CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001766
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Superoxide dismutase [Cu-Zn] 
Protein Synonyms/Alias
  
Gene Name
 SOD1 
Gene Synonyms/Alias
 YJR104C; J1968 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
19AGVSGVVKFEQASESsumoylation[1]
69GPHFNPFKKTHGAPTsumoylation[1]
89VGDMGNVKTDENGVAacetylation[2]
97TDENGVAKGSFKDSLacetylation[2]
101GVAKGSFKDSLIKLIacetylation[2]
101GVAKGSFKDSLIKLIubiquitination[3]
106SFKDSLIKLIGPTSVacetylation[2]
129AGQDDLGKGDTEESLacetylation[2]
129AGQDDLGKGDTEESLubiquitination[3]
137GDTEESLKTGNAGPRacetylation[2]
137GDTEESLKTGNAGPRubiquitination[3, 4]
Reference
 [1] Identification of sumoylated proteins by systematic immunoprecipitation of the budding yeast proteome.
 Wykoff DD, O'Shea EK.
 Mol Cell Proteomics. 2005 Jan;4(1):73-83. [PMID: 15596868]
 [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [3] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [4] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047
Functional Description
 Destroys radicals which are normally produced within the cells and which are toxic to biological systems. 
Sequence Annotation
 METAL 43 43 Zinc 2; shared with CCS1; in apo form.
 METAL 47 47 Copper; catalytic.
 METAL 49 49 Copper; catalytic.
 METAL 64 64 Copper; catalytic.
 METAL 64 64 Zinc 1; structural.
 METAL 72 72 Zinc 1; structural.
 METAL 81 81 Zinc 1; structural.
 METAL 84 84 Zinc 1; structural.
 METAL 121 121 Copper; catalytic.
 BINDING 144 144 Substrate (Probable).
 MOD_RES 26 26 Phosphoserine.
 MOD_RES 39 39 Phosphoserine.
 MOD_RES 99 99 Phosphoserine.
 MOD_RES 117 117 Phosphoserine.
 MOD_RES 132 132 Phosphothreonine.
 MOD_RES 138 138 Phosphothreonine.
 DISULFID 58 147 Alternate; alternate.
 DISULFID 58 58 Interchain (with C-229 in CCS1);
 CROSSLNK 19 19 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 70 70 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Antioxidant; Complete proteome; Copper; Cytoplasm; Direct protein sequencing; Disulfide bond; Isopeptide bond; Metal-binding; Mitochondrion; Oxidoreductase; Phosphoprotein; Reference proteome; Ubl conjugation; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 154 AA 
Protein Sequence
MVQAVAVLKG DAGVSGVVKF EQASESEPTT VSYEIAGNSP NAERGFHIHE FGDATNGCVS 60
AGPHFNPFKK THGAPTDEVR HVGDMGNVKT DENGVAKGSF KDSLIKLIGP TSVVGRSVVI 120
HAGQDDLGKG DTEESLKTGN AGPRPACGVI GLTN 154 
Gene Ontology
 GO:0005829; C:cytosol; IDA:SGD.
 GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0005507; F:copper ion binding; IBA:RefGenome.
 GO:0004784; F:superoxide dismutase activity; IDA:SGD.
 GO:0008270; F:zinc ion binding; IBA:RefGenome.
 GO:0001320; P:age-dependent response to reactive oxygen species involved in chronological cell aging; IMP:SGD.
 GO:0006878; P:cellular copper ion homeostasis; IGI:SGD.
 GO:0006882; P:cellular zinc ion homeostasis; IMP:SGD.
 GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
 GO:1901856; P:negative regulation of cellular respiration; IMP:SGD.
 GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IMP:SGD.
 GO:0050821; P:protein stabilization; IMP:SGD.
 GO:0019430; P:removal of superoxide radicals; IBA:RefGenome. 
Interpro
 IPR024134; SOD_Cu/Zn_/chaperones.
 IPR018152; SOD_Cu/Zn_BS.
 IPR001424; SOD_Cu_Zn_dom. 
Pfam
 PF00080; Sod_Cu 
SMART
  
PROSITE
 PS00087; SOD_CU_ZN_1
 PS00332; SOD_CU_ZN_2 
PRINTS
 PR00068; CUZNDISMTASE.