CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020536
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 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
141DLSLRLKKLTHAAPCubiquitination[1]
153APCMLFMKGTPQEPRacetylation[2]
153APCMLFMKGTPQEPRubiquitination[1]
242PKLEERLKVLTNKASubiquitination[1]
321VGGLDIVKELKDNGEubiquitination[1]
324LDIVKELKDNGELLPubiquitination[1]
Reference
 [1] 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]
 [2] 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
Functional Description
 Critical negative regulator of cardiac hypertrophy and a positive inotropic regulator. May play a role in regulating the function of the thioredoxin system. Does not possess any thyoredoxin activity since it lacks the conserved motif that is essential for catalytic activity. Has an essential function in embryogenesis. 
Sequence Annotation
 DOMAIN 2 119 Thioredoxin.
 DOMAIN 144 238 Glutaredoxin 1.
 DOMAIN 239 337 Glutaredoxin 2.
 METAL 161 161 Iron-sulfur (2Fe-2S); shared with dimeric
 METAL 263 263 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; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 337 AA 
Protein Sequence
MAAGAAEAGE AAVAVVEVGS AQQFEELLRL KTKSLLVVHF WAPWAPQCVQ MNDVMAELAK 60
EHPHVSFVKL EAEAVPEVSE KYEISSVPTF LFFKNSQKVD RLDGAHAPEL TKKVQRHVSS 120
GAFPPSTNEH LKEDLSLRLK KLTHAAPCML FMKGTPQEPR CGFSKQMVEI LHKHNIQFSS 180
FDIFSDEEVR QGLKTYSNWP TYPQLYVSGE LIGGLDIIKE LEASEELDTI CPKAPKLEER 240
LKVLTNKASV MLFMKGNKQE AKCGFSKQIL EILNSTGVEY ETFDILEDEE VRQGLKTFSN 300
WPTYPQLYVR GDLVGGLDIV KELKDNGELL PILKGEN 337 
Gene Ontology
 GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
 GO:0030018; C:Z disc; IDA:UniProtKB.
 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; IMP:UniProtKB.
 GO:0002026; P:regulation of the force of heart contraction; IMP: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