms/Alias
 PKC-interacting cousin of thioredoxin; PICOT; PKC-theta-interacting protein; PKCq-interacting protein; Thioredoxin-like protein 2 
Gene Name
 GLRX3 
Gene Synonyms/Alias
 PICOT; TXNL2; HUSSY-22 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
67LPQVSFVKLEAEGVPubiquitination[1]
79GVPEVSEKYEISSVPubiquitination[1]
92VPTFLFFKNSQKIDRacetylation[2]
92VPTFLFFKNSQKIDRubiquitination[1, 3, 4]
110AHAPELTKKVQRHASacetylation[5, 6]
111HAPELTKKVQRHASSubiquitination[7]
139DLNLRLKKLTHAAPCubiquitination[7]
163EPRCGFSKQMVEILHubiquitination[6, 7, 8]
240PKLEERLKVLTNKASubiquitination[3, 4, 7]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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
Functional Description
 Critical negative regulator of cardiac hypertrophy and a positive inotropic regulator (By similarity). May play a role in regulating the function of the thioredoxin system. Does not posses any thyoredoxin activity since it lacks the conserved motif that is essential for catalytic activity. 
Sequence Annotation
 DOMAIN 2 117 Thioredoxin.
 DOMAIN 144 236 Glutaredoxin 1.
 DOMAIN 237 335 Glutaredoxin 2.
 METAL 159 159 Iron-sulfur (2Fe-2S); shared with dimeric
 METAL 261 261 Iron-sulfur (2Fe-2S); shared with dimeric
 MOD_RES 2 2 N-acetylalanine (By similarity).  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 335 AA 
Protein Sequence
MAAGAAEAAV AAVEEVGSAG QFEELLRLKA KSLLVVHFWA PWAPQCAQMN EVMAELAKEL 60
PQVSFVKLEA EGVPEVSEKY EISSVPTFLF FKNSQKIDRL DGAHAPELTK KVQRHASSGS 120
FLPSANEHLK EDLNLRLKKL THAAPCMLFM KGTPQEPRCG FSKQMVEILH KHNIQFSSFD 180
IFSDEEVRQG LKAYSSWPTY PQLYVSGELI GGLDIIKELE ASEELDTICP KAPKLEERLK 240
VLTNKASVML FMKGNKQEAK CGFSKQILEI LNSTGVEYET FDILEDEEVR QGLKAYSNWP 300
TYPQLYVKGE LVGGLDIVKE LKENGELLPI LRGEN 335 
Gene Ontology
 GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
 GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
 GO:0009055; F:electron carrier activity; IEA:InterPro.
 GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro.
 GO:0010614; P:negative regulation of cardiac muscle hypertrophy; ISS:UniProtKB.
 GO:0002026; P:regulation of the force of heart contraction; ISS:UniProtKB. 
Interpro
 IPR002109; Glutaredoxin.
 IPR004480; Monothiol_GRX-rel.
 IPR012336; Thioredoxin-like_fold.
 IPR013766; Thioredoxin_domain. 
Pfam
 PF00462; Glutaredoxin
 PF00085; Thioredoxin 
SMART
  
PROSITE
 PS51354; GLUTAREDOXIN_2
 PS00194; THIOREDOXIN_1
 PS51352; THIOREDOXIN_2 
PRINTS